|
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: 1388.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 419 QVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 499 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFS 578
Cdd:cd14917 401 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 579 LIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL 658
Cdd:cd14917 481 LIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 659 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 738
Cdd:cd14917 561 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 119586555 739 RKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 1353.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAVIAAIGDrSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSK-KKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 419 QVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 499 EEYKKEGIEWTFIDFGMDLQACIDLIEKP-MGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRniKGKPEAHF 577
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 578 SLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADApieKGKGKAKKGSSFQTVSALHRENLNK 657
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGG---GGGKKKKKGGSFRTVSQLHKEQLNK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 658 LMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFiD 737
Cdd:cd01377 555 LMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD-D 633
|
650 660
....*....|....*....|....*....
gi 119586555 738 SRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 1312.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14913 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 419 QVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 499 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFS 578
Cdd:cd14913 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 579 LIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL 658
Cdd:cd14913 481 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 659 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 738
Cdd:cd14913 561 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 119586555 739 RKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 1246.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQS-PGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPnANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFD 337
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 338 VLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 417
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 418 QQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 497
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 498 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHF 577
Cdd:cd14916 401 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 578 SLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIE-KGKGKAKKGSSFQTVSALHRENLN 656
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSgKGKGGKKKGSSFQTVSALHRENLN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 657 KLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 736
Cdd:cd14916 561 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 640
|
650 660 670
....*....|....*....|....*....|
gi 119586555 737 DSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 1229.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVIQYFAVIAAIGDR-SKKDQSPGK---GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 255
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDGpGKKAQFLATktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 256 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNA 335
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 336 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 415
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 416 NVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 496 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPR-NIKGKPE 574
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRpDKKRKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 575 AHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADA---PIEKGKGKAKKGSSFQTVSALH 651
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDStedPKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 652 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 731
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 119586555 732 EGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 1155.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAVIAAIGDRsKKDQSPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDK-KKEQQPGKmqGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd14923 240 DILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 417 VQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 497 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAH 576
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 577 FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIE--KGKGKAKKGSSFQTVSALHREN 654
Cdd:cd14923 480 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSggSKKGGKKKGSSFQTVSAVFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 655 LNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQ 734
Cdd:cd14923 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 119586555 735 FIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 1152.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14918 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14918 241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 419 QVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 499 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFS 578
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 579 LIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL 658
Cdd:cd14918 481 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 659 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 738
Cdd:cd14918 561 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 119586555 739 RKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14918 641 KKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| 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: 1129.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 417 VQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 497 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAH 576
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 577 FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGAD---APIEKGKGKAKKGSSFQTVSALHRE 653
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEgasAGGGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 654 NLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEG 733
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 119586555 734 QFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| 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: 1127.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 417 VQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 497 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAH 576
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 577 FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPI-EKGKGKAKKGSSFQTVSALHRENL 655
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEgGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 656 NKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 735
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 119586555 736 IDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 1127.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 417 VQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 497 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAH 576
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 577 FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAP-IEKGKGKAKKGSSFQTVSALHRENL 655
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEgGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 656 NKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 735
Cdd:cd14915 561 NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 119586555 736 IDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14915 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| 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: 1083.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 87 IEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 167 TDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKkdqspgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGK 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN------VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 247 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITnNPYDYAFISQ-GETTVASIDD 325
Cdd:pfam00063 155 YIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQsGCYTIDGIDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 326 AEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVK 405
Cdd:pfam00063 234 SEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 406 VGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEK 484
Cdd:pfam00063 314 TGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 485 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSANF 563
Cdd:pfam00063 394 LQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 564 QKPRNIKgkpEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAK---- 639
Cdd:pfam00063 472 QKPRLQG---ETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTpkrt 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 640 KGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 719
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 119586555 720 QRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 1076.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKdqspgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-----LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKpELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14929 156 SSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14929 235 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 419 QVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd14929 315 QVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 499 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFS 578
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHFE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 579 LIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL 658
Cdd:cd14929 475 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQFGEKKRKKGASFQTVASLHKENLNKL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 659 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 738
Cdd:cd14929 555 MTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSS 634
|
650 660
....*....|....*....|....*...
gi 119586555 739 RKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 1029.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 80 NPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISD 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 160 NAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAigdrskkdQSPGKGTLEDQIIQANPALEAFGNAKTVRND 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG--------SNTEVGSVEDQILESNPILEAFGNAKTLRNN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 240 NSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNnPYDYAFISQGET- 318
Cdd:smart00242 153 NSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGGCl 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 319 TVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQA-EPDGTEEADKSAYLMGLNSADLLK 397
Cdd:smart00242 232 TVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 398 GLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLC 477
Cdd:smart00242 312 ALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 478 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLfDNH 556
Cdd:smart00242 392 INYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKL-NQH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 557 LGKSANFQKPRNikgKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGadapiekgkg 636
Cdd:smart00242 470 HKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVS---------- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 637 KAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 716
Cdd:smart00242 537 NAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFD 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119586555 717 DFRQRYRILNPAAIPEGQFiDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRD 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: 1017.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAVIAAigDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGA--SKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14909 159 AGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 419 QVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd14909 319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 499 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIK-GKPEAHF 577
Cdd:cd14909 399 EEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAAHF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 578 SLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADA-PIEKGKGKAKKGSSFQTVSALHRENLN 656
Cdd:cd14909 479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGgGEQAKGGRGKKGGGFATVSSAYKEQLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 657 KLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQfi 736
Cdd:cd14909 559 SLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE-- 636
|
650 660 670
....*....|....*....|....*....|
gi 119586555 737 DSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 1012.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVIQYFAVIAAIGdrskKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTG----KQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVL 339
Cdd:cd14934 158 GADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 340 GFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQ 419
Cdd:cd14934 238 GFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 420 VIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 499
Cdd:cd14934 318 CNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 500 EYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGK-PEAHFS 578
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAHFE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 579 LIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADApiekgKGKAKKGSSFQTVSALHRENLNKL 658
Cdd:cd14934 478 LVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG-----SKKQKRGSSFMTVSNFYREQLNKL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 659 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDS 738
Cdd:cd14934 553 MTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVDN 631
|
650 660
....*....|....*....|....*...
gi 119586555 739 RKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14934 632 KKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
37-1433 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 858.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 37 VFVPDDKQEFVKAKIVSRE--GGKVTAE--TEYGKTVTVKEDQVMQ--QNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYG 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAfnKGKVTEEgkKEDGESVSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 111 SWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKR 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 191 VIQYFAVIAAIgdrskkdQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEK 270
Cdd:COG5022 172 IMQYLASVTSS-------STVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 271 SRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNnPYDYAFISQGE-TTVASIDDAEELMATDNAFDVLGFTSEEKNSM 349
Cdd:COG5022 245 SRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQN-PKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEEQDQI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 350 YKLTGAIMHFGNMKFKlKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAK 429
Cdd:COG5022 324 FKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 430 AVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWT 509
Cdd:COG5022 403 ALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWS 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 510 FIDFgMDLQACIDLIEK--PMGIMSILEEECMFPKATDMTFKAKLFDN-HLGKSANFQKPRNIKGKpeahFSLIHYAGIV 586
Cdd:COG5022 483 FIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVKHYAGDV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 587 DYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADapiekgkgkakKGSSFQTVSALHRENLNKLMTNLRSTH 666
Cdd:COG5022 558 EYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-----------SKGRFPTLGSRFKESLNSLMSTLNSTQ 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 667 PHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI---DSRKGAE 743
Cdd:COG5022 627 PHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDTKNAVK 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 744 KLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQSRGVLARMEYKKLLERRDSLLVIQWNIRAFMG 823
Cdd:COG5022 707 SILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRL 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 824 VKNWPWMKLYFKIKPLLKSAEREKEMASMKEEFTRLKEALEK----SEARRKELEEKMVSLLQE---------------K 884
Cdd:COG5022 787 VDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKRekklRETEEVEFSLKAEVLIQKfgrslkakkrfsllkK 866
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 885 NDLQLQVQAEQDNL--------ADAEER----------------------CDQLIKNKIQLE--AKVKEMNE--RLEDEE 930
Cdd:COG5022 867 ETIYLQSAQRVELAerqlqelkIDVKSIsslklvnleleseiielkkslsSDLIENLEFKTEliARLKKLLNniDLEEGP 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 931 EMNAELTAKKRKLEDECSELKRDIDDLELTLakveKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQ----- 1005
Cdd:COG5022 947 SIEYVKLPELNKLHEVESKLKETSEEYEDLL----KKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQlkelp 1022
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1006 -ALDDLQAEEDKVNTLTKAKvKLEQQVDDLEGSLEQEKK------VRMDLERAKRKLEGDLKLTQESIMDLEN-----DK 1073
Cdd:COG5022 1023 vEVAELQSASKIISSESTEL-SILKPLQKLKGLLLLENNqlqaryKALKLRRENSLLDDKQLYQLESTENLLKtinvkDL 1101
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1074 QQLDERLKKKDFELNAL------NARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEIS 1147
Cdd:COG5022 1102 EVTNRNLVKPANVLQFIvaqmikLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKR 1181
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1148 ER----LEEAGGATSVQIEMnKKREAEFqKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSE 1223
Cdd:COG5022 1182 LYqsalYDEKSKLSSSEVND-LKNELIA-LFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTPASMSNE 1259
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1224 fklELDDVTSNMEQIIKAKAANLEKMCRTLEDQMNEHrskaeetqrSVNDLTSQRAKLQTENGELSRQLDEKEALISQLT 1303
Cdd:COG5022 1260 ---KLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYI---------NVGLFNALRTKASSLRWKSATEVNYNSEELDDWC 1327
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1304 RgkltyTQQLEDLKRQLE---EEVKAKNALAHALQSARHDCDLLREQYEEETEA-KAELQRVLSKANSEvAQWRTKYETD 1379
Cdd:COG5022 1328 R-----EFEISDVDEELEeliQAVKVLQLLKDDLNKLDELLDACYSLNPAEIQNlKSRYDPADKENNLP-KEILKKIEAL 1401
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*.
gi 119586555 1380 AIQRTEELE-EAKKKLAQRLQE-AEEAVEAVNAKCSSLEKTKhRLQNEIEDLMVDV 1433
Cdd:COG5022 1402 LIKQELQLSlEGKDETEVHLSEiFSEEKSLISLDRNSIYKEE-VLSSLSALLTKEK 1456
|
|
| 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: 845.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKR-SEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 178 GESGAGKTVNTKRVIQYFAVIAAigdRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSG---SGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLIT---NNPYDYAFISQGE-TTVASIDDAEELMATD 333
Cdd:cd00124 158 LVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLElllSYYYLNDYLNSSGcDRIDGVDDAEEFQELL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 334 NAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREE--QAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 411
Cdd:cd00124 238 DALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 412 TKGQNVQQVIYATGALAKAVYERMFNWMVTRINATL--ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 489
Cdd:cd00124 318 TKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 490 NHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRn 568
Cdd:cd00124 398 NQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 569 ikgKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSlkllstlfanyagadapiekgkgkakkgssfqtvs 648
Cdd:cd00124 476 ---KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS----------------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 649 aLHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 728
Cdd:cd00124 518 -QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPG 596
|
650 660 670
....*....|....*....|....*....|....*...
gi 119586555 729 AiPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd00124 597 A-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| 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: 807.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVIQYFAVIAAigDRSKKDQSPGK---------GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 250
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAA--SKPKGSGAVPHpavnpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 251 HFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGETTVASIDDAEELM 330
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAEFQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 331 ATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTEeADKSAYLMGLNSADLLKGLCHPRVKVGNE 409
Cdd:cd14911 239 ATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNTV-AQKIAHLLGLSVTDMTRAFLTPRIKVGRD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 410 YVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 488
Cdd:cd14911 318 FVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 489 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLgksanfQKPRN 568
Cdd:cd14911 398 FNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 569 IKG--KPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANY----AGADAPIEKGKGKAKKGS 642
Cdd:cd14911 472 MKTdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAeivgMAQQALTDTQFGARTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 643 SFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 722
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 119586555 723 RILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 772.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE--LERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 417
Cdd:cd14920 238 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 418 QQVIYATGALAKAVYERMFNWMVTRINATLETKQpRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd14920 317 EQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 496 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFdNHLGKSANFQKPRNIKGk 572
Cdd:cd14920 396 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKD- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 573 pEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFAN---YAGAD----APIEKGKGKAKKGSS-F 644
Cdd:cd14920 474 -KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrIVGLDqvtgMTETAFGSAYKTKKGmF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 645 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 724
Cdd:cd14920 553 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 119586555 725 LNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 721.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQSP---GKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVAS-SFKTKKDQSSialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYS-KYRFLSNGNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 415
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 416 NVQQVIYATGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 494
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 495 VLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFdNHLGKSANFQKPRNIKG 571
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPKKLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 572 kpEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANY---AGADA----PIEKGKGKAKKGSSF 644
Cdd:cd14932 478 --DADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdriVGLDKvagmGESLHGAFKTRKGMF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 645 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 724
Cdd:cd14932 556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 119586555 725 LNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 698.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYG-SWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 178 GESGAGKTVNTKRVIQYFAVIAaiGDRSKKDQspgkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVG--GSSSGETQ------VEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNK-KPELLDMLLITNNpyDYAFISQGE-TTVASIDDAEELMATDNA 335
Cdd:cd01380 153 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHLGSAE--DFFYTNQGGsPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 336 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 415
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 416 NVQQVIYATGALAKAVYERMFNWMVTRINATLETKQP--RQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 493
Cdd:cd01380 311 TLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 494 FVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGK-SANFQKPRNIKGK 572
Cdd:cd01380 391 FKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 573 peahFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLlstlfanyagadapiekgkgkakkgssfQTVSALHR 652
Cdd:cd01380 470 ----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK----------------------------KTVGSQFR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 653 ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAipE 732
Cdd:cd01380 518 DSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK--E 595
|
650 660 670
....*....|....*....|....*....|....
gi 119586555 733 GQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 698.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQSPgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVAS-SHKGKKDTSI-TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVASIDDAEELMATDNAFDVL 339
Cdd:cd14921 160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN-NYTFLSNGFVPIPAAQDDEMFQETLEAMSIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 340 GFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14921 239 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 419 QVIYATGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 497
Cdd:cd14921 318 QADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 498 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRNIKGKPE 574
Cdd:cd14921 398 QEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 575 ahFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANY---AGADAPIEKGKGKAKKGSS-----FQT 646
Cdd:cd14921 477 --FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdriVGLDQMAKMTESSLPSASKtkkgmFRT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 647 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 726
Cdd:cd14921 555 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 119586555 727 PAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQspgkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVAS-SHKSKKDQ----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItnNPYD-YAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14919 157 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 417
Cdd:cd14919 235 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 418 QQVIYATGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14919 314 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 497 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRNIKGKp 573
Cdd:cd14919 394 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 574 eAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANY---AGAD-----APIEKGKGKAKKGSSFQ 645
Cdd:cd14919 472 -ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriIGLDqvagmSETALPGAFKTRKGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 646 TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 725
Cdd:cd14919 551 TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 119586555 726 NPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 680.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQSP---GKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVAS-SHKTKKDQNSlalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYN-NYRFLSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 417 VQQVIYATGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd15896 320 QEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 496 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRNIKGk 572
Cdd:cd15896 400 LEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPKKLKD- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 573 pEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANY---AGADAPI---EKGKGKAKKGSSFQT 646
Cdd:cd15896 478 -EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVdriVGLDKVSgmsEMPGAFKTRKGMFRT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 647 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 726
Cdd:cd15896 557 VGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 636
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 119586555 727 PAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 673.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE--LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYdYAFISQGETTVASiDDAEELMATDNAFDVL 339
Cdd:cd14930 160 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 340 GFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 419 QVIYATGALAKAVYERMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14930 317 QADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 497 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRNIKGkp 573
Cdd:cd14930 396 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLRD-- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 574 EAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAG----------ADAPiekgKGKAKKGSS 643
Cdd:cd14930 473 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqvsslGDGP----PGGRPRRGM 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 644 FQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 723
Cdd:cd14930 549 FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 119586555 724 ILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14930 629 ILTPNAIPKG-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: 664.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVIQYFAVIAaigdrskKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVS-------GGSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVL 339
Cdd:cd01378 155 GGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 340 GFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDgTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEY---VTKGQN 416
Cdd:cd01378 235 GFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 417 VQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQ-YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHhmFV 495
Cdd:cd01378 314 VEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--LT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 496 L--EQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFP-KATDMTFKAKLfDNHLGKSANFQKPRNIKG 571
Cdd:cd01378 392 LkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 572 KPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADA---PIekgkgkakkgssfqTVS 648
Cdd:cd01378 470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSkkrPP--------------TAG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 649 ALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 728
Cdd:cd01378 536 TKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPK 615
|
650 660 670
....*....|....*....|....*....|....*...
gi 119586555 729 AIPEGQFIDsRKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd01378 616 TWPAWDGTW-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: 650.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRgkKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYfavIAAIGDrskkdqspGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd01383 79 ESGAGKTETAKIAMQY---LAALGG--------GSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNnPYDYAFISQGET-TVASIDDAEELMATDNAFD 337
Cdd:cd01383 148 CGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNClTIDGVDDAKKFHELKEALD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 338 VLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 417
Cdd:cd01383 227 TVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 418 QQVIYATGALAKAVYERMFNWMVTRINATLET-KQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd01383 307 QQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 497 EQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLfDNHLGKSANFqkprniKGKPEA 575
Cdd:cd01383 387 EQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGERGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 576 HFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENL 655
Cdd:cd01383 459 AFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQKQSVATKFKGQL 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 656 NKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 735
Cdd:cd01383 539 FKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQD 618
|
650 660 670
....*....|....*....|....*....|.
gi 119586555 736 IDSRKGAekLLSSLDIDHNQYKFGHTKVFFK 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: 640.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVIQYFAVIaaigdrskkdqSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd01381 82 SGAGKTESTKLILQYLAAI-----------SGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITnNPYDYAFISQGETTVAS-IDDAEELMATDNAFDV 338
Cdd:cd01381 151 GAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-DASDYYYLTQGNCLTCEgRDDAAEFADIRSAMKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQRE--EQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd01381 230 LMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 417 VQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYF---IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 493
Cdd:cd01381 310 AEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 494 FVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRNikgK 572
Cdd:cd01381 390 FKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKPKS---D 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 573 PEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADApiekgkgkaKKGSSFQTVSALHR 652
Cdd:cd01381 465 LNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGS---------ETRKKSPTLSSQFR 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 653 ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPaAIPE 732
Cdd:cd01381 536 KSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP-GIPP 614
|
650 660 670
....*....|....*....|....*....|....
gi 119586555 733 GQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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: 619.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVIQYfavIAAIGDRSKKdqspgkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14883 82 SGAGKTETTKLILQY---LCAVTNNHSW--------VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKK--PELLDmLLITNNPYDYAFISQ-GETTVASIDDAEELMATDNAF 336
Cdd:cd14883 151 GAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKE-KLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRLAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 415
Cdd:cd14883 230 NVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 416 NVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd14883 310 KVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 496 LEQEEYKKEGIEWTFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRNIKGKPE 574
Cdd:cd14883 390 LEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPDRRRWKTE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 575 ahFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLF-----ANYAGADAPIEKGKGKAKKGSSFQTVSA 649
Cdd:cd14883 468 --FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtypdlLALTGLSISLGGDTTSRGTSKGKPTVGD 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 650 LHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAA 729
Cdd:cd14883 546 TFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRA 625
|
650 660 670
....*....|....*....|....*....|....*...
gi 119586555 730 IPEGQfiDSRKGAEK-LLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14883 626 RSADH--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: 585.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 178 GESGAGKTVNTKRVIQYFAviaaigDRSKKDQSPGKgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLA------YMGGRAVTEGR-SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGET-TVASIDDAEELMATDNAF 336
Cdd:cd01384 154 ISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKL-KDPKQFHYLNQSKCfELDGVDDAEEYRATRRAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKlKQREEQAEPDGTEEADKS----AYLMGLNSADLLKGLCHPRVKVGNEYVT 412
Cdd:cd01384 233 DVVGISEEEQDAIFRVVAAILHLGNIEFS-KGEEDDSSVPKDEKSEFHlkaaAELLMCDEKALEDALCKRVIVTPDGIIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 413 KGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 492
Cdd:cd01384 312 KPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 493 MFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNhLGKSANFQKPRnikg 571
Cdd:cd01384 392 VFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPK---- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 572 KPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFAnyagadapiEKGKGKAKKGSSFQTVSALH 651
Cdd:cd01384 466 LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFP---------PLPREGTSSSSKFSSIGSRF 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 652 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIp 731
Cdd:cd01384 537 KQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVL- 615
|
650 660 670
....*....|....*....|....*....|....*
gi 119586555 732 eGQFIDSRKGAEKLLSSLDIdhNQYKFGHTKVFFK 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 |
1.84e-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: 545.14 E-value: 1.84e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAVIAAigdrskkdqspGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAG-----------STNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLlitNNPYDYAFISQGET-TVASIDDAEELMATDNAFD 337
Cdd:cd14872 150 CGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW---GSSAAYGYLSLSGCiEVEGVDDVADFEEVVLAME 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 338 VLGFTSEEKNSMYKLTGAIMHFGNMKF------KLKQREEQAEPDGTEEAdksAYLMGLNSADLLKGLCHPRVKVgneyv 411
Cdd:cd14872 227 QLGFDDADINNVMSLIAAILKLGNIEFasgggkSLVSGSTVANRDVLKEV---ATLLGVDAATLEEALTSRLMEI----- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 412 tKGQNV-------QQVIYATGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 483
Cdd:cd14872 299 -KGCDPtripltpAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 484 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSan 562
Cdd:cd14872 378 KLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS-- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 563 FQKPRNIKGKPEaHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFanyagadAPIEkgkgkAKKGS 642
Cdd:cd14872 455 TFVYAEVRTSRT-EFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF-------PPSE-----GDQKT 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 643 SFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 722
Cdd:cd14872 522 SKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRY 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 119586555 723 RILnPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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 |
2.32e-172 |
|
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: 540.13 E-value: 2.32e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 178 GESGAGKTVNTKRVIQYFAVIAaigdrskkdqspgkGTLED----QIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 253
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA--------------GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 254 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDmLLITNNPYDYafisQGETTVASID---DAEELM 330
Cdd:cd14903 147 KNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERL-FLDSANECAY----TGANKTIKIEgmsDRKHFA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 331 ATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE--PDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGN 408
Cdd:cd14903 222 RTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 409 EYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 488
Cdd:cd14903 302 DVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 489 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRN 568
Cdd:cd14903 382 FTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRT 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 569 IKgkpeAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGS-----S 643
Cdd:cd14903 461 SR----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRrggalT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 644 FQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 723
Cdd:cd14903 537 TTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFW 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 119586555 724 ILNPAAipEGQFIDSRKGAEKLLSSLDIDH-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 ... |
845-1924 |
3.73e-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: 554.40 E-value: 3.73e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 845 REKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNE 924
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 925 RLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQ 1004
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1005 QALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKD 1084
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1085 FELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMN 1164
Cdd:pfam01576 243 EELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1165 KKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKaA 1244
Cdd:pfam01576 323 SKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK-Q 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1245 NLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEV 1324
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEET 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1325 KAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQEAEEA 1404
Cdd:pfam01576 482 RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1405 VEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFK 1484
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1485 LKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQL 1564
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1565 EFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQV 1644
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1645 KSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSL 1724
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1725 INQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQI 1804
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1805 ALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAE 1884
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|
gi 119586555 1885 EAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1924
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
102-766 |
9.26e-170 |
|
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: 532.59 E-value: 9.26e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 102 LYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 181 GAGKTVNTKRVIQYFAVIAAIGDrskkdqspgkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 260
Cdd:cd01382 84 GAGKTESTKYILRYLTESWGSGA----------GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 261 ADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLitnnpydyafisqgetTVASIDDAEELMATDNAFDVLG 340
Cdd:cd01382 154 GFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 341 FTSEEKNSMYKLTGAIMHFGNMKFklkqrEEQAEPDG-----TEEADKS----AYLMGLNSADLLKGLCHpRVKVGNEYV 411
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSGggcnvKPKSEQSleyaAELLGLDQDELRVSLTT-RVMQTTRGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 412 TKGQ------NVQQVIYATGALAKAVYERMFNWMVTRINATLETKQpRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 485
Cdd:cd01382 292 AKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 486 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNHLgKSANFQ 564
Cdd:cd01382 371 QQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-NHFRLS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 565 KPRniKGKPEAH--------FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADApiekGKG 636
Cdd:cd01382 449 IPR--KSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK----DSK 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 637 KAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 716
Cdd:cd01382 523 QKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFH 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 119586555 717 DFRQRYRILNPAAIPEgqfIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd01382 603 DLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
100-766 |
3.90e-168 |
|
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: 528.55 E-value: 3.90e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVIQYFAVIAaigdrskkdQSPGKGTLEdQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGKLA 259
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVN---------QRRNNLVTE-QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDM--LLitnNPYDYAFISQGETT-VASIDDAEELMATDNAF 336
Cdd:cd01387 151 GAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKygLQ---EAEKYFYLNQGGNCeIAGKSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQRE---EQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 413
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 414 GQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 493
Cdd:cd01387 308 PLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 494 FVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRniKGK 572
Cdd:cd01387 388 FKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR--MPL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 573 PEahFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYagadAPIEKGKGKAKKGSSF-------Q 645
Cdd:cd01387 464 PE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH----RAQTDKAPPRLGKGRFvtmkprtP 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 646 TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 725
Cdd:cd01387 538 TVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 119586555 726 NPAAIPEGQFIDSRkgaEKLLSSLD--IDHNQYKFGHTKVFFK 766
Cdd:cd01387 618 VALKLPRPAPGDMC---VSLLSRLCtvTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
100-766 |
3.51e-167 |
|
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: 526.27 E-value: 3.51e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYML----TDRENQSI 174
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIqsgvLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 175 LITGESGAGKTVNTKRVIQY-------FAVIAAIGDRSKKDQSPGK-GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGK 246
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYlaritsgFAQGASGEGEAASEAIEQTlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 247 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNnPYDYAFISQGETTVASIDDA 326
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 327 EELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEA-DKSAYLMGLNSADLLKGLCHPRVK 405
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTLQSlKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 406 VGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 485
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 486 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILE--EEC--MFPKATDMTFKAKLFDNHLGKS 560
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgKVNGKPGIFItlDDCwrFKGEEANKKFVSQLHASFGRKS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 561 ANFQKPRNIKGKP---------EAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTlfanyagadapi 631
Cdd:cd14890 480 GSGGTRRGSSQHPhfvhpkfdaDKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIREV------------ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 632 ekgkgkakkgssfqTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPN 711
Cdd:cd14890 548 --------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFAL 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 119586555 712 RILYGDFRQRYRILNPAAipegqfiDSRKGAEKLLSS-LDIDHNQYKFGHTKVFFK 766
Cdd:cd14890 614 REEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKmLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
99-766 |
1.33e-165 |
|
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: 520.68 E-value: 1.33e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAVIAAIGDRskkdqspgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVLGKANNR----------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQIL----SNKKpeLLDMLLITNNPYDY-AFISQGETTVASID-DAEELMAT 332
Cdd:cd01379 151 TGARISEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKPPRYlQNDGLTVQDIVNNSgNREKFEEI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 333 DNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQ----AEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGN 408
Cdd:cd01379 229 EQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 409 EYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATL---ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 485
Cdd:cd01379 309 ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpdRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 486 QQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHlgKSANFQ 564
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYW 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 565 KPRnikgKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLStlfanyagadapiekgkgkakkgssf 644
Cdd:cd01379 466 RPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR-------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 645 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 724
Cdd:cd01379 516 QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 119586555 725 L--NPAAIPEGqfidSRKGAEKLLSSLDIDHnqYKFGHTKVFFK 766
Cdd:cd01379 596 LafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-766 |
6.60e-165 |
|
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: 520.02 E-value: 6.60e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRgKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 178 GESGAGKTVNTKRVIQYFAViAAIGDRSKKDqspgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF----- 252
Cdd:cd14888 80 GESGAGKTESTKYVMKFLAC-AGSEDIKKRS------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklks 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 253 ----GATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILS-----------------------NKKPELLDMLLI-T 304
Cdd:cd14888 153 krmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSFeP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 305 NNPYDYAFISqGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQA---EPDGTEEA 381
Cdd:cd14888 233 HLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 382 DKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVL 460
Cdd:cd14888 312 EKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 461 DIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLI-EKPMGIMSILEEECM 539
Cdd:cd14888 392 DIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECF 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 540 FPKATDMTFKAKLFDNHLGKSaNFQKprnIKGKPEAhFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLST 619
Cdd:cd14888 471 VPGGKDQGLCNKLCQKHKGHK-RFDV---VKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISN 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 620 LFANYagadapIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVL 699
Cdd:cd14888 546 LFSAY------LRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVL 619
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119586555 700 EGIRICRKGFPNRILYGDFRQRYRILNPaaiPEGQfidsrkgaekllssldIDHNQYKFGHTKVFFK 766
Cdd:cd14888 620 QAVQVSRAGYPVRLSHAEFYNDYRILLN---GEGK----------------KQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-764 |
7.80e-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: 505.86 E-value: 7.80e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAY------RGKKRSEAPPHIFSISDNAYQYMLTDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 171 --NQSILITGESGAGKTVNTKRVIQYfavIAAIGDRSKKDQSPG-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 247
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNY---LASVSSATTHGQNATeRENVRDRVLESNPILEAFGNARTNRNNNSSRFGKF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 248 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVA--SIDD 325
Cdd:cd14901 158 IRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVE-EYKYLNSSQCYDRrdGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 326 AEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAY-LMGLNSADLLKGLCHPRV 404
Cdd:cd14901 237 SVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 405 KVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQP--RQYFIGVLDIAGFEIFDFNSFEQLCINFTN 482
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 483 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNhLGKSA 561
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 562 NFQKPRNIKGKpeAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTlfanyagadapiekgkgkakkg 641
Cdd:cd14901 475 SFSVSKLQQGK--RQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS---------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 642 ssfqTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 721
Cdd:cd14901 531 ----TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHT 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 119586555 722 YRILNPAAIPEGQFIdsRKGAEKLLSSLDI------DHNQYKFGHTKVF 764
Cdd:cd14901 607 YSCLAPDGASDTWKV--NELAERLMSQLQHselnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
102-766 |
2.03e-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: 503.45 E-value: 2.03e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 102 LYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESG 181
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 182 AGKTVNTKRVIQYFAVIaaigdrSKKDQSPGkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASA 261
Cdd:cd01385 84 SGKTESTNFLLHHLTAL------SQKGYGSG---VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 262 DIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNnPYDYAFISQGET-TVASIDDAEELMATDNAFDVLG 340
Cdd:cd01385 155 VVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDCyTLEGEDEKYEFERLKQAMEMVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 341 FTSEEKNSMYKLTGAIMHFGNMKFKLK--QREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd01385 234 FLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 419 QVIYATGALAKAVYERMFNWMVTRINATLETKQ----PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 494
Cdd:cd01385 314 EAIATRDAMAKCLYSALFDWIVLRINHALLNKKdleeAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 495 VLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKlFDNHLGKSANFQKPRnikgKP 573
Cdd:cd01385 394 KLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ----VM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 574 EAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLF------------------ANYAGADA------ 629
Cdd:cd01385 468 EPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIgidpvavfrwavlraffrAMAAFREAgrrraq 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 630 -----------PIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGV 698
Cdd:cd01385 548 rtaghsltlhdRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGM 627
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119586555 699 LEGIRICRKGFPNRILYGDFRQRYRILnpaaIPEGQfIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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 |
2.18e-152 |
|
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: 485.42 E-value: 2.18e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 105 LKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRG--KKRSEAPPHIFSISDNAYQYMLTDR----ENQSILIT 177
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTPQSIVVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 178 GESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKG--TLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 255
Cdd:cd14892 87 GESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 256 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKpELLDMLLITNNPYDYAFISQGE-TTVASIDDAEELMATDN 334
Cdd:cd14892 167 GRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGNcVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 335 AFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKL--KQREEQAEPDGTEEADKSAYLMGLNSADLLKGLChPRVKVGneyvT 412
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV-TQTTST----A 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 413 KGQNVQ------QVIYATGALAKAVYERMFNWMVTRINAtlETKQ------------PRQYFIGVLDIAGFEIFDFNSFE 474
Cdd:cd14892 321 RGSVLEikltarEAKNALDALCKYLYGELFDWLISRINA--CHKQqtsgvtggaaspTFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 475 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEK-PMGIMSILEEECMFP-KATDMTFKAKL 552
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTIY 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 553 FDNHLGKSANFQKPRNikgkPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSslkllstlfanyagadapie 632
Cdd:cd14892 478 HQTHLDKHPHYAKPRF----ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS-------------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 633 kgkgkakkgSSFqtvsalhRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNR 712
Cdd:cd14892 534 ---------SKF-------RTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIR 597
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119586555 713 ILYGDFRQRYRIL-----NPAAIPEGQ--FIDSRKGAEKLLSSLdiDHNQYKFGHTKVFFK 766
Cdd:cd14892 598 RQFEEFYEKFWPLarnkaGVAASPDACdaTTARKKCEEIVARAL--ERENFQLGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
100-766 |
2.29e-151 |
|
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: 482.76 E-value: 2.29e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAVIA--AIGDRSKKDQSpgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISqqSLELSLKEKTS----CVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITnNPYDYAFISQ-GETTVASIDDAEELMATDNA 335
Cdd:cd14873 158 NIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLNQsGCVEDKTISDQESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 336 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFklkqreeqAEPDGTEEADK-----SAYLMGLNSADLLKGLCHPRVKVGNEY 410
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLRGEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 411 VTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQyFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 490
Cdd:cd14873 309 ILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 491 HHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRnik 570
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPR--- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 571 gKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADApieKGKGKAKKGSSFQTVSAL 650
Cdd:cd14873 463 -VAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNN---QDTLKCGSKHRRPTVSSQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 651 HRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP-AA 729
Cdd:cd14873 539 FKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRnLA 618
|
650 660 670
....*....|....*....|....*....|....*..
gi 119586555 730 IPEgqfiDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14873 619 LPE----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
101-766 |
2.37e-148 |
|
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: 473.79 E-value: 2.37e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKK-RSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVIQYFAVIaaigdrSKKDQSpgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKL------SPSDDS----DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGETTVASIDDAEELMATDNAFDVL 339
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELEYYRQMFHDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 340 -------GFTSEEKNSMYKLTGAIMHFGNMKFklkqrEEQAEPDGTEEADK-----SAYLMGLNSADLLKGLCHPRVKVG 407
Cdd:cd14897 232 tnimkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTIR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 408 NEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYF-----IGVLDIAGFEIFDFNSFEQLCINFTN 482
Cdd:cd14897 307 GERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLSN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 483 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLfDNHLGKSA 561
Cdd:cd14897 387 ERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 562 NFQKPrnIKGKPEahFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYagadapiekgkgkakkg 641
Cdd:cd14897 465 RYVAS--PGNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY----------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 642 ssfqtvsalHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 721
Cdd:cd14897 524 ---------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKR 594
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 119586555 722 YRILNPAAIPegqfidSRKGAE-KLLSSLDIDHNQ-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 |
1.12e-143 |
|
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: 461.33 E-value: 1.12e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 178 GESGAGKTVNTKRVIQYFAVIAAigdrSKKDQSPGKgtledqIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG----GRKDKTIAK------VIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSN-KKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14904 151 LIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFkLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd14904 231 SLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 417 VQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQY-FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd14904 310 PVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 496 LEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNH--LGKSANFQKPRNIKgkp 573
Cdd:cd14904 390 TVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 574 eAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANyagADAPIEKGKGKA-KKGSSFQTVSALHR 652
Cdd:cd14904 466 -TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGS---SEAPSETKEGKSgKGTKAPKSLGSQFK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 653 ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE 732
Cdd:cd14904 542 TSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHS 621
|
650 660 670
....*....|....*....|....*....|....*
gi 119586555 733 GqfiDSRKGAEKLLSSLDIDHN-QYKFGHTKVFFK 766
Cdd:cd14904 622 K---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
101-731 |
1.78e-141 |
|
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: 454.38 E-value: 1.78e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAY-----------RGKKRSEAPPHIFSISDNAYQYM--- 165
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 166 -LTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRF 244
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 245 GKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLdmllitnnpydyafisqgettvaSID 324
Cdd:cd14900 163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAAR-----------------------KRD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 325 DAEELMAtdnAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFK-------LKQREEQAEPDGTEEADKSAYLMGLNSADLLK 397
Cdd:cd14900 220 MYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEhdensdrLGQLKSDLAPSSIWSRDAAATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 398 GLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATL-----ETKQPRQYFIGVLDIAGFEIFDFNS 472
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 473 FEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAK 551
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLASK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 552 LFdNHLGKSANFQKPRNIKGKpeAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQksslkllstlfanYAGAdapi 631
Cdd:cd14900 456 LY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV-------------YGLQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 632 ekgkgkakkgssfqtvsalHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPN 711
Cdd:cd14900 516 -------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPI 576
|
650 660
....*....|....*....|
gi 119586555 712 RILYGDFRQRYRILNPAAIP 731
Cdd:cd14900 577 RLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-766 |
1.28e-140 |
|
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: 453.21 E-value: 1.28e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYML----TDRENQSILI 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 177 TGESGAGKTVNTKRVIqyfaviaaigdRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATG 256
Cdd:cd14889 83 SGESGAGKTESTKLLL-----------RQIMELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQI---LSNKKPELLDMLlitnNPYDYAFISQG---ETTVASIDDA-EEL 329
Cdd:cd14889 151 HVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNGagcKREVQYWKKKyDEV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 330 MatdNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREE-QAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGN 408
Cdd:cd14889 227 C---NAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 409 EYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQY---FIGVLDIAGFEIFDFNSFEQLCINFTNEKL 485
Cdd:cd14889 304 EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVelrEIGILDIFGFENFAVNRFEQACINLANEQL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 486 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDL-IEKPMGIMSILEEECMFPKATDMTFKAKLfDNHLGKSANFQ 564
Cdd:cd14889 384 QYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 565 KPRNIKGKpeahFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSF 644
Cdd:cd14889 462 KSRSKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSDN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 645 ------QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 718
Cdd:cd14889 538 fnstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEF 617
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 119586555 719 RQRYRIL-NPAAIPegqfiDSRKGAEKLLSSLDIdhNQYKFGHTKVFFK 766
Cdd:cd14889 618 AERYKILlCEPALP-----GTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
101-766 |
5.83e-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: 448.71 E-value: 5.83e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGK--------KRSEAPPHIFSISDNAYQYMLTDREN 171
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 172 QSILITGESGAGKTVNTKRVIQYFAVIAA--------IGDRSKKDQ-SPGKGTLEDQIIQANPALEAFGNAKTVRNDNSS 242
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevLTLTSSIRAtSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 243 RFGKFIRIHFG-ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNP--YDYAFISQGET- 318
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLsgDRYDYLKKSNCy 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 319 TVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQ--REEQAEPDGTEEADKSAYLMGLNSADLL 396
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 397 KGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATL--------ETKQPRQYFIGVLDIAGFEIF 468
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 469 DFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF--IDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATD 545
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 546 MTFKAKLFDNHlGKSANFQKPRNIKGKpeaHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFanYA 625
Cdd:cd14907 482 EKLLNKIKKQH-KNNSKLIFPNKINKD---TFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF--SG 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 626 GADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRIC 705
Cdd:cd14907 556 EDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVR 635
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119586555 706 RKGFPNRILYGDFRQRYRILNpaaipegqfidsrkgaekllssldidhNQYKFGHTKVFFK 766
Cdd:cd14907 636 KQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-766 |
3.02e-134 |
|
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: 434.86 E-value: 3.02e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGS--WMIYTYSGLFCVTVNPYKWLPvyTPEVvAAYRGKKRSEAPPHIFSISDNAYQYMLTDRE---NQS 173
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 174 ILITGESGAGKTVNTKRVIQY--------FAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFG 245
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFlttravggKKASGQDIEQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 246 KFIRIHFGATG-KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITnNPYDYAFISQ-GETTVASI 323
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLL-SPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 324 DDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKlKQREEQAEPDGTEEADK-----SAYLMGLNSADLLKG 398
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFD-EEDTSEGEAEIASESDKealatAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 399 LCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFD-FNSFEQLC 477
Cdd:cd14891 316 ITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 478 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNH 556
Cdd:cd14891 396 INYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 557 lGKSANFQKPRNiKGKPEAhFSLIHYAGIVDYNIIGWLQKNKDPLNETvvglyqksslklLSTLFANyagadapiekgkg 636
Cdd:cd14891 475 -KRHPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPED------------FEDLLAS------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 637 kakkgssfqtvSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 716
Cdd:cd14891 527 -----------SAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYA 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 119586555 717 DFRQRYRILNPAAI------PEGQFIdsrkgaEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14891 596 ELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-727 |
3.24e-134 |
|
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: 437.40 E-value: 3.24e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYR--------GKKRSEAPPHIFSISDNAYQYML-TD 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 169 RENQSILITGESGAGKTVNTKRVIQYFAviaAIGDRSKKDQSPGKGTLE--DQIIQANPALEAFGNAKTVRNDNSSRFGK 246
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLT---SVGRDQSSTEQEGSDAVEigKRILQTNPILESFGNAQTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 247 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNpYDYAFISQGETTVA----- 321
Cdd:cd14902 158 FIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKG-GKYELLNSYGPSFArkrav 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 322 SIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEA---DKSAYLMGLNSADLLKG 398
Cdd:cd14902 237 ADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 399 LCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRIN-------ATLETKQPRQYF--IGVLDIAGFEIFD 469
Cdd:cd14902 317 LSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSdeinyfdSAVSISDEDEELatIGILDIFGFESLN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 470 FNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLqACIDLIE-KPMGIMSILEEECMFPKATDMTF 548
Cdd:cd14902 397 RNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNA-ACLALFDdKSNGLFSLLDQECLMPKGSNQAL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 549 KAKLFDNHLgksanfqkprnikgkPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGAD 628
Cdd:cd14902 476 STKFYRYHG---------------GLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 629 APIEKGKGKAKKGSSFQT--VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICR 706
Cdd:cd14902 541 PGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIAR 620
|
650 660
....*....|....*....|.
gi 119586555 707 KGFPNRILYGDFRQRYRILNP 727
Cdd:cd14902 621 HGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-727 |
6.33e-132 |
|
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: 429.71 E-value: 6.33e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYR--GKKRS---EAP----PHIFSISDNAYQYMLTD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 169 RENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKD-QSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 247
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEgEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 248 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQIL------SNKKPELLDMLLITNN-PYDYAFISQGET-T 319
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDGITGGLQlPNEFHYTGQGGApD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 320 VASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAY---LMGLNSADLL 396
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 397 KGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATL--ETKQPRQYFIGVLDIAGFEIFDFNSFE 474
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 475 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFP-KATDMTFKAKL 552
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 553 FDNHL-------GKSANFQKPRNIKGKpeAHFSLIHYAGIVDYNI-IGWLQKNKDPLNETVVGLYQKsslkllSTLFany 624
Cdd:cd14908 480 YETYLpeknqthSENTRFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFES------GQQF--- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 625 agadapiekgkgkakkgssfqtvsalhRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRI 704
Cdd:cd14908 549 ---------------------------KAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRV 601
|
650 660
....*....|....*....|...
gi 119586555 705 CRKGFPNRILYGDFRQRYRILNP 727
Cdd:cd14908 602 ARSGYPVRLPHKDFFKRYRMLLP 624
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-766 |
4.38e-129 |
|
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: 420.34 E-value: 4.38e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYfavIAAIGDRSKKDQspgkgtlEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGKL 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQF---LSSLYQDQTEDR-------LRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGET-TVASIDDAEELMATDNAFD 337
Cdd:cd14896 150 VGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 338 VLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQRE--EQAEPDGTEEADKSAYLMGLnSADLLKGLCHPRVKVGN-EYVTKG 414
Cdd:cd14896 229 GLGLCAEELTAIWAVLAAILQLGNICFSSSEREsqEVAAVSSWAEIHTAARLLQV-PPERLEGAVTHRVTETPyGRVSRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 415 QNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYF--IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 492
Cdd:cd14896 308 LPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 493 MFVLEQEEYKKEGIEWTFIDfGMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRNikg 571
Cdd:cd14896 388 LLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL--- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 572 kPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANyagADAPIEKGKGKAKKGSSFQtvsalh 651
Cdd:cd14896 463 -PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE---AEPQYGLGQGKPTLASRFQ------ 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 652 rENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILnpAAIP 731
Cdd:cd14896 533 -QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL--GSER 609
|
650 660 670
....*....|....*....|....*....|....*
gi 119586555 732 EGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14896 610 QEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
62-819 |
1.02e-128 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 425.21 E-value: 1.02e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 62 ETEYGKTVTVKEDQVMQQNPP-KFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVA 140
Cdd:PTZ00014 72 DPPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 141 AYR-GKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAViAAIGDRSKKDQspgkgtleDQ 219
Cdd:PTZ00014 152 RYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS-SKSGNMDLKIQ--------NA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 220 IIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLD 299
Cdd:PTZ00014 223 IMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 300 MLLITNNPyDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFklKQREEQAEPDGTE 379
Cdd:PTZ00014 303 KYKLKSLE-EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEI--EGKEEGGLTDAAA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 380 EADKS-------AYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQP 452
Cdd:PTZ00014 380 ISDESlevfneaCELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGG 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 453 RQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGI-----EWTfidfgmDLQACIDLI-EK 526
Cdd:PTZ00014 460 FKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGIsteelEYT------SNESVIDLLcGK 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 527 PMGIMSILEEECMFPKATDMTFKAKLFdNHLGKSANFQKPRNIKGKpeaHFSLIHYAGIVDYNIIGWLQKNKDPLNETVV 606
Cdd:PTZ00014 534 GKSVLSILEDQCLAPGGTDEKFVSSCN-TNLKNNPKYKPAKVDSNK---NFVIKHTIGDIQYCASGFLFKNKDVLRPELV 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 607 GLYQKSSLKLLSTLFanyagADAPIEKGKGKAKKGSSFQTVsalhrENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDN 686
Cdd:PTZ00014 610 EVVKASPNPLVRDLF-----EGVEVEKGKLAKGQLIGSQFL-----NQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNS 679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 687 PLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNpAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:PTZ00014 680 SKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLK 758
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 119586555 767 AGLLGLLEEMRDERLSR---IITRIQAQSRGVLARmeyKKLLERRDSLLVIQWNIR 819
Cdd:PTZ00014 759 KDAAKELTQIQREKLAAwepLVSVLEALILKIKKK---RKVRKNIKSLVRIQAHLR 811
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
99-766 |
1.69e-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: 398.17 E-value: 1.69e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTpevVAAYRGK--KRSEAPPHIFSISDNAYQYMLT-------D 168
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 169 RENQSILITGESGAGKTVNTKRVIQYFAVIA----AIGDRSKKDQSPGkgtleDQIIQANPALEAFGNAKTVRNDNSSRF 244
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSkhttATSSSKRRRAISG-----SELLSANPILESFGNARTLRNDNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 245 GKFIRIHFG-----ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDML-LITNNPYDYAFISQGET 318
Cdd:cd14895 153 GKFVRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELqLELLSAQEFQYISGGQC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 319 TVAS--IDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGT------------------ 378
Cdd:cd14895 233 YQRNdgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAasapcrlasaspssltvq 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 379 EEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQY--- 455
Cdd:cd14895 313 QHLDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnk 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 456 --------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-K 526
Cdd:cd14895 393 aankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 527 PMGIMSILEEECMFPKATDMTFKAKLFdNHLGKSANFQKPRniKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVV 606
Cdd:cd14895 472 PSGIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 607 GLYQKSSLKLLSTLFANY-AGADAPIEKGKGKAKKGSSFQT---VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPG 682
Cdd:cd14895 549 SVLGKTSDAHLRELFEFFkASESAELSLGQPKLRRRSSVLSsvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASD 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 683 VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPegqfidSRKGAEKLLSSLDIDHNQykFGHTK 762
Cdd:cd14895 629 QFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNA------SDATASALIETLKVDHAE--LGKTR 700
|
....
gi 119586555 763 VFFK 766
Cdd:cd14895 701 VFLR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-766 |
2.88e-119 |
|
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: 392.81 E-value: 2.88e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRG-KKRSEAPPHIFSIS----DNAYQYmltdRENQS 173
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTArralENLHGV----NKSQT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 174 ILITGESGAGKTVNTKRVIQYFAViaaigdrSKKDQSPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 253
Cdd:cd14876 77 IIVSGESGAGKTEATKQIMRYFAS-------AKSGNMDLR--IQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 254 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLD--MLLITNnpyDYAFISQGETTVASIDDAEELMA 331
Cdd:cd14876 148 SEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSkyHLLGLK---EYKFLNPKCLDVPGIDDVADFEE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 332 TDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQ-----AEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKV 406
Cdd:cd14876 225 VLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 407 GNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQ 486
Cdd:cd14876 305 GGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 487 QFFNHHMFVLEQEEYKKEGI-----EWTfidfgmDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLFDNhLGKS 560
Cdd:cd14876 385 KNFIDIVFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 561 ANFQKprnIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANyagadAPIEKGKGKAKK 640
Cdd:cd14876 458 GKFKP---AKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG-----VVVEKGKIAKGS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 641 GSSFQTVSalhreNLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ 720
Cdd:cd14876 530 LIGSQFLK-----QLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLY 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 119586555 721 RYRILNPaAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14876 605 QFKFLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
101-764 |
6.16e-112 |
|
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: 371.88 E-value: 6.16e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEA-PPHIFSISDNAYQYMLTDRE--NQSILI 176
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 177 TGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAER--IEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILsnkKPELLDMLLITNNP--YDYAFISQGETTVASiDDAEelmATDN 334
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQIC---KGASADERLQWHLPegAAFSWLPNPERNLEE-DCFE---VTRE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 335 AFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQA---EPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 411
Cdd:cd14880 234 AMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 412 TKGQNVQQVIYAT--GALAKAVYERMFNWMVTRINATLETKQPR-QYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 488
Cdd:cd14880 314 VFKKPCSRAECDTrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 489 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDmtfkAKLFDNHLGKS-ANFQKP 566
Cdd:cd14880 394 FVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSS----AAQLQTRIESAlAGNPCL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 567 RNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEkgkGKAKKGSSFQT 646
Cdd:cd14880 469 GHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEE---PSGQSRAPVLT 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 647 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL- 725
Cdd:cd14880 546 VVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLr 625
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 119586555 726 --NPAAIPEGQFIDSRKGAEKLLSSldidhnqykfGHTKVF 764
Cdd:cd14880 626 rlRPHTSSGPHSPYPAKGLSEPVHC----------GRTKVF 656
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
100-723 |
4.49e-107 |
|
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: 360.18 E-value: 4.49e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYR-------GKKRSEA---PPHIFSISDNAYQYMLTD 168
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 169 RENQSILITGESGAGKTVNTKRVIQYFAV-------IAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNS 241
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAVhcgtgnnNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 242 SRFGKFIRIHF-GATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNK----KPELLDMLLITNNPYDYAFISQG 316
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 317 ETTVA--SIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKL--KQREEQAEPDGTEEA----------D 382
Cdd:cd14899 242 LCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 383 KSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQY------- 455
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 456 --------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlQACIDLIE-K 526
Cdd:cd14899 402 ddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 527 PMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVV 606
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 607 GLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSAL--------HRENLNKLMTNLRSTHPHFVRCIIPNET 678
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIaavsvgtqFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 119586555 679 KSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 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 |
2.49e-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: 356.04 E-value: 2.49e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 101 VLYNLKDRYGSWMI-YTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEA-PPHIFSISDNAY-QYMLTDRENQSILIT 177
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 178 GESGAGKTVNTKRVIQYFAVIAAIgdRSKkdqSPGKGTLEDQIIQ----ANPALEAFGNAKTVRNDNSSRFGKFIRIHF- 252
Cdd:cd14875 83 GESGSGKTENAKMLIAYLGQLSYM--HSS---NTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 253 GATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTV------ASIDDA 326
Cdd:cd14875 158 PTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 327 EELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEAdKSAYLMGLNSADLLKGLChprVKV 406
Cdd:cd14875 238 HEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL---VKS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 407 GNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLetkQPRQ-----YFIGVLDIAGFEIFDFNSFEQLCINFT 481
Cdd:cd14875 314 KTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASI---TPQGdcsgcKYIGLLDIFGFENFTRNSFEQLCINYA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 482 NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKS 560
Cdd:cd14875 391 NESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 561 ANFQKPrniKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADapiekgkgkakk 640
Cdd:cd14875 470 PYFVLP---KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLA------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 641 gSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF-R 719
Cdd:cd14875 535 -RRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFcR 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 119586555 720 QRYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHN----QYKFGHTKVFFK 766
Cdd:cd14875 614 YFYLIMPRSTASLFKQEKYSEAAKDFLAYYQRLYGwakpNYAVGKTKVFLR 664
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
101-726 |
6.59e-106 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 356.60 E-value: 6.59e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKR-SEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT-GK 257
Cdd:cd14906 83 ESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 258 LASADIETYLLEKSRVIFQL-KAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASI------------- 323
Cdd:cd14906 163 IDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsnhnn 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 324 --DDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQ---REEQAEPDGTEEADKSAYLMGLNSADLLKG 398
Cdd:cd14906 243 ktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFKQA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 399 LCHPRVKVGNE--YVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINAT-LETKQPRQ----------YFIGVLDIAGF 465
Cdd:cd14906 323 LLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKfNQNTQSNDlaggsnkknnLFIGVLDIFGF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 466 EIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKAT 544
Cdd:cd14906 403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPKGS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 545 DMTFKAKLfdNHLGKSANFQKPRNI-KGKpeahFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFan 623
Cdd:cd14906 482 EQSLLEKY--NKQYHNTNQYYQRTLaKGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLF-- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 624 yagaDAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIR 703
Cdd:cd14906 554 ----QQQITSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIK 629
|
650 660
....*....|....*....|...
gi 119586555 704 ICRKGFPNRILYGDFRQRYRILN 726
Cdd:cd14906 630 VRKMGYSYRRDFNQFFSRYKCIV 652
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
101-766 |
2.33e-103 |
|
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: 348.15 E-value: 2.33e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 181 GAGKTVNTKRVIQYFAVIAAIgdrSKKDQSPGKgtledqiIQA-NPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAGS---VGGVLSVEK-------LNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFisqGETTVASIDD----AEELMATDNA 335
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF---GIVPLQKPEDkqkaAAAFSKLQAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 336 FDVLGFTSEEKNSMYKLTGAIMHFGN---MKFKLKQREEQAEPdgtEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVT 412
Cdd:cd01386 230 MKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQST 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 413 ---------------KGQNVQQviyATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------ 471
Cdd:cd01386 307 tssgqesparsssggPKLTGVE---ALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrga 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 472 SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEK---------------PMGIMSILEE 536
Cdd:cd01386 384 TFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLDE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 537 ECMFPKATDMTFKAKLFdNHLGKSANFQKPRNIKGKPEA-HFSLIHYAGI--VDYNIIGWLQKNK-DPLNETVVGLYQKS 612
Cdd:cd01386 464 EALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQES 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 613 SlKLLSTLFANYAGADApiekgkgkakkgsSFQtvsalhrenLNKLMTNLRSTHPHFVRCIIPN------------ETKS 680
Cdd:cd01386 543 Q-KETAAVKRKSPCLQI-------------KFQ---------VDALIDTLRRTGLHFVHCLLPQhnagkderstssPAAG 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 681 PGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA----AIPEGQFIDSRKGAEKLLSSLDIDHNQY 756
Cdd:cd01386 600 DELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkkLGLNSEVADERKAVEELLEELDLEKSSY 679
|
730
....*....|
gi 119586555 757 KFGHTKVFFK 766
Cdd:cd01386 680 RIGLSQVFFR 689
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
105-766 |
4.27e-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: 4.27e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 105 LKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRS-----EAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAViaaigdrskkDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAY----------GHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQI---LSNKKPELLDMLLITNnpydYAFISQGET-TVASIDDAEELMATDN 334
Cdd:cd14886 157 KGGKITSYMLELSRIEFQSTNERNYHIFYQCikgLSPEEKKSLGFKSLES----YNFLNASKCyDAPGIDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 335 AFDVLgFTSEEKNSMYKLTGAIMHFGNMKFKLKQR---EEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 411
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 412 TKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 491
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFIN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 492 HMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKP-MGIMSILEEECMFPKATDMTFKAKLfDNHLgKSANFqkprnIK 570
Cdd:cd14886 392 QVFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF-----IP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 571 GKPEA-HFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLstlfaNYAGADAPIEKGKGKAkkgssfQTVSA 649
Cdd:cd14886 464 GKGSQcNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIV-----NKAFSDIPNEDGNMKG------KFLGS 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 650 LHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL---N 726
Cdd:cd14886 533 TFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishN 612
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 119586555 727 PAAIPEGQfiDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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 |
4.35e-96 |
|
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: 323.39 E-value: 4.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKwlPVYTPEVVAAYRgKKRSEAPPHIFSISDNAYQYMLTdRENQSILITGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVIQYFAviaaigdrskkDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgaTGKLA 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLV-----------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKIT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKpelldmLLITNNPYDYAFISQGETTVasIDDAEELMATDNAFDVL 339
Cdd:cd14898 145 GAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSAMKSL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 340 GFTSEEknSMYKLTGAIMHFGNMKFklkQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQ 419
Cdd:cd14898 217 GIANFK--SIEDCLLGILYLGSIQF---VNDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 420 VIYATGALAKAVYERMFNWMVTRINATLETKQPRQyfIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 499
Cdd:cd14898 292 ARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 500 EYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKAT--DMTFKAKLFDNHlgksanfqkprNIKGKPEAHF 577
Cdd:cd14898 370 MYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNG-----------FINTKARDKI 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 578 SLIHYAGIVDYNIIGWLQKNKdplnetvvglyQKSSLKLLSTLFANYAGadapiekgkgkakkgsSFQTVSALHRENLNK 657
Cdd:cd14898 438 KVSHYAGDVEYDLRDFLDKNR-----------EKGQLLIFKNLLINDEG----------------SKEDLVKYFKDSMNK 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 658 LMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIpegQFID 737
Cdd:cd14898 491 LLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLF---EVVD 567
|
....
gi 119586555 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 |
2.81e-95 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 323.69 E-value: 2.81e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYR---GKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 176
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 177 TGESGAGKTVNTKRVIQYFAViaaigdRSkkdqSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTC------RA----SSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 257 K-LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGE----TTVASIDDAEELMA 331
Cdd:cd14878 152 KhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHL-NNLCAHRYLNQTMredvSTAERSLNREKLAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 332 TDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 411
Cdd:cd14878 231 LKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 412 TKGQNVQQVIYATGALAKAVYERMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQ 487
Cdd:cd14878 311 IRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 488 FFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLfdNHLGKSANFQ-- 564
Cdd:cd14878 391 YINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDFFfQKPSGFLSLLDEESQMIWSVEPNLPKKL--QSLLESSNTNav 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 565 ----KPRNIKGKPEAH---FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFanyagadapiekgkgk 637
Cdd:cd14878 469 yspmKDGNGNVALKDQgtaFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF---------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 638 akkGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGD 717
Cdd:cd14878 533 ---QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSD 609
|
....*...
gi 119586555 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 |
8.08e-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: 312.74 E-value: 8.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGS--------WMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 171 NQSILITGESGAGKTVNTKRVIQYfavIAAIGDRSKKDQSPGkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTY---LAAVSDRRHGADSQG---LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 251 HFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKK-PELLDMLLITNNPYDYafisqgettvasiddaeEL 329
Cdd:cd14887 155 HFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVaAATQKSSAGEGDPEST-----------------DL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 330 MATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPD-------GTEE--ADKS--AYLMGLNS------ 392
Cdd:cd14887 218 RRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRkltsvsvGCEEtaADRShsSEVKCLSSglkvte 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 393 ------ADLLKGLCHPRVKVGNEYV------------TKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQ 454
Cdd:cd14887 298 asrkhlKTVARLLGLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 455 Y--------------FIGVLDIAGFEIF---DFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEG--IEWTFIDFGM 515
Cdd:cd14887 378 EsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCSAFPF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 516 DLQACIDLIEKP------------------------MGIMSILEEE-CMFPKATDMTFKAKLFDNHLGKSA-NFQKPRNI 569
Cdd:cd14887 458 SFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKNIiNSAKYKNI 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 570 K---GKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYqksslkllstLFANYAGADAPIEKGKGKAKKGSSFQT 646
Cdd:cd14887 538 TpalSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF----------LACSTYTRLVGSKKNSGVRAISSRRST 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 647 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 726
Cdd:cd14887 608 LSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKL 687
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 119586555 727 PAAIPEgqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 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 |
1.50e-85 |
|
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: 294.62 E-value: 1.50e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEvvaaYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 181 GAGKTVNTKRVIQYFavIAAIgdrsKKDQSPGKgTLEDqiiqANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 260
Cdd:cd14937 79 GSGKTEASKLVIKYY--LSGV----KEDNEISN-TLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 261 ADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVASIDDAEELMATDNAFDVLG 340
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 341 FTSEEKNSMYKLTGAIMhFGNMKFKL-----KQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 415
Cdd:cd14937 227 MHDMKDDLFLTLSGLLL-LGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 416 NVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd14937 306 SVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 496 LEQEEYKKEGIEWTFIDFGMDlQACIDLIEKPMGIMSILEEECMFPKATDMTFkAKLFDNHLGKSANFQKPRNIKGKpea 575
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYASTKKDINK--- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 576 HFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADApiekgkgkakkGSSFQTVSALHRENL 655
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSES-----------LGRKNLITFKYLKNL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 656 NKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRIcRKGFPNRILYGDFRQRYRILNPAAIPEGQF 735
Cdd:cd14937 530 NNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSL 608
|
650 660 670
....*....|....*....|....*....|.
gi 119586555 736 IDSRKGAEKLLSSLDIDhnQYKFGHTKVFFK 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 |
8.60e-83 |
|
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: 286.75 E-value: 8.60e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 105 LKDRYGSWMIYTY---SGLfcVTVNPYKWLPVYTPEVVAAYR-------GKKRSEAPPHIFSISDNAYQYMLTDRENQSI 174
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 175 LITGESGAGKTVNTKRVIQyfaviaAIGDRSKkdqSPGKGT-LEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 253
Cdd:cd14879 88 VFLGETGSGKSESRRLLLR------QLLRLSS---HSKKGTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 254 ATGKLASADIETYLLEKSRVIfQLKA-ERDYHIFYQILSNKKPELLDMLLItNNPYDYAFI--SQGETTVAS--IDDAEE 328
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGL-DDPSDYALLasYGCHPLPLGpgSDDAEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 329 LMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFklkqreeQAEPDGTEEA---------DKSAYLMGLNSADLLKGL 399
Cdd:cd14879 237 FQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEF-------TYDHEGGEESavvkntdvlDIVAAFLGVSPEDLETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 400 CHPRVKVGNEYVTkgqnvqqvIY--ATGA------LAKAVYERMFNWMVTRINATL-ETKQPRQYFIGVLDIAGFEIFD- 469
Cdd:cd14879 310 TYKTKLVRKELCT--------VFldPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSs 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 470 --FNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEEC-MFPKATD 545
Cdd:cd14879 382 tgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 546 MTFKAKLfDNHLGKSANFQKPRNIKGKPEAH-FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLyqksslkLLSTLFANY 624
Cdd:cd14879 461 EQMLEAL-RKRFGNHSSFIAVGNFATRSGSAsFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNL-------LRGATQLNA 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 625 AgadapiekgkgkakkgssfqtvsalhrenLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRI 704
Cdd:cd14879 533 A-----------------------------LSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAAR 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119586555 705 CRKGFPNRILYGDFRQRYrilnpaaIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFF 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 |
9.79e-75 |
|
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: 264.46 E-value: 9.79e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEA-------PPHIFSISDNAYQYMLTDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 171 NQSILITGESGAGKTVNTKRVIQYFAVIAaiGDRSKKDqspgkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQ--TDSQMTE-------RIDKLIYINNILESMSNATTIKNNNSSRCGRINLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 251 HF---------GATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGE---- 317
Cdd:cd14884 152 IFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEshqk 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 318 --------TTVASIDDAEELMATD--------NAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLkqreeqaepdgteea 381
Cdd:cd14884 232 rsvkgtlrLGSDSLDPSEEEKAKDeknfvallHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA--------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 382 dkSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINAT----------LETKQ 451
Cdd:cd14884 297 --AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNvlkckekdesDNEDI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 452 PR--QYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF--GMDLQACIDLIEKP 527
Cdd:cd14884 375 YSinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVApsYSDTLIFIAKIFRR 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 528 MGIMSILEEECMfpKATDMTFKAKLFDN----HLGK--SANFQKPRNIKGKPEAH------FSLIHYAGIVDYNIIGWLQ 595
Cdd:cd14884 455 LDDITKLKNQGQ--KKTDDHFFRYLLNNerqqQLEGkvSYGFVLNHDADGTAKKQnikkniFFIRHYAGLVTYRINNWID 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 596 KNKDPLNETVVGLYQKSSLKLLStlfanyagadapiekGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIP 675
Cdd:cd14884 533 KNSDKIETSIETLISCSSNRFLR---------------EANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLP 597
|
650 660 670
....*....|....*....|....*....|....*....
gi 119586555 676 NETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRIL 714
Cdd:cd14884 598 NAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
100-766 |
1.67e-70 |
|
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: 250.17 E-value: 1.67e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYrgkkrseappHIFSISDNAYQYMLTDREN-QSILITG 178
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 179 ESGAGKTVNTKRVIQYFAviaaigdrskkdQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14874 72 ESGSGKSYNAFQVFKYLT------------SQPKSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNpYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14874 140 GLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL-QKFFYINQGNSTENIQSDVNHFKHLEDALHV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQ----REEQAEPDGTEEADKSAYLMGLNSADLLKGLChPRVKVGNEYvtkg 414
Cdd:cd14874 219 LGFSDDHCISIYKIISTILHIGNIYFRTKRnpnvEQDVVEIGNMSEVKWVAFLLEVDFDQLVNFLL-PKSEDGTTI---- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 415 qNVQQVIYATGALAKAVYERMFNWMVTRINatLETKQPRQY-FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 493
Cdd:cd14874 294 -DLNAALDNRDSFAMLIYEELFKWVLNRIG--LHLKCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 494 FVLEQEEYKKEGIEwtfIDFGMdlQACID-------LIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSAnFQKP 566
Cdd:cd14874 371 FHDQLVDYAKDGIS---VDYKV--PNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGKA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 567 RNikgKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQT 646
Cdd:cd14874 445 RN---KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMIVSQAQFILRGAQEI 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 647 VsalhrENLNKlmtnlrsTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 726
Cdd:cd14874 522 A-----DKING-------SHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLL 589
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 119586555 727 PAAIPEGQfiDSRKGAEKLLSSLDIDH-NQYKFGHTKVFFK 766
Cdd:cd14874 590 PGDIAMCQ--NEKEIIQDILQGQGVKYeNDFKIGTEYVFLR 628
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-746 |
7.27e-70 |
|
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: 248.49 E-value: 7.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPvyTPEVVAAYRGKKRSeapPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 180 SGAGKTVNTKRVI-QYFAVIaaigdrskkdqspGKGTLED---QIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgAT 255
Cdd:cd14881 77 SGSGKTYASMLLLrQLFDVA-------------GGGPETDafkHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 256 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITN-NPYDYAFISQGETTVASIDDAEELMATDN 334
Cdd:cd14881 143 GALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGySPANLRYLSHGDTRQNEAEDAARFQAWKA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 335 AFDVLG--FTSeeknsMYKLTGAIMHFGNMKFkLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGL---CHprvkvgne 409
Cdd:cd14881 223 CLGILGipFLD-----VVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRGLttrTH-------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 410 yVTKGQNVQQVIYAT------GALAKAVYERMFNWMVTRIN------ATLETKQpRQYFIGVLDIAGFEIFDFNSFEQLC 477
Cdd:cd14881 289 -NARGQLVKSVCDANmsnmtrDALAKALYCRTVATIVRRANslkrlgSTLGTHA-TDGFIGILDMFGFEDPKPSQLEHLC 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 478 INFTNEKLQQFFNHHMFVLEQEEYKKEGIewtfidfGMDLQA-------CIDLIEK-PMGIMSILEEECMfPKATDMTFK 549
Cdd:cd14881 367 INLCAETMQHFYNTHIFKSSIESCRDEGI-------QCEVEVdyvdnvpCIDLISSlRTGLLSMLDVECS-PRGTAESYV 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 550 AKLfdnhlgKSANFQKPRNIKGKPEA--HFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLkllSTLFANYAga 627
Cdd:cd14881 439 AKI------KVQHRQNPRLFEAKPQDdrMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNC---NFGFATHT-- 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 628 dapiekgkgkakkgSSFQTvsalhreNLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRK 707
Cdd:cd14881 508 --------------QDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAG 566
|
650 660 670
....*....|....*....|....*....|....*....
gi 119586555 708 GFPNRILYGDFRQRYRILNPAAiPEGQFIDSRKGAEKLL 746
Cdd:cd14881 567 GYPHRMRFKAFNARYRLLAPFR-LLRRVEEKALEDCALI 604
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
105-718 |
1.41e-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: 236.91 E-value: 1.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 105 LKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYrgKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAG 183
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 184 KTVNTKRVIQYfaVIAAIGDRSKkdqspgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADI 263
Cdd:cd14905 85 KSENTKIIIQY--LLTTDLSRSK--------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 264 ETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITN-NPYDYafISQGET-TVASIDDAEELMATDNAFDVLGF 341
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDiNSYHY--LNQGGSiSVESIDDNRVFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 342 TSEEKNSMYKLTGAIMHFGNMKFKLKQREeqaepdgTEEADKSaylmglnsadLLKGLCH----PRVKVGNEYVT-KGQN 416
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRT----------LIESLSHnitfDSTKLENILISdRSMP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 417 VQQVIYATGALAKAVYERMFNWMVTRINATLetkQPRQY--FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 494
Cdd:cd14905 296 VNEAVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 495 VLEQEEYKKEGIEW-TFIDFgMDLQACIDLIEKpmgIMSILEEECMFPKATDMTFKAKLfdnhlgksANFQKPRNIKGKP 573
Cdd:cd14905 373 KQEQREYQTERIPWmTPISF-KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 574 EAHFSLIHYAGIVDYNIIGWLQKNKDP-------------------------LNETVVGLYQ---------KSSLKLLST 619
Cdd:cd14905 441 PNKFGIEHYFGQFYYDVRGFIIKNRDEilqrtnvlhknsitkylfsrdgvfnINATVAELNQmfdakntakKSPLSIVKV 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 620 LFA--------------NYAGADAPIEKGKGKAKKGSSFQTVSAlhrenLNKLMTNlRSTHPHFVRCIIPNETKSPGVMD 685
Cdd:cd14905 521 LLScgsnnpnnvnnpnnNSGGGGGGGNSGGGSGSGGSTYTTYSS-----TNKAINN-SNCDFHFIRCIKPNSKKTHLTFD 594
|
650 660 670
....*....|....*....|....*....|....*..
gi 119586555 686 NPLVMHQLRCNGVLEGIRICRKGFP----NRILYGDF 718
Cdd:cd14905 595 VKSVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-765 |
1.55e-65 |
|
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: 238.33 E-value: 1.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 102 LYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKR----------SEAPPHIFSISDNAYQYMLTDREN 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 172 QSILITGESGAGKTVNTKRVIQYfavIAAIGDRS--KKDQSPGKGTLE---DQIIQANPALEAFGNAKTVRNDNSSRFGK 246
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQY---LCEIGDETepRPDSEGASGVLHpigQQILHAFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 247 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKK--PELLDMLLITNNPYDYAFISQG--ETTVAS 322
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 323 ID--DAEELMATdnaFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLN-------SA 393
Cdd:cd14893 241 LDarDYRDLMSS---FSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQSCALKdpaqillAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 394 DLLKglCHPRV------------KVGNEYVT--KGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPR------ 453
Cdd:cd14893 318 KLLE--VEPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 454 ---QYFIGVLDIAGFEIFD--FNSFEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEG--IEWTFIDFGMDLQACI 521
Cdd:cd14893 396 vinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 522 DLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNH-----LGKSANFQKPRNIKGKPEAHFSLI----HYAGIVDYNII 591
Cdd:cd14893 476 QLFEdKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNeavggLSRPNMGADTTNEYLAPSKDWRLLfivqHHCGKVTYNGK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 592 GWLQKNKDPLNETVVGLYQKSSLKLLSTLFANY---AGADAPIEKGKGKAKKGSSFQTVSALHRENLN------------ 656
Cdd:cd14893 556 GLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQmaaASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynq 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 657 --KLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRilnpaaipegQ 734
Cdd:cd14893 636 adALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK----------N 705
|
730 740 750
....*....|....*....|....*....|....*
gi 119586555 735 FIDSRKGAEKLLSSLD----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 |
3.93e-62 |
|
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: 209.89 E-value: 3.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 121 FCVTVNPYKWLPVYTPEVV-AAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 119586555 200 AIGDRSKKDQ-----SPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 250
Cdd:cd01363 81 FNGINKGETEgwvylTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
101-725 |
2.04e-61 |
|
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: 223.85 E-value: 2.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 181 GAGKTVNTKRVIQYFAViaaIGDrskkdqspGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 260
Cdd:cd14882 83 YSGKTTNARLLIKHLCY---LGD--------GNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 261 ADIETYLLEKSRVIFQLKAERDYHIFYQILS--NKKPELLDMLLITNNPYDYAFISQG-------------ETTVASIDD 325
Cdd:cd14882 152 AIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 326 AEELmatdnaFDVLGFTSEEKNSMYKLTGAIMHFGNMKFklKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVK 405
Cdd:cd14882 232 FEEI------LKDLDFNEEQLETVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 406 VGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETkqPR-----QYFIGVLDIAGFEIFDFNSFEQLCINF 480
Cdd:cd14882 304 KGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVNT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 481 TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEecmfpKATDMTFKAKLFDNHLGKS 560
Cdd:cd14882 382 LNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 561 ANFQKPRNikgkpeAH-FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANyagadapiekgkgkaK 639
Cdd:cd14882 457 SQFVKKHS------AHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN---------------S 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 640 KGSSFQTVSALHR----ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILY 715
Cdd:cd14882 516 QVRNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPF 595
|
650
....*....|
gi 119586555 716 GDFRQRYRIL 725
Cdd:cd14882 596 QEFLRRYQFL 605
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-764 |
1.70e-44 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 174.25 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSE-APPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 178 GESGAGKTVNTKRVIQYFAViAAIGDRSKKDQS--------------PGKGTLEDQIIQANPALEAFGNAKTVRNDNSSR 243
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAY-QVKGSRRLPTNLndqeednihneentDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 244 FGKFIRIHFgATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYdYAFISQGETTVASI 323
Cdd:cd14938 160 FSKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIEN-YSMLNNEKGFEKFS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 324 DDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGN-------------MKFKLKQRE----------EQAEPDGTEE 380
Cdd:cd14938 238 DYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 381 ADKSAYL----MGLNSADLLKGLCHPRVkVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYF 456
Cdd:cd14938 318 NVKNLLLacklLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 457 ---IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM--GIM 531
Cdd:cd14938 397 tnyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 532 SILEEECMfPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAhFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQK 611
Cdd:cd14938 477 SLLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 612 SSLKLLSTL--FANYAGADAPIEKGKG----------KAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETK 679
Cdd:cd14938 555 SENEYMRQFcmFYNYDNSGNIVEEKRRysiqsalklfKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 680 SP-GVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPaaipegqfiDSRKGAEKLLSSLDIDHNQYKF 758
Cdd:cd14938 635 RElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMI 705
|
....*.
gi 119586555 759 GHTKVF 764
Cdd:cd14938 706 GNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1173-1931 |
4.83e-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: 137.11 E-value: 4.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1173 KMRRdlEEATLQHEATAAALrKKHADSVAELGEQIDNLQRVKQK----LEKEKSEFKLELDDVTSNMEQiIKAKAANLEK 1248
Cdd:TIGR02168 171 KERR--KETERKLERTRENL-DRLEDILNELERQLKSLERQAEKaeryKELKAELRELELALLVLRLEE-LREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1249 MCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEevkAKN 1328
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE---LEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1329 ALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRtkyetDAIQRTEELEEAKKKLAQRLQEAEEAVEAV 1408
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE-----ELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1409 NAKCSSLEKTKHRLQNEIEDLMVDVE--RSNAAAAALDKKQRNF---DKILAEWKQKYEESQSELESSQKEARSLSTELF 1483
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEelLKKLEEAELKELQAELeelEEELEELQEELERLEEALEELREELEEAEQALD 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1484 KLKN----------AYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEA---EKME------LQSA 1544
Cdd:TIGR02168 479 AAERelaqlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAalgGRLQavvvenLNAA 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1545 LEEAEASLEHEEGK--------ILRAQLEFN--QIKAEIERKLAEKDEEMEQAKR---------NHLRVVDSLQTSLDAE 1605
Cdd:TIGR02168 559 KKAIAFLKQNELGRvtflpldsIKGTEIQGNdrEILKNIEGFLGVAKDLVKFDPKlrkalsyllGGVLVVDDLDNALELA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1606 TRSRNEALRVKKkmEGDL-----------NEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAI 1674
Cdd:TIGR02168 639 KKLRPGYRIVTL--DGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1675 V-------ERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQ 1747
Cdd:TIGR02168 717 LrkeleelSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1748 ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKgGKKQLQKLEARVRELENEL 1827
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESEL 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1828 EAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFR-KVQHELDE 1906
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEE 955
|
810 820
....*....|....*....|....*
gi 119586555 1907 AEERADIAESQVNKLRAKSRDIGTK 1931
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
840-1673 |
3.99e-30 |
|
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: 130.95 E-value: 3.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 840 LKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKV 919
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 920 KEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKAL 999
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1000 QEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLEraKRKLEGDLKLTQESIMDLENDKQQLDER 1079
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1080 LKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERT---ARAKVEKLRSDLSRELEEISER------- 1149
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfseGVKALLKNQSGLSGILGVLSELisvdegy 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1150 ---LEEAGGATSVQIEMNKKREAefqkmrRDLEEATLQHEATAAAL----RKKHADSVAELGEQIDNLQRVKQ---KLEK 1219
Cdd:TIGR02168 536 eaaIEAALGGRLQAVVVENLNAA------KKAIAFLKQNELGRVTFlpldSIKGTEIQGNDREILKNIEGFLGvakDLVK 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1220 EKSEFKLELDD------VTSNMEQII-KAKAANLEKMCRTLEDQM-----------NEHRSKAEETQRSVNDLTSQRAKL 1281
Cdd:TIGR02168 610 FDPKLRKALSYllggvlVVDDLDNALeLAKKLRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEEL 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1282 QTENGELSRQLDEKEALISQLtrgkltyTQQLEDLKRQLEEEVKAKNALAHALQSArhdcdllreqyEEETEAKAELQRV 1361
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEEL-------EEELEQLRKELEELSRQISALRKDLARL-----------EAEVEQLEERIAQ 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1362 LSKANSEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLmvdversNAAAA 1441
Cdd:TIGR02168 752 LSKELTELEAEIEELE----ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-------NEEAA 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1442 ALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSG 1521
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1522 KTIHELEKVRKQLEAEKMELQSALEEAEASLEheegkilRAQLEFNQIKAeierKLAEKDE-EMEQAKRNHLRVVDSLQt 1600
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLE-------GLEVRIDNLQE----RLSEEYSlTLEEAEALENKIEDDEE- 968
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119586555 1601 sldaETRSRNEALRVKKKMEGDLNEMEIQlshanrmaaEAQKQVKSLQSLLKdtqiQLDDAVRANDDLKENIA 1673
Cdd:TIGR02168 969 ----EARRRLKRLENKIKELGPVNLAAIE---------EYEELKERYDFLTA----QKEDLTEAKETLEEAIE 1024
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
942-1872 |
9.95e-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: 126.32 E-value: 9.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 942 KLEDECSELKRDIDDLELTLAKVEkekhatenKVKNLTEEMAGLDeiIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLT 1021
Cdd:TIGR02168 190 RLEDILNELERQLKSLERQAEKAE--------RYKELKAELRELE--LALLVLRLEELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1022 KAKVKLEQQVDDLEGSLEQekkvrmdLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEdeqalg 1101
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSE-------LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE------ 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1102 sQLQKKLKELQARIeeleeeleaertarAKVEKLRSDLSRELEEISERLEEAGGatsvQIEMNKKREAEFQKMRRDLEEA 1181
Cdd:TIGR02168 327 -ELESKLDELAEEL--------------AELEEKLEELKEELESLEAELEELEA----ELEELESRLEELEEQLETLRSK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1182 TLQHEATAAALRKKhadsVAELGEQIDNLQRVKQKLEKEKSEFKLELDdvtsnmeqiikakaanlekmcrtlEDQMNEHR 1261
Cdd:TIGR02168 388 VAQLELQIASLNNE----IERLEARLERLEDRRERLQQEIEELLKKLE------------------------EAELKELQ 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1262 SKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVK----AKNALAHALQSA 1337
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegVKALLKNQSGLS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1338 RHDcDLLREQYEEETEAKAELQRVLSKANSEVAqwrTKYETDAIQRTEELEEAKK--------------KLAQRLQEAEE 1403
Cdd:TIGR02168 520 GIL-GVLSELISVDEGYEAAIEAALGGRLQAVV---VENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILK 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1404 AVEAVNAKCSSLEKTKHRLQNEIEDL-----MVD-VERSNAAAAALDKKQRNF----DKILAEWkqkyeesqseleSSQK 1473
Cdd:TIGR02168 596 NIEGFLGVAKDLVKFDPKLRKALSYLlggvlVVDdLDNALELAKKLRPGYRIVtldgDLVRPGG------------VITG 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1474 EARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLgssgktiHELEKVRKQLEAEKMELQSALEEAEASLE 1553
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL-------EELEEELEQLRKELEELSRQISALRKDLA 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1554 HEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQakrnhlrvvdslqtsLDAETRSRNEALRVKKKMEGDLNEMEIQLSHA 1633
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEER---------------LEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1634 NRMAAEAQKQvkslqslLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKlAEQELIETser 1713
Cdd:TIGR02168 802 REALDELRAE-------LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE-ELEELIEE--- 870
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1714 vqlLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNMEQTIKD 1793
Cdd:TIGR02168 871 ---LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE---LRLEGLEVRIDNLQER 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1794 L--QHRLDEAEQIALK-GGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVD 1870
Cdd:TIGR02168 945 LseEYSLTLEEAEALEnKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE 1024
|
..
gi 119586555 1871 KL 1872
Cdd:TIGR02168 1025 EI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1312-1937 |
5.31e-27 |
|
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: 120.55 E-value: 5.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1312 QLEDLKRQLEeevKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEvaqwRTKYETDAIQRTEELEEAK 1391
Cdd:TIGR02168 201 QLKSLERQAE---KAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEE----LEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1392 KK---LAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSEL 1468
Cdd:TIGR02168 274 LEvseLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1469 ESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEA 1548
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1549 EASLEHEEGKILRAQLE--------FNQIKAEIERKLAEKDEEMEQAKRNH------LRVVDSLQTSLDAETRSRNEALR 1614
Cdd:TIGR02168 434 ELKELQAELEELEEELEelqeelerLEEALEELREELEEAEQALDAAERELaqlqarLDSLERLQENLEGFSEGVKALLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1615 VKKKMEGDLN--------------EMEIQL-----------SHANRMAAEAQKQVKS------LQSLLKDTQIQLDDAVR 1663
Cdd:TIGR02168 514 NQSGLSGILGvlselisvdegyeaAIEAALggrlqavvvenLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1664 AN---------------------------------DDLKENIAI----------------------------VERRNNLL 1682
Cdd:TIGR02168 594 LKniegflgvakdlvkfdpklrkalsyllggvlvvDDLDNALELakklrpgyrivtldgdlvrpggvitggsAKTNSSIL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1683 --QAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEK---AK 1757
Cdd:TIGR02168 674 erRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqLS 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1758 KAITDA----AMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKR 1833
Cdd:TIGR02168 754 KELTELeaeiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-ALDELRAELTLLNEEAANLRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1834 NAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADI 1913
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
730 740
....*....|....*....|....
gi 119586555 1914 AESQVNKLRAKSRDIGTKRCGFTM 1937
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEV 936
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
833-1453 |
2.06e-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: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 833 YFKIKPLLKSAERE---KEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLI 909
Cdd:COG1196 215 YRELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 910 KNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEII 989
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 990 AKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDL 1069
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1070 ENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAK---------VEKLRSDLS 1140
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLaglrglagaVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1141 RELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKE 1220
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1221 KSEFKLELDDVTSNMEQIIKAKAanlekmcrtledQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALIS 1300
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALR------------RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1301 QLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAqwrtKYETDA 1380
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPE 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1381 IQRTEELEEAKKKLAQRLQE-------AEEAVEAVNAKCSSLEKTKHRLQNEIEDLM-----VDVERSNAAAAALDKKQR 1448
Cdd:COG1196 759 PPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEeaieeIDRETRERFLETFDAVNE 838
|
....*
gi 119586555 1449 NFDKI 1453
Cdd:COG1196 839 NFQEL 843
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
963-1857 |
4.86e-25 |
|
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: 114.00 E-value: 4.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 963 KVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALD--DLQAEEDKVNtLTKAKVKLEQQVDDLEGSLEQ 1040
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykELKAELRELE-LALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1041 EKKvrmdLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDeqalgsqLQKKLKELQARIEELEE 1120
Cdd:TIGR02168 248 LKE----AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR-------LEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1121 ELEAERTARAKVEKLRSDLSRELEEISERLEEAggatSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsV 1200
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEEL----KEELESLEAELEELEAELEELESRLEELEEQLETLRSK----V 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1201 AELGEQIDNLQRVKQKLEKEKSEFKLELDdvtsNMEQIIKAKAANLEkmcrtlEDQMNEHRSKAEETQRSVNDLTSQRAK 1280
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRE----RLQQEIEELLKKLE------EAELKELQAELEELEEELEELQEELER 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1281 LQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVK----AKNALAHALQSARHDcDLLREQYEEETEAKA 1356
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegVKALLKNQSGLSGIL-GVLSELISVDEGYEA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1357 ELQRVLSKANSEVAqwrTKYETDAIQRTEELEEAKK--------------KLAQRLQEAEEAVEAVNAKCSSLEKTKHRL 1422
Cdd:TIGR02168 538 AIEAALGGRLQAVV---VENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1423 QNEIEDL-----MVD-VERSNAAAAALDKKQRNF----DKILAEWkqkyeesqseleSSQKEARSLSTELFKLKNAYEES 1492
Cdd:TIGR02168 615 RKALSYLlggvlVVDdLDNALELAKKLRPGYRIVtldgDLVRPGG------------VITGGSAKTNSSILERRREIEEL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1493 LEHLETFKRENKNLQEEISDLTEQLgssgktiHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAE 1572
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKEL-------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1573 IERKLAEKDEEMEQakrnhlrvvdslqtsLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQvkslqslLK 1652
Cdd:TIGR02168 756 LTELEAEIEELEER---------------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE-------LT 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1653 DTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKlAEQELIETservqlLHSQNTSLINQKKKMD 1732
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE-ELEELIEE------LESELEALLNERASLE 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1733 ADLSQLQTEVEEAVQECRNAEEKAKkaitdaammaeelkkeqdtsahlermkknmeqtikDLQHRLDEAEQiALKGGKKQ 1812
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRS-----------------------------------ELRRELEELRE-KLAQLELR 930
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 119586555 1813 LQKLEARVRELENELEAEQKRNAESVKGM--------RKSERRIKELTYQTEE 1857
Cdd:TIGR02168 931 LEGLEVRIDNLQERLSEEYSLTLEEAEALenkieddeEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
841-1534 |
1.50e-24 |
|
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: 112.46 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVK 920
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 921 EMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQ 1000
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1001 EAHQQAldDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDER- 1079
Cdd:TIGR02168 428 KKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFs 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1080 -----LKKKDFELNALNARIED------------EQALGSQLQK----------------------KLKELQARIEELEE 1120
Cdd:TIGR02168 506 egvkaLLKNQSGLSGILGVLSElisvdegyeaaiEAALGGRLQAvvvenlnaakkaiaflkqnelgRVTFLPLDSIKGTE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1121 ELEAERTARAKVEKLRSDLSrELEEISERLEEAGG--------ATSVQIEMNKKREAEFQKM------------------ 1174
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAK-DLVKFDPKLRKALSyllggvlvVDDLDNALELAKKLRPGYRivtldgdlvrpggvitgg 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1175 RRDLEEATLQHEATAAALRKKhadsVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQI------IKAKAANLEK 1248
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEK----IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELsrqisaLRKDLARLEA 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1249 MCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKN 1328
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1329 ALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETdAIQRTEELEEAKKKLAQRLQEAEEAVEAV 1408
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-LESELEALLNERASLEEALALLRSELEEL 899
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1409 NAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKK-QRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKN 1487
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRiDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 119586555 1488 AYEE----SLEHLETFKRENK---NLQEEISDLTEQLGSSGKTIHELEKVRKQL 1534
Cdd:TIGR02168 980 KIKElgpvNLAAIEEYEELKErydFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
840-1701 |
1.54e-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: 112.47 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 840 LKSAEREKEMAsmkEEFTRLKEalEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKV 919
Cdd:TIGR02169 200 LERLRREREKA---ERYQALLK--EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 920 KEMNERLEDE-EEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 998
Cdd:TIGR02169 275 EELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 999 LQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDkqqlde 1078
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA------ 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1079 rLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERL----EEAG 1154
Cdd:TIGR02169 429 -IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseERVR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1155 GATSVQIEMNKKREAEFQKMRrDLEEATLQHEA---TAAALRKKHA----DSVAElgEQIDNLQRVKQ------KLEKEK 1221
Cdd:TIGR02169 508 GGRAVEEVLKASIQGVHGTVA-QLGSVGERYATaieVAAGNRLNNVvvedDAVAK--EAIELLKRRKAgratflPLNKMR 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1222 SEFKleldDVTSNMEQIIKAKAANLekmcRTLEDQMNEHRSKAEETQRSVNDLTSQRA-----KLQTENGELSrqldEKE 1296
Cdd:TIGR02169 585 DERR----DLSILSEDGVIGFAVDL----VEFDPKYEPAFKYVFGDTLVVEDIEAARRlmgkyRMVTLEGELF----EKS 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1297 ALIS----QLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRvLSKANSEVAQw 1372
Cdd:TIGR02169 653 GAMTggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE-IEKEIEQLEQ- 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1373 rtkYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNaaaaaLDKKQRNFDK 1452
Cdd:TIGR02169 731 ---EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR-----IPEIQAELSK 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1453 IlaewkqkyeesqselessQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRK 1532
Cdd:TIGR02169 803 L------------------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1533 QLEAEKMELQSALEEAEASLEHEEGKILRAQLEfnqiKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEA 1612
Cdd:TIGR02169 865 ELEEELEELEAALRDLESRLGDLKKERDELEAQ----LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1613 LRVKKKMEGDLNEMEIQLshanrMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEniaiverRNNLLQAELEELRAV 1692
Cdd:TIGR02169 941 GEDEEIPEEELSLEDVQA-----ELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE-------KRAKLEEERKAILER 1008
|
....*....
gi 119586555 1693 VEQTERSRK 1701
Cdd:TIGR02169 1009 IEEYEKKKR 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1311-1929 |
3.73e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.18 E-value: 3.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1311 QQLEDLKRQ-----------LEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVaqwrtkyetd 1379
Cdd:COG1196 200 RQLEPLERQaekaeryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL---------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1380 aiqrtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQ 1459
Cdd:COG1196 270 -----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1460 KYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKM 1539
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1540 ELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRsrneaLRVKKKM 1619
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-----LLLLLEA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1620 EGDlnemeiqlshanrmAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQaeleelRAVVEQTERS 1699
Cdd:COG1196 500 EAD--------------YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ------NIVVEDDEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1700 RKLAEQELIETSERVQLLHSqntSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAH 1779
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPL---DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1780 LERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVkgmRKSERRIKELTYQTEEDR 1859
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL---EEALLAEEEEERELAEAE 713
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1860 KNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSkfrKVQHELDEAEERADIAESQVNKLRAKSRDIG 1929
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLE---EEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1106-1910 |
1.25e-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: 109.39 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1106 KKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEaggatsVQIEMNKKReaEFQKMRRDLEEAtlqh 1185
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLER------LRREREKAE--RYQALLKEKREY---- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1186 EATAAALRKKHADsvaelgEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKAANLEKMCRTLEDQMNEHRSKAE 1265
Cdd:TIGR02169 224 EGYELLKEKEALE------RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1266 ETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRgkltytqQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLR 1345
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA-------EIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1346 EQYEEETEAKAELQRvlskansEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNE 1425
Cdd:TIGR02169 371 AELEEVDKEFAETRD-------ELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1426 IEDLMVDVErsnaaaaALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLknayEESLEHLETFKRENKN 1505
Cdd:TIGR02169 443 KEDKALEIK-------KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA----EAQARASEERVRGGRA 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1506 LQEEISDLTEqlGSSGkTIHELEKVRKQ------------LEAEKMELQSALEEAEASLEHEegKILRAQ-LEFNQIKAE 1572
Cdd:TIGR02169 512 VEEVLKASIQ--GVHG-TVAQLGSVGERyataievaagnrLNNVVVEDDAVAKEAIELLKRR--KAGRATfLPLNKMRDE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1573 --------------IERKLAEKDEEMEQAKRNHLR---VVDSLQT-----------SLDAE-----------TRSRNEAL 1613
Cdd:TIGR02169 587 rrdlsilsedgvigFAVDLVEFDPKYEPAFKYVFGdtlVVEDIEAarrlmgkyrmvTLEGElfeksgamtggSRAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1614 RVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVV 1693
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1694 EQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSqlQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKE 1773
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1774 QDTSAHLERMKKNMEQTIKDLQHRLDE-AEQIALKGGKK-----QLQKLEARVRELENELEAEQKRNAESVKGMRKSERR 1847
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSiEKEIENLNGKKeeleeELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119586555 1848 IKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSkFRKVQHELDEAEER 1910
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1579 |
7.07e-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: 107.08 E-value: 7.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 844 EREKEMAsmKEEFTRLKEALEKSEARRKELEEKMVSLLQEKND--------------------------------LQLQV 891
Cdd:TIGR02169 169 DRKKEKA--LEELEEVEENIERLDLIIDEKRQQLERLRREREKaeryqallkekreyegyellkekealerqkeaIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 892 QAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLED--EEEMN------AELTAKKRKLEDECSELKRDIDDLELTLAK 963
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLrvkekiGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 964 VEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKK 1043
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1044 VRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFE--------------LNALNARIEDEQALGSQLQKKLK 1109
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEikkqewkleqlaadLSKYEQELYDLKEEYDRVEKELS 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1110 ELQARIEELEEELEAERTA----RAKVEKLRSDLS------RELEEISER----LEEAGG----ATSVQIEMNKKREAEF 1171
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERvrggRAVEEVLKASIQgvhgtvAQLGSVGERyataIEVAAGnrlnNVVVEDDAVAKEAIEL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1172 QKmRRDLEEATLqheATAAALRKKHAD-SVAELGEQIDNLQRVKQKLEKEKSEFKLELDDvTSNMEQIIKAKAANLEKMC 1250
Cdd:TIGR02169 567 LK-RRKAGRATF---LPLNKMRDERRDlSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGD-TLVVEDIEAARRLMGKYRM 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1251 RTLEDQMNEhRSKA-----EETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGK---LTYTQQLEDLKRQLEE 1322
Cdd:TIGR02169 642 VTLEGELFE-KSGAmtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1323 EVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQwrtkYETDAIQRTEELEEAKKKLAQrlqeae 1402
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE----LEEDLHKLEEALNDLEARLSH------ 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1403 EAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTEL 1482
Cdd:TIGR02169 791 SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1483 FKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEgKILRA 1562
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-EIPEE 949
|
810
....*....|....*..
gi 119586555 1563 QLEFNQIKAEIERKLAE 1579
Cdd:TIGR02169 950 ELSLEDVQAELQRVEEE 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1074-1730 |
2.02e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.40 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1074 QQLDERLKKKD-----FELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISE 1148
Cdd:COG1196 216 RELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1149 RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALrkkhadsvAELGEQIDNLQRVKQKLEKEKSEFKLEL 1228
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL--------EELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1229 DDVTSNMEQIIKAKAANLEKMcRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTrgklt 1308
Cdd:COG1196 368 LEAEAELAEAEEELEELAEEL-LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE----- 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1309 ytQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELE 1388
Cdd:COG1196 442 --EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1389 EAKKKLAQRLQEAEEAVEAVnakcsslektkhrLQNEIEDLMVDVERSNAAAAAldkKQRNFDKILAEWKQKYEESQSEL 1468
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAA-------------LEAALAAALQNIVVEDDEVAA---AAIEYLKAAKAGRATFLPLDKIR 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1469 ESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEA 1548
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1549 EASLEHEEGKILRAQlefnqikAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEI 1628
Cdd:COG1196 664 GGSRRELLAALLEAE-------AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1629 QLShanrmaaeaqkqvkslqsLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEqtersrkLAEQELI 1708
Cdd:COG1196 737 LLE------------------ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNL-------LAIEEYE 791
|
650 660
....*....|....*....|..
gi 119586555 1709 ETSERVQLLHSQNTSLINQKKK 1730
Cdd:COG1196 792 ELEERYDFLSEQREDLEEARET 813
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
978-1861 |
8.67e-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: 100.14 E-value: 8.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 978 LTEEMAGLDEIIAKLTKEKKALQEAHQQaLDDLQAEEDKVNtltkakvkleQQVDDLEGslEQEKKVR-MDLERAKRKLE 1056
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEEN-IERLDLIIDEKR----------QQLERLRR--EREKAERyQALLKEKREYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1057 GDLKLTQesIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEaeRTARAKVEKLR 1136
Cdd:TIGR02169 225 GYELLKE--KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ--LRVKEKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1137 SDLS---RELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATA---AALRKKHADSVAELGEQIDNL 1210
Cdd:TIGR02169 301 AEIAsleRSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTeeyAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1211 QRVKQKLekekSEFKLELDDVTSNMEQiikakaanLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSR 1290
Cdd:TIGR02169 381 AETRDEL----KDYREKLEKLKREINE--------LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1291 QLDEKEALISQLTRGKLTYTQQLEDLK---RQLEEEV-KAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKAn 1366
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKeeyDRVEKELsKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTV- 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1367 SEVAQWRTKYETdaiqrteELEEAkkkLAQRLQEAEEAVEAVNAKCSSLEKTKH--RLQ----NEIEDLMVDVERSNAAA 1440
Cdd:TIGR02169 528 AQLGSVGERYAT-------AIEVA---AGNRLNNVVVEDDAVAKEAIELLKRRKagRATflplNKMRDERRDLSILSEDG 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1441 AA--------LDKKQRN-----------FDKILAEWKQ-------------------------KYEESQSELESSQKEAR 1476
Cdd:TIGR02169 598 VIgfavdlveFDPKYEPafkyvfgdtlvVEDIEAARRLmgkyrmvtlegelfeksgamtggsrAPRGGILFSRSEPAELQ 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1477 SLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVR-------KQLEAEKMELQSALEEAE 1549
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEeklkerlEELEEDLSSLEQEIENVK 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1550 ASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDslqtsldaETRSRNEALrvkkkmegdLNEMEIQ 1629
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE--------EEVSRIEAR---------LREIEQK 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1630 LSHANRMAAEAQKQVKSLQSLlkdtqiqlddavraNDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIE 1709
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQ--------------RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1710 TSErvqllhsqntslinQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKkeqdtsaHLERMKKNMEQ 1789
Cdd:TIGR02169 887 LKK--------------ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS-------EIEDPKGEDEE 945
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1790 tikdlqhrlDEAEQIALKGGKKQLQKLEARVRELE-------NELEAEQKRNAESVKGMRK--SERR-IKELTYQTEEDR 1859
Cdd:TIGR02169 946 ---------IPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKleEERKaILERIEEYEKKK 1016
|
..
gi 119586555 1860 KN 1861
Cdd:TIGR02169 1017 RE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
841-1513 |
2.98e-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: 98.59 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKM-------VSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKI 913
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLetlrskvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 914 QL-----EAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKV---KNLTEEMAGL 985
Cdd:TIGR02168 425 ELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQENLEGF 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 986 DEIIAKLTKEKKALQEAHQQALDDLQAEED---KVNT-----LTKAKVKLEQQVDDLEGSLEQEKKVRMDL-------ER 1050
Cdd:TIGR02168 505 SEGVKALLKNQSGLSGILGVLSELISVDEGyeaAIEAalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFlpldsikGT 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1051 AKRKLEGDLKLTQESIMDLENDKQQLDERLKK------------KDFElNALNARIE----------------------- 1095
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggvlvvDDLD-NALELAKKlrpgyrivtldgdlvrpggvitg 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1096 -DEQALGSQLQKK--LKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnkkrEAEFQ 1172
Cdd:TIGR02168 664 gSAKTNSSILERRreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL--------------SRQIS 729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1173 KMRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIiKAKAANLEKMCRT 1252
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-KEELKALREALDE 807
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1253 LEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAH 1332
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1333 ALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKC 1412
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDE 967
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1413 SSLEKTKHRLQNEIEDLmvdverSNAAAAALDKkqrnfdkiLAEWKQKYEESQselessqKEARSLSTELFKLKNAYEE- 1491
Cdd:TIGR02168 968 EEARRRLKRLENKIKEL------GPVNLAAIEE--------YEELKERYDFLT-------AQKEDLTEAKETLEEAIEEi 1026
|
730 740
....*....|....*....|....*.
gi 119586555 1492 ----SLEHLETFKRENKNLQEEISDL 1513
Cdd:TIGR02168 1027 dreaRERFKDTFDQVNENFQRVFPKL 1052
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
917-1794 |
3.09e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 98.60 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 917 AKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRdIDDLELTLAKVE-----KEKHATENKVKNLTEEMAGLDEIIAK 991
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 992 LTKEKKALQEAHQQALDDLQAEEDKVNTLTKAK-VKLEQQVDDLEGSLEQekkvrmdlerakrkLEGDLKLTQESIMDLE 1070
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAEIAS--------------LERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1071 NDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERL 1150
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1151 EEAGGATSVQIEMNKKREAEFQKMRRDLEEAtlqhEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFkleldd 1230
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGI----EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL------ 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1231 vtsnmeqiikakaanlekmcRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEA-------LISQLT 1303
Cdd:TIGR02169 472 --------------------YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLG 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1304 RGKLTYTQQLEDLKRQ------LEEEVKAKNA--LAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTK 1375
Cdd:TIGR02169 532 SVGERYATAIEVAAGNrlnnvvVEDDAVAKEAieLLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPK 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1376 YETD---AIQRT---EELEEAKK--------KLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAA 1441
Cdd:TIGR02169 612 YEPAfkyVFGDTlvvEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELS 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1442 ALDKKQRNFDKILAEWKQKyeesqselessqkeARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSG 1521
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQE--------------LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1522 KTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEF-NQIKAEIERKLAEKDeemeqAKRNHLRVVDSLQT 1600
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKlEEEVSRIEARLREIE-----QKLNRLTLEKEYLE 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1601 SLDAETRSRNEALRVKKKMEGD-LNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDavranddlkeniaiverrn 1679
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKeIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE------------------- 893
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1680 nlLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKM------DADLSQLQTEVEEAVQECRNAE 1753
Cdd:TIGR02169 894 --LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipeeELSLEDVQAELQRVEEEIRALE 971
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 119586555 1754 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDL 1794
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1287-1829 |
4.45e-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: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1287 ELSRQLDEKEALISQLTRGKLTytQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKAN 1366
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELE--AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1367 SEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKK 1446
Cdd:COG1196 295 AELAR--------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1447 QRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHE 1526
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1527 LEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEM---EQAKRNHLR---------- 1593
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflEGVKAALLLaglrglagav 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1594 -VVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEI-------QLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRAN 1665
Cdd:COG1196 527 aVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAieylkaaKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1666 DDLKENIAIVERRNNLLQAELEELRA--------VVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQ 1737
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLeaalrravTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1738 LQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLE 1817
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
570
....*....|....*
gi 119586555 1818 ---ARvreLENELEA 1829
Cdd:COG1196 767 relER---LEREIEA 778
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
220-706 |
1.05e-19 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 96.35 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 220 IIQANPALEAFGNAKTVRNDNSSRFGKF--IRIHFGATG---KLASADIETYLLEKSRVIFQL------KAERDYHIFYQ 288
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 289 ILSNKKPELLDMLLITNNPYD------YAFISQGETTVASIDDAEELMATD--------NAFDVLGFTSEEKNSMYKLTG 354
Cdd:cd14894 329 MVAGVNAFPFMRLLAKELHLDgidcsaLTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 355 AIMHFGNMKFKLKQREEQAEPDGT---EEADKSAYLMGLNSADLLKGLCHPR---VKVGNEYVTKGQNVQQVIYATGALA 428
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 429 KAVYERMFNWMV------TRINATLETKQPRQY-----------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLqqffnh 491
Cdd:cd14894 489 RLLYQLAFNYVVfvmneaTKMSALSTDGNKHQMdsnasapeavsLLKIVDVFGFEDLTHNSLDQLCINYLSEKL------ 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 492 hmFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTF-----KAKLFDNHL--GKSANFQ 564
Cdd:cd14894 563 --YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIydRNSSRLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 565 KPRNIKGKPEAH---------FSLIHYAGIVDYNIIGWLQKNKDPL-NETVVGLYQKSSLKLLSTLFANYAGADAPIEKG 634
Cdd:cd14894 641 EPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLNESSQLGWSPNTNR 720
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119586555 635 KGKAKKGSSFQTVSAL---HRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICR 706
Cdd:cd14894 721 SMLGSAESRLSGTKSFvgqFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1128-1908 |
1.61e-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: 95.96 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1128 ARAKVEKLRSDLSRELEEISERLEEAGgatsvqiEMNKKREAEFQK----MRRDLEEATLQHEATAAaLRKKHADSVAEL 1203
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESN-------ELHEKQKFYLRQsvidLQTKLQEMQMERDAMAD-IRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1204 GEQidnLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKAAN---LEKMCRTLED-------QMNEHRSKAEETQRSVND 1273
Cdd:pfam15921 144 RNQ---LQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHegvLQEIRSILVDfeeasgkKIYEHDSMSTMHFRSLGS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1274 LTSQRAK-LQTENGELSRQL----DEKEALISQLTRGKLTYTQQLEDLKRQL--EEEVKAkNALAHALQSARHDCDLLRE 1346
Cdd:pfam15921 221 AISKILReLDTEISYLKGRIfpveDQLEALKSESQNKIELLLQQHQDRIEQLisEHEVEI-TGLTEKASSARSQANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1347 QYE----EETEAKAELQRVLSKANSEVAQWRTkyetdaiqrteELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHR- 1421
Cdd:pfam15921 300 QLEiiqeQARNQNSMYMRQLSDLESTVSQLRS-----------ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQf 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1422 ------LQNEIEDLMVDV-ERSNAAAAALDKKQRNFDKILAEwKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLE 1494
Cdd:pfam15921 369 sqesgnLDDQLQKLLADLhKREKELSLEKEQNKRLWDRDTGN-SITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQME 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1495 -HLETFKRENKNLqEEISDLTEQLGSsgkTIHELEKVRKQLEAEKMELQSA---LEEAEASLEHEEGKILRAQLEFNQIK 1570
Cdd:pfam15921 448 rQMAAIQGKNESL-EKVSSLTAQLES---TKEMLRKVVEELTAKKMTLESSertVSDLTASLQEKERAIEATNAEITKLR 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1571 AEIERKLaekdEEMEQAKR--NHLRVVdslQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQ 1648
Cdd:pfam15921 524 SRVDLKL----QELQHLKNegDHLRNV---QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLE 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1649 SLLKDTQIQLDDAVRANDdlKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQElietSERVQLLHSQNTSLiNQK 1728
Cdd:pfam15921 597 KEINDRRLELQEFKILKD--KKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIK----QERDQLLNEVKTSR-NEL 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1729 KKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEE----LKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAE-- 1802
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQtrntLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQsk 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1803 ----QIALKGGKKQLQKLEARVRELENELEA---EQKRNAESVKGMRKSERRIKEltyqteedrkNLLRLQDLVDKLQLK 1875
Cdd:pfam15921 750 iqflEEAMTNANKEKHFLKEEKNKLSQELSTvatEKNKMAGELEVLRSQERRLKE----------KVANMEVALDKASLQ 819
|
810 820 830
....*....|....*....|....*....|...
gi 119586555 1876 VkAYKRQAEEAEEQANTNLskfrKVQHELDEAE 1908
Cdd:pfam15921 820 F-AECQDIIQRQEQESVRL----KLQHTLDVKE 847
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
847-1590 |
2.18e-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: 95.52 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 847 KEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERL 926
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 927 EDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAhqqa 1006
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE---- 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1007 lddLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLK----- 1081
Cdd:TIGR02169 450 ---IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgt 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1082 -------KKDFEL-------NALNARIEDEQALGSQLQKKLKELQArieeleeeleaERTARAKVEKLRsDLSRELEEIS 1147
Cdd:TIGR02169 527 vaqlgsvGERYATaievaagNRLNNVVVEDDAVAKEAIELLKRRKA-----------GRATFLPLNKMR-DERRDLSILS 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1148 ErlEEAGGATSVQIEMNKKREAEFQKMRRD------LEEA----------TLQHE-------ATAAALRKKHADSVA-EL 1203
Cdd:TIGR02169 595 E--DGVIGFAVDLVEFDPKYEPAFKYVFGDtlvvedIEAArrlmgkyrmvTLEGElfeksgaMTGGSRAPRGGILFSrSE 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1204 GEQIDNLQRVKQKLEKEKSEFKLELddvtsnmeqiikakaanlekmcRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQT 1283
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSEL----------------------RRIENRLDELSQELSDASRKIGEIEKEIEQLEQ 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1284 ENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQsarhdcDLLREQYEEETEakaELQRVLS 1363
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN------DLEARLSHSRIP---EIQAELS 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1364 KANSEVAQWRtkyetdaiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAAL 1443
Cdd:TIGR02169 802 KLEEEVSRIE--------ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1444 DKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKnlqeEISDLTEQLGSSGKT 1523
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEE 949
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1524 IHELEKVRKQLEAEKMELQsALEEAE--ASLEHEEGKILRAQLEFNQIKAEIERK-LAEKDEEMEQAKRN 1590
Cdd:TIGR02169 950 ELSLEDVQAELQRVEEEIR-ALEPVNmlAIQEYEEVLKRLDELKEKRAKLEEERKaILERIEEYEKKKRE 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
845-1619 |
4.48e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.82 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 845 REKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQleaKVKEMNE 924
Cdd:PTZ00121 1158 RKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAE---AVKKAEE 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 925 RLEDEEEmnAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNlTEEMAGLDEiiAKLTKEKKALQEAHQ 1004
Cdd:PTZ00121 1235 AKKDAEE--AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADE--AKKAEEKKKADEAKK 1309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1005 QALDDLQAEEDKVNT------LTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDE 1078
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAeeakkkADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1079 RLKKKDFELNALNARIE-DEQALGSQLQKKLKELQARIEELEEELEAERTA----RAKVEKLRSDLSRELEEISERLEEA 1153
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKaDELKKAAAAKKKADEAKKKAEEKKKADEAKKKAeeakKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1154 GGATSVQIEMNKKREAEfqKMRRDLEEATLQ-HEATAAALRKKHADSV--AELGEQIDNLQRVKQKL---EKEKSEFKLE 1227
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKAD--EAKKKAEEAKKKaDEAKKAAEAKKKADEAkkAEEAKKADEAKKAEEAKkadEAKKAEEKKK 1547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1228 LDDVtSNMEQIIKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQ---LDEKEALISQLTR 1304
Cdd:PTZ00121 1548 ADEL-KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELK 1626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1305 GKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLS-KANSEVAQWRTKYETDAIQR 1383
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEdEKKAAEALKKEAEEAKKAEE 1706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1384 TEELEEAKKKLAQRLQEAEEAVEavnAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNfdkilAEWKQKYEE 1463
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENK---IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK-----AEEIRKEKE 1778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1464 SQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRE----NKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKM 1539
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGnlviNDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNN 1858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1540 EL-QSALEEAEASLEheegKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHL-RVVDSLQTSLDAETRSRNEALRVKK 1617
Cdd:PTZ00121 1859 ENgEDGNKEADFNKE----KDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAgKNNDIIDDKLDKDEYIKRDAEETRE 1934
|
..
gi 119586555 1618 KM 1619
Cdd:PTZ00121 1935 EI 1936
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
841-1436 |
6.23e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.44 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSllQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIqlEAKVK 920
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE--EKKKADEAKKKAEEAKKADEAKKKAEEAKKKA--DAAKK 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 921 EMNERLEDEEEMNAELTAKKRKLEDecSELKRDIDDLEltlaKVEKEKHATENKVKnlTEEMAGLDEIIAKLTKEKKALQ 1000
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEA--AEEKAEAAEKK----KEEAKKKADAAKKK--AEEKKKADEAKKKAEEDKKKAD 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1001 EAHQQALDDLQAEEdkvntlTKAKVKLEQQVDDLEGSLEQEKKVrmdlERAKRKLEGDLKltqesimdLENDKQQLDERL 1080
Cdd:PTZ00121 1409 ELKKAAAAKKKADE------AKKKAEEKKKADEAKKKAEEAKKA----DEAKKKAEEAKK--------AEEAKKKAEEAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1081 KKKDFELNALNARIEDEqalgsqLQKKLKELQARIEELEEELEAERTA---RAKVEKLRSDLSRELEEiSERLEEAGGAT 1157
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADE------AKKKAEEAKKKADEAKKAAEAKKKAdeaKKAEEAKKADEAKKAEE-AKKADEAKKAE 1543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1158 SVQI--EMNKKREAEFQKMRRDLEEATLQHEATAAALRKkhadsvAELGEQIDNlQRVKQKLEKEKSEFKLELDDVTSNM 1235
Cdd:PTZ00121 1544 EKKKadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK------AEEAKKAEE-ARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1236 EQIIKAkaanlekmcrtledqmnEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLED 1315
Cdd:PTZ00121 1617 EAKIKA-----------------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1316 LKRQLEEEVKAKNALAHALQSARhDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEEL---EEAKK 1392
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEAkkdEEEKK 1757
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 119586555 1393 KLAQRLQEAEEAVEAVNAKCSSLekTKHRLQNEIEDLMVDVERS 1436
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKK 1799
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
987-1802 |
1.04e-18 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 93.26 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 987 EIIAKLTKE--KKALQEAHQQaLDDLQAEEDKVNTL-TKAKVKLEQQVDDLEGSLEQ---EKKVRMDLERAKRKLEGDLK 1060
Cdd:pfam15921 66 KIIAYPGKEhiERVLEEYSHQ-VKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1061 -LTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQAR-----IEELEEELEAERTARAKVEK 1134
Cdd:pfam15921 145 nQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEAsgkkiYEHDSMSTMHFRSLGSAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1135 LRSDLSRELEEISERLEEAGGA-TSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRV 1213
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQlEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1214 KQKLEKEKSEFKLELDDVTSNMEQIikakAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLd 1293
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLESTVSQL----RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1294 ekEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHalqsarhdcdlLREQYEEETEAKAELQRVLSKANSEvAQWR 1373
Cdd:pfam15921 380 --QKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDH-----------LRRELDDRNMEVQRLEALLKAMKSE-CQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1374 TKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLmvdversnaaAAALDKKQRNFDKI 1453
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL----------TASLQEKERAIEAT 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1454 LAEwkqkYEESQSELESSQKEARSLSTELFKLKNAYEESlEHLETFKRENKN----LQEEISDLTEQLGSSGKTIHELEK 1529
Cdd:pfam15921 516 NAE----ITKLRSRVDLKLQELQHLKNEGDHLRNVQTEC-EALKLQMAEKDKvieiLRQQIENMTQLVGQHGRTAGAMQV 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1530 VRKQLEAE----KMELQS---ALEEAEASLEHEEGKILRAQLE-FNQIKAEIERKLAEKDEEMEQAK-RNHLRVVDSLQT 1600
Cdd:pfam15921 591 EKAQLEKEindrRLELQEfkiLKDKKDAKIRELEARVSDLELEkVKLVNAGSERLRAVKDIKQERDQlLNEVKTSRNELN 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1601 SLDAETRSRNEALRVK-KKMEGDLNEMEIQLShanrmaaEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRN 1679
Cdd:pfam15921 671 SLSEDYEVLKRNFRNKsEEMETTTNKLKMQLK-------SAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQI 743
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1680 NLLQAELEELRAVVEQTERSRKLAEQELIETSERVqllhsqnTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKA 1759
Cdd:pfam15921 744 DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL-------STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA 816
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 119586555 1760 ITDAAMMAEELKKEQDTSAHLErmkknmeqtikdLQHRLDEAE 1802
Cdd:pfam15921 817 SLQFAECQDIIQRQEQESVRLK------------LQHTLDVKE 847
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
870-1429 |
1.85e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 92.41 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 870 RKELEEKmvsllqEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTakkrkledecsE 949
Cdd:PRK02224 193 KAQIEEK------EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE-----------T 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 950 LKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEkKALQEAHQQALDDLQAEedkvntltkakvkLEQ 1029
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLDDADAEAVEARREE-------------LED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1030 QVDDLEGSLEQekkVRMDLERAKRKLEGdlklTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLK 1109
Cdd:PRK02224 322 RDEELRDRLEE---CRVAAQAHNEEAES----LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1110 ELQARIEELEeeleaerTARAKVEKLRSDLSRELEEISERLEEAggATSVQIEMNKKREAEfqkmrrDLEEATLQHEATA 1189
Cdd:PRK02224 395 ELRERFGDAP-------VDLGNAEDFLEELREERDELREREAEL--EATLRTARERVEEAE------ALLEAGKCPECGQ 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1190 AALRKKHADSVAELGEQIDnlqrvkqKLEKEKSEFKLELDDVTSNMEQIIKAKAA-----NLEKMCRTLEDQMNEHRSKA 1264
Cdd:PRK02224 460 PVEGSPHVETIEEDRERVE-------ELEAELEDLEEEVEEVEERLERAEDLVEAedrieRLEERREDLEELIAERRETI 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1265 EETQRSVNDLTSQRAKLQTEnGELSRQLDEKEALISQLTRGKL-TYTQQLEDLKRQLEEEVKAKNALAhALQSARHDCDL 1343
Cdd:PRK02224 533 EEKRERAEELRERAAELEAE-AEEKREAAAEAEEEAEEAREEVaELNSKLAELKERIESLERIRTLLA-AIADAEDEIER 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1344 LREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQ 1423
Cdd:PRK02224 611 LREKREALAELNDERRERLAEKRERKRELEAEFDEARI---EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVE 687
|
....*.
gi 119586555 1424 NEIEDL 1429
Cdd:PRK02224 688 NELEEL 693
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1254-1928 |
2.70e-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: 92.16 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1254 EDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLD-------EKEALISQLTRGKLTYTQQLEDLKRQLEEEVKA 1326
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1327 KNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEeLEEAKKKLAQRLQEAEEAVE 1406
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK-LSKERKLLEERISEFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1407 AVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLK 1486
Cdd:pfam01576 170 EEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1487 NAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEF 1566
Cdd:pfam01576 250 ARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1567 NQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKS 1646
Cdd:pfam01576 330 TELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1647 LQSLLKDTQIQLDDAVRANDDLKEniaiverRNNLLQAELEELRAVVEQTE-RSRKLA------EQELIETSERVQLLHS 1719
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAE-------KLSKLQSELESVSSLLNEAEgKNIKLSkdvsslESQLQDTQELLQEETR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1720 QNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLD 1799
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1800 EAEQIALKggkkqLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTyqtEEDRKNLLRLQDLVDKlqlkvkay 1879
Cdd:pfam01576 563 EKAAAYDK-----LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQML---AEEKAISARYAEERDR-------- 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 119586555 1880 krqaeeAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1928
Cdd:pfam01576 627 ------AEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDL 669
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1156-1912 |
5.89e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 91.36 E-value: 5.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1156 ATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAElGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNM 1235
Cdd:PTZ00121 1089 ADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARK-AEDARKAEEARKAEDAKRVEIARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1236 EQIIKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVndlTSQRAKLQTENGELSRQLDEKealisqltrgKLTYTQQLED 1315
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAE---AARKAEEERKAEEARKAEDAK----------KAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1316 LKRQlEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRvlsKANsEVAQWRTKYETDAIQRTEE---LEEAKK 1392
Cdd:PTZ00121 1235 AKKD-AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KAD-ELKKAEEKKKADEAKKAEEkkkADEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1393 KlaqrlqeAEEAVEAVNAKCSSLEKTKhrlqnEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQ 1472
Cdd:PTZ00121 1310 K-------AEEAKKADEAKKKAEEAKK-----KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1473 KEARSLSTELFKLKNAyeeslEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKmELQSALEEAEASL 1552
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKA-----DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK-KAEEAKKADEAKK 1451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1553 EHEEGKilraqlefnqiKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAEtRSRNEALRVKKKMEGDLNEMEIQLSH 1632
Cdd:PTZ00121 1452 KAEEAK-----------KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKKAE 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1633 ANRMAAEAQK--QVKSLQSLLKDTQIQLDDAVRANDDLKEniaiVERRNNLLQAELEELRavveqteRSRKLAEQELIET 1710
Cdd:PTZ00121 1520 EAKKADEAKKaeEAKKADEAKKAEEKKKADELKKAEELKK----AEEKKKAEEAKKAEED-------KNMALRKAEEAKK 1588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1711 SERVQLlhSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQT 1790
Cdd:PTZ00121 1589 AEEARI--EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1791 IKDLQHRLDEAEQiALKGGKKQLQKLEARVREleneleAEQKRNAESVKGMRKSERRIKELTYQTEEDRKnllrlqdlvd 1870
Cdd:PTZ00121 1667 AKKAEEDKKKAEE-AKKAEEDEKKAAEALKKE------AEEAKKAEELKKKEAEEKKKAEELKKAEEENK---------- 1729
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 119586555 1871 klqLKVKAYKRQAEEAE---EQANTNLSKFRKVQHELDEAEERAD 1912
Cdd:PTZ00121 1730 ---IKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
931-1786 |
1.37e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 89.65 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 931 EMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDL 1010
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1011 QAEEDKVNTLTKAKVKLEQQvddlegSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNAL 1090
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEE------KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1091 NARIEdeqalgsQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAE 1170
Cdd:pfam02463 320 EKEKK-------KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1171 FQKMRRDLEEatlqhEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKAANLEKMC 1250
Cdd:pfam02463 393 KEEELELKSE-----EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1251 RTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNAL 1330
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIST 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1331 AHALQSAR--HDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAV 1408
Cdd:pfam02463 548 AVIVEVSAtaDEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEG 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1409 NAKCSSL--EKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLK 1486
Cdd:pfam02463 628 ILKDTELtkLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQR 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1487 NAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEF 1566
Cdd:pfam02463 708 EKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1567 NQIKAEIERKLAEKDEEMEQAKRNH----LRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQlsHANRMAAEAQK 1642
Cdd:pfam02463 788 VEEEKEEKLKAQEEELRALEEELKEeaelLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE--ELERLEEEITK 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1643 QVKSLQSLLKDTQIQLDDAVRanddlkENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNT 1722
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKD------ELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEE 939
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119586555 1723 SLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKN 1786
Cdd:pfam02463 940 LLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1077-1884 |
1.66e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.82 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1077 DERLK--KKDFELNALNARIEDEQAlgSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAG 1154
Cdd:PTZ00121 1069 DEGLKpsYKDFDFDAKEDNRADEAT--EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR 1146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1155 GATSVQIEMNKKREAEFQKMR--RDLEEATLQHEA-------TAAALRKKHADSVAELGEQIDNLQR---VKQKLEKEKS 1222
Cdd:PTZ00121 1147 KAEDAKRVEIARKAEDARKAEeaRKAEDAKKAEAArkaeevrKAEELRKAEDARKAEAARKAEEERKaeeARKAEDAKKA 1226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1223 EFKLELDDVTSNMEQIIKAKAANLEKMCRTLEDQMNEHRSKAEETQRSvndlTSQRAKLQTENGELSRQLDEKEalisql 1302
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA----EEARKADELKKAEEKKKADEAK------ 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1303 trgKLTYTQQLEDLKRQLEEEVKAKNALAHAlQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQ 1382
Cdd:PTZ00121 1297 ---KAEEKKKADEAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1383 RteelEEAKKKLAQRLQEAEEAVEAVNAKCSSLEktkhrlqneiedlmvdversnaaaaalDKKQRNFDKILAEWKQKyE 1462
Cdd:PTZ00121 1373 K----EEAKKKADAAKKKAEEKKKADEAKKKAEE---------------------------DKKKADELKKAAAAKKK-A 1420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1463 ESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQ 1542
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD 1500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1543 SALEEAEASLEHEEGKilRAQlefNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGD 1622
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAK--KAE---EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1623 LNEmeiqlshANRMAAEAQKQVKSlqsllkdtqiQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKL 1702
Cdd:PTZ00121 1576 KNM-------ALRKAEEAKKAEEA----------RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1703 AEQELIETSERVQLLHSQNTSLINQkkkmdADLSQLQTEVEEAVQECRNAEEKAKKAitdaammAEELKKEQDTSAHLER 1782
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKA-----AEEAKKAEEDKKKAEEAKKAEEDEKKA-------AEALKKEAEEAKKAEE 1706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1783 MKKNMEQTIKdlqhrldEAEQIalkggKKQLQKLEARVRELENELEaEQKRNAESVKGMRKSERRIKELTYQTEEDRKNL 1862
Cdd:PTZ00121 1707 LKKKEAEEKK-------KAEEL-----KKAEEENKIKAEEAKKEAE-EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEI 1773
|
810 820
....*....|....*....|..
gi 119586555 1863 LRLQDLVDKLQLKVKAYKRQAE 1884
Cdd:PTZ00121 1774 RKEKEAVIEEELDEEDEKRRME 1795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
858-1574 |
2.79e-17 |
|
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: 88.15 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 858 RLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLiKNKIQ-LEAKVKEMNERLEDEEEMNAEL 936
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNS-NNKIKiLEQQIKDLNDKLKKNKDKINKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 937 TAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATE-------NKVKNLTEEMAGLDEIIAKLTKEKKALqeahqqaldd 1009
Cdd:TIGR04523 102 NSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEEL---------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1010 lqaeEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLErakrKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNA 1089
Cdd:TIGR04523 172 ----ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1090 LNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEaggatsvqiEMNKKREA 1169
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ---------DWNKELKS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1170 EFQKMRRDLEEATLQheataaalRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKAANLEKM 1249
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQ--------ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1250 cRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLtrgkltyTQQLEDLKRQLEEEVKAKNA 1329
Cdd:TIGR04523 387 -KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN-------NSEIKDLTNQDSVKELIIKN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1330 LAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQEAEEAVEAVN 1409
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL---------------KKLNEEKKELEEKVKDLTKKISSLK 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1410 AKCSSLEKTKHRLQNEIEDLMVDVER--SNAAAAALDKKQRNFDKILAEWKQKYEesqselessqkearslstelfKLKN 1487
Cdd:TIGR04523 524 EKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQK---------------------SLKK 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1488 AYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFN 1567
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWP 662
|
....*..
gi 119586555 1568 QIKAEIE 1574
Cdd:TIGR04523 663 EIIKKIK 669
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
854-1730 |
3.80e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 88.49 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 854 EEFTRLKEALEKsearRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERcdQLIKNKIQLEAKVKEMNERLEDEEEMN 933
Cdd:pfam02463 166 RLKRKKKEALKK----LIEETENLAELIIDLEELKLQELKLKEQAKKALEY--YQLKEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 934 AELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAE 1013
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1014 EDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEgdlkltqesiMDLENDKQQLDERLKKKDFELNALNAR 1093
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE----------KLQEKLEQLEEELLAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1094 IEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQK 1173
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1174 MRRDLEEATLQHEATAAALRkkhadsvaelgEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKAANLEKMCRTL 1253
Cdd:pfam02463 470 SEDLLKETQLVKLQEQLELL-----------LSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAV 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1254 EDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHA 1333
Cdd:pfam02463 539 ENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADED 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1334 LQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDaiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCS 1413
Cdd:pfam02463 619 DKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV--KASLSELTKELLEIQELQEKAESELAKEEILR 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1414 SLEKTKHRLQNEIEDL-MVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNaYEES 1492
Cdd:pfam02463 697 RQLEIKKKEQREKEELkKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL-KEKE 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1493 LEHLETFKRENKNLQEEISDLTEQLGSsgktihELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAE 1572
Cdd:pfam02463 776 LAEEREKTEKLKVEEEKEEKLKAQEEE------LRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1573 IERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLShanRMAAEAQKQVKSLQSLLK 1652
Cdd:pfam02463 850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK---LNLLEEKENEIEERIKEE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1653 DTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQ--ELIETSERVQLLHSQNTSLINQKKK 1730
Cdd:pfam02463 927 AEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAieEFEEKEERYNKDELEKERLEEEKKK 1006
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
939-1588 |
3.10e-16 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 85.07 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 939 KKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLD----EIIAKLTKEKKALQEAHQqaldDLQAEE 1014
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEqqikDLNDKLKKNKDKINKLNS----DLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1015 DKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARI 1094
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1095 EDEQALGSQLQKKLKELQARIEeleeeleaertaraKVEKLRSDLSrELEEISERLEEAggATSVQIEMNKKrEAEFQKM 1174
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQ--------------KNKSLESQIS-ELKKQNNQLKDN--IEKKQQEINEK-TTEISNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1175 RRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMeqiIKAKAANLEKMCRTLE 1254
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKE-LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKE---LKSELKNQEKKLEEIQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1255 DQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQ---LEEEVKAKNALA 1331
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQindLESKIQNQEKLN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1332 HALQSARHDCDLLREQYEEETEakaELQRVLSKANSEVaqwrtkyeTDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAK 1411
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIE---RLKETIIKNNSEI--------KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1412 CSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKnaYEE 1491
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD--FEL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1492 SLEHLETFKRENknlQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKA 1571
Cdd:TIGR04523 555 KKENLEKEIDEK---NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
650
....*....|....*..
gi 119586555 1572 EIERKLAEKDEEMEQAK 1588
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEVK 648
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
845-1581 |
3.31e-16 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 85.48 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 845 REKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLadaeeRCDQLIKNKIQLEAKVKEMNE 924
Cdd:TIGR00606 310 HQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHI-----RARDSLIQSLATRLELDGFER 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 925 RLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQ 1004
Cdd:TIGR00606 385 GPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1005 QALDDLQAEEDKVNTLTKAKVKLEQ-----QVDDLEGSLEQEKKVRMDLERAKRKLEGDL------KLTQESIMDLENDK 1073
Cdd:TIGR00606 465 QLEGSSDRILELDQELRKAERELSKaeknsLTETLKKEVKSLQNEKADLDRKLRKLDQEMeqlnhhTTTRTQMEMLTKDK 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1074 QQLDERLKKKDF----ELNALNARIEDEQALGSQLQKKLKE---LQARIEELEEELEAERTARAKVEKLRSDLSRELEEI 1146
Cdd:TIGR00606 545 MDKDEQIRKIKSrhsdELTSLLGYFPNKKQLEDWLHSKSKEinqTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1147 SERLEEAGGATSVQIEMNKKREaEFQKMRRDLE-------------EATLQHEATAAALRKKHADSVAELGEQIDNLQRV 1213
Cdd:TIGR00606 625 EDKLFDVCGSQDEESDLERLKE-EIEKSSKQRAmlagatavysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSK 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1214 KQKLEKEKSEFKLELDDVTSNMEQII---KAKAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSR 1290
Cdd:TIGR00606 704 LRLAPDKLKSTESELKKKEKRRDEMLglaPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEES 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1291 QLDEK------EALISQLTRGKLTYTQQLE-----DLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQ 1359
Cdd:TIGR00606 784 AKVCLtdvtimERFQMELKDVERKIAQQAAklqgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLK 863
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1360 RVLSKANSEVAQWRTkyetdAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAA 1439
Cdd:TIGR00606 864 SKTNELKSEKLQIGT-----NLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK 938
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1440 AA-ALDKKQRNFDKILAEWK--QKYEESQSELESSQKEarslsTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQ 1516
Cdd:TIGR00606 939 AQdKVNDIKEKVKNIHGYMKdiENKIQDGKDDYLKQKE-----TELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQ 1013
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1517 ---------LGSSGKTIHELEKVRKQLEAEKMELQ--------SALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAE 1579
Cdd:TIGR00606 1014 erwlqdnltLRKRENELKEVEEELKQHLKEMGQMQvlqmkqehQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
..
gi 119586555 1580 KD 1581
Cdd:TIGR00606 1094 PQ 1095
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1271-1932 |
6.51e-16 |
|
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: 84.35 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1271 VNDLTSQRAKLQTENGELSRQLDEKEALISQLTrgkltytQQLEDLKRQLEEEVKAKN-----------ALAHALQSARH 1339
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKR-------QQLERLRREREKAERYQAllkekreyegyELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1340 DCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTK 1419
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1420 HRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETF 1499
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1500 KRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAE 1579
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1580 KD---EEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEG------DLNEME------IQLSHANRM-------- 1636
Cdd:TIGR02169 478 YDrveKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGvhgtvaQLGSVGeryataIEVAAGNRLnnvvvedd 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1637 --AAEAQKQVKS-------------LQSLLKDTQIQLDDAVRAN-------DDLKENIAIVERRNNLLQAELEELRAVVE 1694
Cdd:TIGR02169 558 avAKEAIELLKRrkagratflplnkMRDERRDLSILSEDGVIGFavdlvefDPKYEPAFKYVFGDTLVVEDIEAARRLMG 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1695 Q----------------------TERSRKL----AEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQE 1748
Cdd:TIGR02169 638 KyrmvtlegelfeksgamtggsrAPRGGILfsrsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1749 CRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEAR-----VREL 1823
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE-DLHKLEEALNDLEARlshsrIPEI 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1824 ENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHE 1903
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
730 740
....*....|....*....|....*....
gi 119586555 1904 LDEAEERADIAESQVNKLRAKSRDIGTKR 1932
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRELERKI 905
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1259-1841 |
8.57e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.55 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1259 EHRSKAEETQRSVNDLTSQRaklQTENGELSRQLDEKEA--LISQLTRgkltytqqLEDLKRQLEEEVKAKNALAHALQS 1336
Cdd:PRK02224 166 EYRERASDARLGVERVLSDQ---RGSLDQLKAQIEEKEEkdLHERLNG--------LESELAELDEEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1337 ARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYET------DAIQRTEELEEAKKKLAQRLQEAEEAVEAVNA 1410
Cdd:PRK02224 235 TRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREElaeevrDLRERLEELEEERDDLLAEAGLDDADAEAVEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1411 KCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQkyeesqselessqkEARSLSTELfklknayE 1490
Cdd:PRK02224 315 RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE--------------EAAELESEL-------E 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1491 ESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIK 1570
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1571 -----------------AEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDA-ETRSRNEALRVKKKMEGDL-NEMEIQLS 1631
Cdd:PRK02224 454 cpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDLvEAEDRIERLEERREDLEELiAERRETIE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1632 HANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERsRKLAEQELIETS 1711
Cdd:PRK02224 534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLR 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1712 ERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEA-VQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQT 1790
Cdd:PRK02224 613 EKREALAELNDERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 119586555 1791 IKDLQHRLDeaeqiALKGGKKQLQKLEARVRELEN---ELEAE-QKRNAESVKGM 1841
Cdd:PRK02224 693 LEELRERRE-----ALENRVEALEALYDEAEELESmygDLRAElRQRNVETLERM 742
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1485-1927 |
1.46e-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: 83.24 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1485 LKNAYEESLEHLETfkreNKNLQEEIsdlteqLGSSGKTIHELEKVRKQLEAEKMELQSAL---EEAEASLEHEEGKIlr 1561
Cdd:pfam15921 143 LRNQLQNTVHELEA----AKCLKEDM------LEDSNTQIEQLRKMMLSHEGVLQEIRSILvdfEEASGKKIYEHDSM-- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1562 AQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTsLDAETRSRNEAL--RVKKKMEGDLNEMEIQLSHANRMAAE 1639
Cdd:pfam15921 211 STMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEA-LKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1640 AQKQVKSLQSLLKDTQIQlddavranddlkeniaiVERRNNLLQAELEELRAVVEQTE---RSRKLAEQELIETSERVQL 1716
Cdd:pfam15921 290 ARSQANSIQSQLEIIQEQ-----------------ARNQNSMYMRQLSDLESTVSQLRselREAKRMYEDKIEELEKQLV 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1717 LhsqntslinqkkkMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQH 1796
Cdd:pfam15921 353 L-------------ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRR 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1797 RLDEAEQialkggkkQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKV 1876
Cdd:pfam15921 420 ELDDRNM--------EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1877 KAYKR----------QAEEAEEQANTNLSKFR--------KVQHELDEAEERADI-AESQVNKLRAKSRD 1927
Cdd:pfam15921 492 ESSERtvsdltaslqEKERAIEATNAEITKLRsrvdlklqELQHLKNEGDHLRNVqTECEALKLQMAEKD 561
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
840-1402 |
1.46e-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: 83.24 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 840 LKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNladAEERCDQLIKNKIQLEAKV 919
Cdd:pfam15921 250 LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 920 kemnerledeEEMNAELTAKKRKLEDECSELKRD--IDDLELTLAKVEKEKHATENkvKNLTEEmagLDEIIAKLTKEKK 997
Cdd:pfam15921 327 ----------SQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQ---LQKLLADLHKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 998 ALQEAHQQ--------------------ALDDLQAEEDKVNTLTKA-----KVKLEQQVDDLEG---SLEQEKKVRMDLE 1049
Cdd:pfam15921 392 ELSLEKEQnkrlwdrdtgnsitidhlrrELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneSLEKVSSLTAQLE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1050 RAKRKLEGDLKLTQESIMDLENDKQ---QLDERLKKKDFELNALNARIedeQALGSQLQKKLKELQ------ARIEELEE 1120
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLESSERtvsDLTASLQEKERAIEATNAEI---TKLRSRVDLKLQELQhlknegDHLRNVQT 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1121 ELEAERTARAKVEKLRSDLSRELEEISERLEEAG-GATSVQIEmNKKREAEFQKMRRDLEEATLqheataaaLRKKHADS 1199
Cdd:pfam15921 549 ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGrTAGAMQVE-KAQLEKEINDRRLELQEFKI--------LKDKKDAK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1200 VAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQI---IKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTS 1276
Cdd:pfam15921 620 IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLlneVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKM 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1277 QRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQ----------LEEEVKAKNALAHALQSARH------- 1339
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQidalqskiqfLEEAMTNANKEKHFLKEEKNklsqels 779
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119586555 1340 -----------DCDLLREQYEEETEAKAELQRVLSKANSEVAQWRtkyetDAIQRTEElEEAKKKLAQRLQEAE 1402
Cdd:pfam15921 780 tvateknkmagELEVLRSQERRLKEKVANMEVALDKASLQFAECQ-----DIIQRQEQ-ESVRLKLQHTLDVKE 847
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
901-1453 |
1.47e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.72 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 901 AEERCDQLIKNKIQ-LEAKVKEMNERLEDEEEMNAELtAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLT 979
Cdd:PRK03918 187 RTENIEELIKEKEKeLEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 980 EEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLtKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLE--- 1056
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEEEINGIEERIKELEEKEERLEelk 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1057 GDLKLTQESIMDLENDKQQLDERLKKKDfELNALNARIEDEQAlgSQLQKKLKELQARIEELEEELEAERTARAKVEKLR 1136
Cdd:PRK03918 345 KKLKELEKRLEELEERHELYEEAKAKKE-ELERLKKRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1137 SDLSRELEEiserLEEAGGATSVQiemnkKREAEFQKMRRDLEEATLQheataaalRKKHADSVAELGEQIDNLQRVKQK 1216
Cdd:PRK03918 422 KELKKAIEE----LKKAKGKCPVC-----GRELTEEHRKELLEEYTAE--------LKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1217 LEKEKSEFKlELDDVTSNMEQII----KAKAANLEKMCRTLED--QMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSR 1290
Cdd:PRK03918 485 LEKVLKKES-ELIKLKELAEQLKeleeKLKKYNLEELEKKAEEyeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1291 QLDEKEA----LISQLTRGKLTYTQQLEDLKRQLE----EEVKAKNAlAHALQSARHDCDLLREQYEEETEAKAELQRVL 1362
Cdd:PRK03918 564 KLDELEEelaeLLKELEELGFESVEELEERLKELEpfynEYLELKDA-EKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1363 SKANSEVAQWRTKYETDaiqRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAA 1442
Cdd:PRK03918 643 EELRKELEELEKKYSEE---EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKA 719
|
570
....*....|.
gi 119586555 1443 LDKKQRNFDKI 1453
Cdd:PRK03918 720 LERVEELREKV 730
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
32-76 |
3.27e-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: 68.23 E-value: 3.27e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 119586555 32 DLKKDVFVPDDKQEFVKAKIVSREGGKVTAETEYGKTVTVKEDQV 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1053-1801 |
4.67e-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: 77.75 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1053 RKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKelqarieeleeeleaerTARAKV 1132
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLK-----------------KNKDKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1133 EKLRSDLSRELEEISERLEEaggatsvqieMNKKrEAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQR 1212
Cdd:TIGR04523 99 NKLNSDLSKINSEIKNDKEQ----------KNKL-EVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1213 VKQKLEKEKSEFKLELDDVTSNMEQIiKAKAANLEKMCRTLEDQMNEHRSkaeetqrsvndLTSQRAKLQTENGELSRQL 1292
Cdd:TIGR04523 167 QKEELENELNLLEKEKLNIQKNIDKI-KNKLLKLELLLSNLKKKIQKNKS-----------LESQISELKKQNNQLKDNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1293 DEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAknalahaLQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQ- 1371
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ-------LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQd 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1372 WRTKYETDAIQRTEELEEAKKKLAQrlqeAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFD 1451
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQ----NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1452 KILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVR 1531
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1532 KQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAE---IERKLAEKDEEMEQAKRNhLRVVDSLQTSLDAETRS 1608
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEkkeLEEKVKDLTKKISSLKEK-IEKLESEKKEKESKISD 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1609 RNEALrVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEE 1688
Cdd:TIGR04523 543 LEDEL-NKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1689 LRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKA----KKAIT--- 1761
Cdd:TIGR04523 622 AKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELslhyKKYITrmi 701
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 119586555 1762 ---DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEA 1801
Cdd:TIGR04523 702 rikDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1037-1927 |
5.16e-14 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 78.16 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1037 SLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFElNALNARIEDEQALGSQLQKKLKELQARIE 1116
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS-REIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1117 ELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGatsvQIEMNKKREA-EFQKMRRDLEEATLQHEATAAALRKK 1195
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLN----DLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1196 HADSVAELGE-----QIDNLQRVKQKLEKEKSEFKLELD------DVTSNMEQIIKAKAANLEKMCRTLEDQMNEHRSKA 1264
Cdd:TIGR00606 342 KTELLVEQGRlqlqaDRHQEHIRARDSLIQSLATRLELDgfergpFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1265 EETQRSVNDLTSQRAKL----QTENGELSRQLDEKEALISQLTRGkltyTQQLEDLKRQLEEEVKAKNALAHALQSARHD 1340
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLgrtiELKKEILEKKQEELKFVIKELQQL----EGSSDRILELDQELRKAERELSKAEKNSLTE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1341 CDLLREQYEEETeaKAELQRVLSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRL-----QEAEEAVEAVN--AKCS 1413
Cdd:TIGR00606 498 TLKKEVKSLQNE--KADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQIrkiksRHSDELTSLLGyfPNKK 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1414 SLEKTKHRLQNEI---EDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEES-------------QSELESSQKEARS 1477
Cdd:TIGR00606 574 QLEDWLHSKSKEInqtRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgsqdeesdLERLKEEIEKSSK 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1478 LSTELFKLKNAYEESLEHLET------------FKREnKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSAL 1545
Cdd:TIGR00606 654 QRAMLAGATAVYSQFITQLTDenqsccpvcqrvFQTE-AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLA 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1546 EEAEASLEHEEGKILRAQLEFNQIKAEIERKLA--EKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDL 1623
Cdd:TIGR00606 733 PGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNdiEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQA 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1624 NEMEiqlshanrmAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRA----VVEQTERS 1699
Cdd:TIGR00606 813 AKLQ---------GSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklqIGTNLQRR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1700 RKLAEQeLIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQecrNAEEKAKKAITDAAMMAEELKK------- 1772
Cdd:TIGR00606 884 QQFEEQ-LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS---SKETSNKKAQDKVNDIKEKVKNihgymkd 959
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1773 -EQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENELEAE--QKRNAESVKGMRKSERRIK 1849
Cdd:TIGR00606 960 iENKIQDGKDDYLKQKETELNTVNAQLEECEK--------HQEKINEDMRLMRQDIDTQkiQERWLQDNLTLRKRENELK 1031
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119586555 1850 ELtyqtEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRD 1927
Cdd:TIGR00606 1032 EV----EEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYRE 1105
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
841-1415 |
5.39e-14 |
|
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: 77.91 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAE--------------QDNLADAEERCD 906
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEeeakrnverqlstlQAQLSDMKKKLE 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 907 QLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLD 986
Cdd:pfam01576 535 EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEK 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 987 EIIAKLT------------KEKKALQEAHqqALDDLQaeeDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRK 1054
Cdd:pfam01576 615 AISARYAeerdraeaeareKETRALSLAR--ALEEAL---EAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRA 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1055 LEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIE-DEQALGSQLQKKLKELQARIEELEEELEAERTARAKVE 1133
Cdd:pfam01576 690 LEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFErDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAV 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1134 KLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEA--------------------------TLQHEA 1187
Cdd:pfam01576 770 AAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEArasrdeilaqskesekklknleaellQLQEDL 849
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1188 TAAALRKKHADSVA-ELGEQIDN-------LQRVKQKLEKEKSEFKLELDDVTSNMEqIIKAKAANLEKMCRTLEDQMNE 1259
Cdd:pfam01576 850 AASERARRQAQQERdELADEIASgasgksaLQDEKRRLEARIAQLEEELEEEQSNTE-LLNDRLRKSTLQVEQLTTELAA 928
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1260 HRSKAEETQrsvndltSQRAKLQTENGELSRQLDEKEALI-SQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSAR 1338
Cdd:pfam01576 929 ERSTSQKSE-------SARQQLERQNKELKAKLQEMEGTVkSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTE 1001
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119586555 1339 HDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSL 1415
Cdd:pfam01576 1002 KKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE-EAEEEASRANAARRKLQRELDDATESNESMNREVSTL 1077
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1077-1924 |
5.95e-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: 77.70 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1077 DERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEEleaertARAKVEKLRSDLSRELEEISERLEEAGGA 1156
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELK------LQELKLKEQAKKALEYYQLKEKLELEEEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1157 TSVQIEMnkKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNME 1236
Cdd:pfam02463 226 LLYLDYL--KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1237 Q------IIKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYT 1310
Cdd:pfam02463 304 KlerrkvDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1311 QQLEDLKRQLEEEvkaknaLAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEA 1390
Cdd:pfam02463 384 ERLSSAAKLKEEE------LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1391 KKKLAQRLQEAEEAVEAVNAKCsSLEKTKHRLQNEIEDLMVDVERSNAA---AAALDKKQRNFDKILAEWKQKYEESQSE 1467
Cdd:pfam02463 458 LKLLKDELELKKSEDLLKETQL-VKLQEQLELLLSRQKLEERSQKESKArsgLKVLLALIKDGVGGRIISAHGRLGDLGV 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1468 LESSQKEARSLST-ELFKLKNAYEESLEHLETFKRENKN----LQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQ 1542
Cdd:pfam02463 537 AVENYKVAISTAViVEVSATADEVEERQKLVRALTELPLgarkLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1543 SALEEAEASLEHEEGKILraqlefnqiKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGD 1622
Cdd:pfam02463 617 EDDKRAKVVEGILKDTEL---------TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAES 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1623 LNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIV---ERRNNLLQAELEELRAVVEQTERS 1699
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLlkqKIDEEEEEEEKSRLKKEEKEEEKS 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1700 RKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKA----ITDAAMMAEELKKEQD 1775
Cdd:pfam02463 768 ELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEekikEEELEELALELKEEQK 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1776 TSAHLE---RMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELT 1852
Cdd:pfam02463 848 LEKLAEeelERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEA 927
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119586555 1853 YQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1924
Cdd:pfam02463 928 EILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
900-1575 |
7.16e-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: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 900 DAEERCDQLIKNKIQLEakvkEMNERLEDEEEmNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATenKVKNLT 979
Cdd:COG4913 222 DTFEAADALVEHFDDLE----RAHEALEDARE-QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR--RLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 980 EEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTL-TKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGD 1058
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1059 LKLTQEsimDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIeeleeeleaertarAKVEKLRSD 1138
Cdd:COG4913 375 LPASAE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI--------------ASLERRKSN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1139 LSRELEEISERLEEAGGATSVQ-------IEMnKKREAEFqkmrRDLEEATLQHEATAAALRKKHADSVAELGEQID--- 1208
Cdd:COG4913 438 IPARLLALRDALAEALGLDEAElpfvgelIEV-RPEEERW----RGAIERVLGGFALTLLVPPEHYAAALRWVNRLHlrg 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1209 --NLQRVKQKLEKEKSEF--------KLELDD--VTSNMEQIIkAKAANLEKmCRTLEDQMNEHRS-------KAEETQR 1269
Cdd:COG4913 513 rlVYERVRTGLPDPERPRldpdslagKLDFKPhpFRAWLEAEL-GRRFDYVC-VDSPEELRRHPRAitragqvKGNGTRH 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1270 SVNDLTSQRAKLQT--ENGelsRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQ 1347
Cdd:COG4913 591 EKDDRRRIRSRYVLgfDNR---AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1348 yEEETEAKAELQRvLSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIE 1427
Cdd:COG4913 668 -REIAELEAELER-LDASSDDL---------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1428 DLMVDVErsnaAAAALDKKQRNFDkiLAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNlq 1507
Cdd:COG4913 731 ELQDRLE----AAEDLARLELRAL--LEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPA-- 802
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119586555 1508 eEISDLTEQLGSsgktIHELEKVRKQLEAEKM-ELQSALEEAEASLEHEEGKILRAQL--EFNQIKAEIER 1575
Cdd:COG4913 803 -ETADLDADLES----LPEYLALLDRLEEDGLpEYEERFKELLNENSIEFVADLLSKLrrAIREIKERIDP 868
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
843-1600 |
8.48e-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: 8.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 843 AEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM 922
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 923 NERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEA 1002
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1003 HQQALDDLQA--EEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERL 1080
Cdd:pfam02463 435 EEESIELKQGklTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1081 KKKDFELNALNARIEDEQALGSQLQKklKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQ 1160
Cdd:pfam02463 515 LIKDGVGGRIISAHGRLGDLGVAVEN--YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLK 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1161 IEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLE-KEKSEFKLELDDVTSNMEQII 1239
Cdd:pfam02463 593 SIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKgVSLEEGLAEKSEVKASLSELT 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1240 KAKAANLEKMCRTLEDQMNEHRSKAEETQrsvnDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQ 1319
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILRRQLEI----KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEE 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1320 LEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSevaqwrtkyetdaiqRTEELEEAKKKLAQRLQ 1399
Cdd:pfam02463 749 EEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKL---------------KAQEEELRALEEELKEE 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1400 EAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVErsnaAAAALDKKQRNFDKILAEWK------QKYEESQSELESSQK 1473
Cdd:pfam02463 814 AELLEEEQLLIEQEEKIKEEELEELALELKEEQKL----EKLAEEELERLEEEITKEELlqelllKEEELEEQKLKDELE 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1474 EARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLE 1553
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAK 969
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 119586555 1554 HEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQT 1600
Cdd:pfam02463 970 EELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
880-1701 |
9.39e-14 |
|
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: 77.19 E-value: 9.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 880 LLQEKNDLQLQVQAEQDNLADAEERC---DQLIKNKIQLEAK---VKEMNERLEDEEEMNAEltaKKRKLEDECSELKRD 953
Cdd:pfam12128 153 TLLGRERVELRSLARQFALCDSESPLrhiDKIAKAMHSKEGKfrdVKSMIVAILEDDGVVPP---KSRLNRQQVEHWIRD 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 954 IDdlelTLAKVEKEKHatenKVKNLTEEMAGLDEIIAKLTKEKKALQEaHQQALDDLQAEEDKvntltkAKVKLEQQVDD 1033
Cdd:pfam12128 230 IQ----AIAGIMKIRP----EFTKLQQEFNTLESAELRLSHLHFGYKS-DETLIASRQEERQE------TSAELNQLLRT 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1034 LEGSLeqekkvrmdlerakrklegdlkltQESIMDLENDKQQLDERLKKKDFELNALNARiedeqalgsqlqkKLKELQA 1113
Cdd:pfam12128 295 LDDQW------------------------KEKRDELNGELSAADAAVAKDRSELEALEDQ-------------HGAFLDA 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1114 RIEeleeeleaerTARAKVEKLRSdLSRELEEISERLE-EAGGATSVQIEMNKKREAEFQKMRRDL-----------EEA 1181
Cdd:pfam12128 338 DIE----------TAAADQEQLPS-WQSELENLEERLKaLTGKHQDVTAKYNRRRSKIKEQNNRDIagikdklakirEAR 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1182 TLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKAAnlekmcrtlEDQMNEHR 1261
Cdd:pfam12128 407 DRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENF---------DERIERAR 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1262 SKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTrgkltytQQLEDLKRQL------------EEEVKAKNA 1329
Cdd:pfam12128 478 EEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQ-------SALDELELQLfpqagtllhflrKEAPDWEQS 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1330 LAHALQSAR-HDCDLLREQYEEETEAKAELQRV-LSKANSEVAQWrtkyetdaIQRTEELEEakkklaqRLQEAEEAVEA 1407
Cdd:pfam12128 551 IGKVISPELlHRTDLDPEVWDGSVGGELNLYGVkLDLKRIDVPEW--------AASEEELRE-------RLDKAEEALQS 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1408 VNAKCSSLEKTKHRLQNEIEDLmvDVERSNAAAA---ALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFK 1484
Cdd:pfam12128 616 AREKQAAAEEQLVQANGELEKA--SREETFARTAlknARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ 693
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1485 LKNAYEESLEHLETFKRENKN-----LQEEISDLTEQLGSSGKTIhelEKVRKQLEAEKMELQSALEEAEASLEHEEGKI 1559
Cdd:pfam12128 694 LDKKHQAWLEEQKEQKREARTekqayWQVVEGALDAQLALLKAAI---AARRSGAKAELKALETWYKRDLASLGVDPDVI 770
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1560 LRaqlefnqIKAEIeRKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRvkkKMEGDLNEMEIQLShanRMAAE 1639
Cdd:pfam12128 771 AK-------LKREI-RTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLS---NIERAISELQQQLA---RLIAD 836
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119586555 1640 AQKQVKSLQSLLK---DTQIQLDDAVRANDDLKENIAIVERRNNLLQAELE--ELRAVVEQTERSRK 1701
Cdd:pfam12128 837 TKLRRAKLEMERKaseKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSigERLAQLEDLKLKRD 903
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1382-1927 |
1.66e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.26 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1382 QRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKhrlqNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKy 1461
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1462 eesqselESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVR---KQLEAEK 1538
Cdd:PRK03918 275 -------IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1539 MELQSALEEAEASLE-HEEGKILRAQLEfnQIKAEIE----RKLAEKDEEMEQAK---RNHLRVVDSLQTSLDAETRSRN 1610
Cdd:PRK03918 348 KELEKRLEELEERHElYEEAKAKKEELE--RLKKRLTgltpEKLEKELEELEKAKeeiEEEISKITARIGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1611 EALRVKKKMEGD--LNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLkENIAIVERRNNLLQAELEE 1688
Cdd:PRK03918 426 KAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQ 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1689 LRAVVEQTErsrKLAEQELIETSERVQLLHSQNTslinqkkKMDADLSQLQTEVEEAvqecrNAEEKAKKAITDAAMMAE 1768
Cdd:PRK03918 505 LKELEEKLK---KYNLEELEKKAEEYEKLKEKLI-------KLKGEIKSLKKELEKL-----EELKKKLAELEKKLDELE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1769 ELKKEQdtsahLERMKKNMEQTIKDLQHRLDEAEQ-----IALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRK 1843
Cdd:PRK03918 570 EELAEL-----LKELEELGFESVEELEERLKELEPfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1844 SERRIKELTYQ-TEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERAD---IAESQVN 1919
Cdd:PRK03918 645 LRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEkleKALERVE 724
|
....*...
gi 119586555 1920 KLRAKSRD 1927
Cdd:PRK03918 725 ELREKVKK 732
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1174-1872 |
1.74e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.11 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1174 MRRDLEEATLQHEATAAAlrKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELddvtsnmeqiIKAKAANLEKMCRTL 1253
Cdd:COG4913 240 AHEALEDAREQIELLEPI--RELAERYAAARERLAELEYLRAALRLWFAQRRLEL----------LEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1254 EDQMNEHRSKAEETQRSVNDLTSQRAklqtENGelsrqldekealisqltrgkltyTQQLEDLKRQLEEEVKAKNALAHA 1333
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIR----GNG-----------------------GDRLEQLEREIERLERELEERERR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1334 LQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQE-----------AE 1402
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiaslerrksniPA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1403 EAVEAVNAKCSSLEKTKHRL----------------QNEIE--------DLMVDVERSNAAAAALDK---KQR-NFDKIl 1454
Cdd:COG4913 441 RLLALRDALAEALGLDEAELpfvgelievrpeeerwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV- 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1455 aewkqkyEESQSELESSQKEARSLSTELFKLKNAYEESLEHL-------------ETFKRENKNlqeeisdLTEQ-LGSS 1520
Cdd:COG4913 520 -------RTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRA-------ITRAgQVKG 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1521 GKTIHELEKVRKqleaekmeLQSAL---EEAEASLEHEEGKILRAQLEFNQIKAEIErKLAEKDEEMEQAKRNHLRVVDS 1597
Cdd:COG4913 586 NGTRHEKDDRRR--------IRSRYvlgFDNRAKLAALEAELAELEEELAEAEERLE-ALEAELDALQERREALQRLAEY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1598 LQTSLDAETRSRnealrvkkkmegDLNEMEIQLSHANrmaaEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVER 1677
Cdd:COG4913 657 SWDEIDVASAER------------EIAELEAELERLD----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1678 RNNLLQAELEELRAVVEQTERSRKLAEQELIEtsERVQLLHSQNT------SLINQKKKMDADLSQLQTEVEEAVQE-CR 1750
Cdd:COG4913 721 ELEQAEEELDELQDRLEAAEDLARLELRALLE--ERFAAALGDAVerelreNLEERIDALRARLNRAEEELERAMRAfNR 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1751 NAEEKAKKAITDAAMMAEELK-----KEQDTSAHLERMK----KNMEQTIKDLQHRLDEAEQIAlkggKKQLQKLEARVR 1821
Cdd:COG4913 799 EWPAETADLDADLESLPEYLAlldrlEEDGLPEYEERFKellnENSIEFVADLLSKLRRAIREI----KERIDPLNDSLK 874
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 119586555 1822 ELE-NE-----LEAEQKRNAEsVKGMRKSERRIKELTYQTEED--RKNLLRLQDLVDKL 1872
Cdd:COG4913 875 RIPfGPgrylrLEARPRPDPE-VREFRQELRAVTSGASLFDEElsEARFAALKRLIERL 932
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
843-1386 |
2.10e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.87 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 843 AEREKEMASMKEEFTRLKEaLEKSEARRKELEEKMVSLLQEKNDLQlqvqaeqdnladaeercdqliKNKIQLEAKVKEM 922
Cdd:PRK03918 269 EELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIE---------------------KRLSRLEEEINGI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 923 NERLEDEEEMNAELtakkRKLEDECSELKRDIDDLEltlakvekEKHATENKVKNLTEEMAGLDEIIAKLTKEK--KALQ 1000
Cdd:PRK03918 327 EERIKELEEKEERL----EELKKKLKELEKRLEELE--------ERHELYEEAKAKKEELERLKKRLTGLTPEKleKELE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1001 EAHQQALDdlqaEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGD-----LKLTQESIMDLENDKQQ 1075
Cdd:PRK03918 395 ELEKAKEE----IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1076 LDERLKKKDFELNALNARIEDEQALGSQLQ--KKLKELQARIEELEeeleaertarakVEKLRSDlSRELEEISERLEEA 1153
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYN------------LEELEKK-AEEYEKLKEKLIKL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1154 GGATSVqIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsVAELG-EQIDNLQRVKQKLEKEKSEFkLELDDVT 1232
Cdd:PRK03918 538 KGEIKS-LKKELEKLEELKKKLAELEKKLDELEEELAELLKE----LEELGfESVEELEERLKELEPFYNEY-LELKDAE 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1233 SNMEqIIKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTS-----QRAKLQTENGELSRQLDEKEALISQLTRGKL 1307
Cdd:PRK03918 612 KELE-REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1308 TYTQQLEDLKRQLEEEVKAKNALaHALQSARHDCDLLREQY-----EEETEAKAELQRVLSKANSEVAQwrTKYETDAIQ 1382
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKKEL-EKLEKALERVEELREKVkkykaLLKERALSKVGEIASEIFEELTE--GKYSGVRVK 767
|
....
gi 119586555 1383 RTEE 1386
Cdd:PRK03918 768 AEEN 771
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1312-1873 |
2.64e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.46 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1312 QLEDLKRQLEE-EVKAKNALAHALQSARHDCDLLREQYEEETEAKAElqrVLSKANSEVAQWRTKYEtdaiqRTEELEEA 1390
Cdd:PRK02224 188 SLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARE---TRDEADEVLEEHEERRE-----ELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1391 KKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELES 1470
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1471 SQKEARSLS--------------TELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEA 1536
Cdd:PRK02224 340 HNEEAESLRedaddleeraeelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1537 EKMELQSALEEAEASLEHEEGKIlraqlefnqikAEIERKLAE-KDEEMEQAkrnhlrVVDSLQTSLDAETRSRNEALRV 1615
Cdd:PRK02224 420 ERDELREREAELEATLRTARERV-----------EEAEALLEAgKCPECGQP------VEGSPHVETIEEDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1616 K-KKMEGDLNEMEIQLSHANRmAAEAQKQVKSLQSllkdtqiQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVE 1694
Cdd:PRK02224 483 ElEDLEEEVEEVEERLERAED-LVEAEDRIERLEE-------RREDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1695 QTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDaDLSQLQTEVEEAVQECRNAEEKAKkaitDAAMMAEELKkeq 1774
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKRE----ALAELNDERR--- 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1775 dtsahlERMKKNMEQtIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEaEQKRNAESVKGMRKSErrIKELtyq 1854
Cdd:PRK02224 627 ------ERLAEKRER-KRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELR-EERDDLQAEIGAVENE--LEEL--- 693
|
570
....*....|....*....
gi 119586555 1855 tEEDRKNLLRLQDLVDKLQ 1873
Cdd:PRK02224 694 -EELRERREALENRVEALE 711
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1254-1926 |
4.13e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1254 EDQMNEHRSKAEETQRSVNDltsQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKrqLEEEVKAKNALAHA 1333
Cdd:PTZ00121 1050 EDIDGNHEGKAEAKAHVGQD---EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGK--AEEARKAEEAKKKA 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1334 LQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKK----KLAQRLQEAEEAVEAVN 1409
Cdd:PTZ00121 1125 EDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKaeevRKAEELRKAEDARKAEA 1204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1410 AKCSSLEKT-----KHRLQNEIEDLM-VDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELF 1483
Cdd:PTZ00121 1205 ARKAEEERKaeearKAEDAKKAEAVKkAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1484 KLknayEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQ 1563
Cdd:PTZ00121 1285 KA----EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1564 lefnqiKAEIERKLAEKDEEMEQAKRNHLRVvdslqtslDAETRSRNEALRvKKKMEGDLNEMEIQLSHANRMAAEAQKQ 1643
Cdd:PTZ00121 1361 ------AAEEKAEAAEKKKEEAKKKADAAKK--------KAEEKKKADEAK-KKAEEDKKKADELKKAAAAKKKADEAKK 1425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1644 VKSLQSLLKDTQIQLDDAVRAnDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTS 1723
Cdd:PTZ00121 1426 KAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1724 LINQKKKMDadlSQLQTEVEEAVQECRNAEEKAKkaiTDAAMMAEELKKEQDTSAhLERMKKNMEQTIKDLQHRLDEAEQ 1803
Cdd:PTZ00121 1505 AAEAKKKAD---EAKKAEEAKKADEAKKAEEAKK---ADEAKKAEEKKKADELKK-AEELKKAEEKKKAEEAKKAEEDKN 1577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1804 IALKGGKKQLQKLEARVRELENELEAEQKRNAESVKgmRKSERRIK-ELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQ 1882
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 119586555 1883 AEE----AEEQANTNLSKFRKVQhELDEAEERADIAESQVNKLRAKSR 1926
Cdd:PTZ00121 1656 EEEnkikAAEEAKKAEEDKKKAE-EAKKAEEDEKKAAEALKKEAEEAK 1702
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
831-1328 |
1.02e-12 |
|
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: 73.52 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 831 KLYFKIKPLLKSA-EREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADaeercdqlI 909
Cdd:TIGR04523 121 KLEVELNKLEKQKkENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK--------I 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 910 KNKI-QLEAKVKEMNERLEDEEEMNAELT---AKKRKLEDECSELKRDIDDLELTLAKVE-------------------- 965
Cdd:TIGR04523 193 KNKLlKLELLLSNLKKKIQKNKSLESQISelkKQNNQLKDNIEKKQQEINEKTTEISNTQtqlnqlkdeqnkikkqlsek 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 966 -KEKHATENKVKNLTEEMAGLDEIIAKLTKEKKalQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKV 1044
Cdd:TIGR04523 273 qKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1045 RMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEA 1124
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1125 ERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAAL------RKKHAD 1198
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkklneeKKELEE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1199 SVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIikakaaNLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQR 1278
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD------DFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 119586555 1279 AKLQTEngelsrqLDEKEALISQLTRGKLTYTQQLEDLKRQLeEEVKAKN 1328
Cdd:TIGR04523 585 EEKQEL-------IDQKEKEKKDLIKEIEEKEKKISSLEKEL-EKAKKEN 626
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
860-1209 |
1.32e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.41 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 860 KEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDnLADAEERCDQLIKNKI---QLEAKVKEMNERLEDEEEMNAEL 936
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE-RREALQRLAEYSWDEIdvaSAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 937 takkRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEmagLDEIIAKLTKEKKALQEAHQQALDDLQAEEDK 1016
Cdd:COG4913 688 ----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE---LDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1017 VNTLTKAKVKLEQQVDDLEGSLEQ-EKKVRMDLERAKRKLEGDLKLTQESIMDLEndkqqlderlkkkdfELNALNARIE 1095
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLP---------------EYLALLDRLE 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1096 DEqalgsqlqkKLKELQARIEELEEeleaeRTARAKVEKLRSDLSRELEEISERLEEA---------GGATSVQIEMNKK 1166
Cdd:COG4913 826 ED---------GLPEYEERFKELLN-----ENSIEFVADLLSKLRRAIREIKERIDPLndslkripfGPGRYLRLEARPR 891
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 119586555 1167 REAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDN 1209
Cdd:COG4913 892 PDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1488-1925 |
1.58e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.15 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1488 AYEESLEHLETfkrenknLQEEISDLTEqlgssgkTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFN 1567
Cdd:PRK02224 245 EHEERREELET-------LEAEIEDLRE-------TIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1568 QIKAEIErKLAEKDEEMEQAKRNHLrvVDSLQTSLDAET--------RSRNEALRVK-KKMEGDLNEMEIQLSHANRMAA 1638
Cdd:PRK02224 311 AVEARRE-ELEDRDEELRDRLEECR--VAAQAHNEEAESlredaddlEERAEELREEaAELESELEEAREAVEDRREEIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1639 EAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSR---KLAE--QElIETSER 1713
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagKCPEcgQP-VEGSPH 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1714 VQLLHSQNtsliNQKKKMDADLSQLQTEVEEAvqecrnaEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTIKD 1793
Cdd:PRK02224 467 VETIEEDR----ERVEELEAELEDLEEEVEEV-------EERLERA--------EDLVEAEDRIERLEERREDLEELIAE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1794 LQHRLDEAEQialkggkkQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEE---DRKNLLRLQDLVD 1870
Cdd:PRK02224 528 RRETIEEKRE--------RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAElkeRIESLERIRTLLA 599
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119586555 1871 KLQLKVKAYKRQAEEAEEQANTN------LSKFRKVQHELDEAEERADIAESQVNKLRAKS 1925
Cdd:PRK02224 600 AIADAEDEIERLREKREALAELNderrerLAEKRERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1489-1829 |
3.86e-12 |
|
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: 71.26 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1489 YEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQsaleEAEASLEHEEGKILRAQLEFNQ 1568
Cdd:pfam05622 140 YKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1569 IKA-------EIERKLAEKD---EEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAA 1638
Cdd:pfam05622 216 LEEklealqkEKERLIIERDtlrETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1639 EAQKQvkSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRavveqtersRKLAEQElietservqllh 1718
Cdd:pfam05622 296 LGQEG--SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQ---------KALQEQG------------ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1719 SQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---T 1790
Cdd:pfam05622 353 SKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksV 432
|
330 340 350
....*....|....*....|....*....|....*....
gi 119586555 1791 IKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEA 1829
Cdd:pfam05622 433 IKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEK 471
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
835-1512 |
4.11e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.10 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 835 KIKPLLKSAEREKEMAsmKEEFTRLKEALEKSEARRKELEEKmvsllqekndlqlqvqaeqdnladaeercdqliKNKIQ 914
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKA--DAAKKKAEEAKKAAEAAKAEAEAA---------------------------------ADEAE 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 915 LEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRdiddleltlaKVEKEKHATEnKVKNLTEEMAGLDEIIAKLTK 994
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK----------KAEEDKKKAD-ELKKAAAAKKKADEAKKKAEE 1429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 995 EKKAlQEAHQQALDDLQAEEdkvntlTKAKVKLEQQVDDLEGSLEQEKKVrmdlERAKRKLEgDLKLTQESIMDLENDKQ 1074
Cdd:PTZ00121 1430 KKKA-DEAKKKAEEAKKADE------AKKKAEEAKKAEEAKKKAEEAKKA----DEAKKKAE-EAKKADEAKKKAEEAKK 1497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1075 QLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQArieeleeeleaeRTARAKVEKLRSDLSRELEEISERLEEAg 1154
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA------------DEAKKAEEKKKADELKKAEELKKAEEKK- 1564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1155 gatsvQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEfklelDDVTSN 1234
Cdd:PTZ00121 1565 -----KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKK 1634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1235 MEQIIKAKAANLEKMcrtledqmnEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLE 1314
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKA---------EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1315 DLKRQLEEEVKAKNALAHALQSARHDCDLLREQyEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEEL-----EE 1389
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeavieEE 1784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1390 AKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKilAEWKQKYEESQSELE 1469
Cdd:PTZ00121 1785 LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEAD--AFEKHKFNKNNENGE 1862
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 119586555 1470 SSQKEARSlSTELFKLKNAYEESLEHLETFKRENKNLQEEISD 1512
Cdd:PTZ00121 1863 DGNKEADF-NKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
914-1859 |
1.59e-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: 70.08 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 914 QLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKekhatenkvknLTEEMAGLDEIIAKLT 993
Cdd:TIGR00606 214 QYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMK-----------LDNEIKALKSRKKQME 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 994 KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVK-LEQQVDDLEGSLEQEKKVRMDLERAKRKLEgdlklTQESIMDLEND 1072
Cdd:TIGR00606 283 KDNSELELKMEKVFQGTDEQLNDLYHNHQRTVReKERELVDCQRELEKLNKERRLLNQEKTELL-----VEQGRLQLQAD 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1073 KQQldERLKKKDFELNALNARIE-DEQALGSQLQKKLKelQARIEELEEELEAERTARAKVEKLRSDLS---RELEEISE 1148
Cdd:TIGR00606 358 RHQ--EHIRARDSLIQSLATRLElDGFERGPFSERQIK--NFHTLVIERQEDEAKTAAQLCADLQSKERlkqEQADEIRD 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1149 RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATlqheataaalrkKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEL 1228
Cdd:TIGR00606 434 EKKGLGRTIELKKEILEKKQEELKFVIKELQQLE------------GSSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1229 DDVTSNMEQ--IIKAKAANLEKMcrtleDQMNEHRSKAEETQRSVNDLTSQRAKLQTENgelSRQLDEkeaLISQLtrGK 1306
Cdd:TIGR00606 502 EVKSLQNEKadLDRKLRKLDQEM-----EQLNHHTTTRTQMEMLTKDKMDKDEQIRKIK---SRHSDE---LTSLL--GY 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1307 LTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTkYETDAIQRTEE 1386
Cdd:TIGR00606 569 FPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQD-EESDLERLKEE 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1387 LEEAKKKLA----------QRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDL----MVDVERSNAAAAALDKKQRNFDK 1452
Cdd:TIGR00606 648 IEKSSKQRAmlagatavysQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLqsklRLAPDKLKSTESELKKKEKRRDE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1453 IL--AEWKQKYEESQSELESSQKEA-RSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLT--EQLgssgktIHEL 1527
Cdd:TIGR00606 728 MLglAPGRQSIIDLKEKEIPELRNKlQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTimERF------QMEL 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1528 EKVRKQLEAEKMELQSAleEAEASLEHEEGKILRAQLEFNQIKAEIErkLAEKDEEMEQAKRNHLRvvdSLQTSLDAETR 1607
Cdd:TIGR00606 802 KDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKIE--LNRKLIQDQQEQIQHLK---SKTNELKSEKL 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1608 SRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANddlkeniaivERRNNLLQAELE 1687
Cdd:TIGR00606 875 QIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK----------ETSNKKAQDKVN 944
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1688 ELRAVVEQTERSRKLAEQELIETSERvqllhsqntslinQKKKMDADLSQLQTEVEEAVQECRNAEE--KAKKAITDAAM 1765
Cdd:TIGR00606 945 DIKEKVKNIHGYMKDIENKIQDGKDD-------------YLKQKETELNTVNAQLEECEKHQEKINEdmRLMRQDIDTQK 1011
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1766 MAEELKKEQDTSAHLERMKKNMEQTIKdlQHrLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSE 1845
Cdd:TIGR00606 1012 IQERWLQDNLTLRKRENELKEVEEELK--QH-LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFK 1088
|
970
....*....|....
gi 119586555 1846 RRIKELTYQTEEDR 1859
Cdd:TIGR00606 1089 KELREPQFRDAEEK 1102
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
861-1659 |
1.84e-11 |
|
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: 69.61 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 861 EALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDnlaDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAK- 939
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTL---CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKr 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 940 -----KRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKnlteemagldeiIAKLTKEKKALQEAHQQALDDLQAEE 1014
Cdd:TIGR00618 250 eaqeeQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK------------AAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1015 DKVNTLTKAKVKLEQQVDDlEGSLEQEKKVRMDLERAKRKLEgDLKLTQESIMDLENDKQQLDERLKKKDFELNALnari 1094
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQ-QSSIEEQRRLLQTLHSQEIHIR-DAHEVATSIREISCQQHTLTQHIHTLQQQKTTL---- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1095 EDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKlrsdlSRELEEISERLEEAGGATSVQIEmnKKREAEFQKM 1174
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKK-----QQELQQRYAELCAAAITCTAQCE--KLEKIHLQES 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1175 RRDLEEATlQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDvtsnmeqiikakAANLEKMCRTLE 1254
Cdd:TIGR00618 465 AQSLKERE-QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQD------------IDNPGPLTRRMQ 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1255 DQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRgkltYTQQLEDLkRQLEEEVKaknalahal 1334
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR----SKEDIPNL-QNITVRLQ--------- 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1335 qsarhdcDLLREQYEEETEAKAELQRVLSKANSEVAqwrtKYETDAIQRTEELEEAKKKLAqrlqeaeeaveavnakcss 1414
Cdd:TIGR00618 598 -------DLTEKLSEAEDMLACEQHALLRKLQPEQD----LQDVRLHLQQCSQELALKLTA------------------- 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1415 lektkhrLQNEIEDLMVDVERSNAAAAALDKKQRnfdkilaewkqkyeesqselessqkeARSLSTELFKLKNAYEESLE 1494
Cdd:TIGR00618 648 -------LHALQLTLTQERVREHALSIRVLPKEL--------------------------LASRQLALQKMQSEKEQLTY 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1495 HLETFKRENKNLQEEIsdltEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIE 1574
Cdd:TIGR00618 695 WKEMLAQCQTLLRELE----THIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV 770
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1575 RKLAEKDEEMEQAKRNHLRVVDSLQTSLdAETRSRNEALRVKKKMEGDLNEMEIQLshanrmAAEAQKQVKSLQSLLKDT 1654
Cdd:TIGR00618 771 TAALQTGAELSHLAAEIQFFNRLREEDT-HLLKTLEAEIGQEIPSDEDILNLQCET------LVQEEEQFLSRLEEKSAT 843
|
....*
gi 119586555 1655 QIQLD 1659
Cdd:TIGR00618 844 LGEIT 848
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1311-1848 |
2.60e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1311 QQLEDLKRQLEEEVKAKNALAHALQSArhdcdllrEQYEEETEAKAELQRVLSKANSEVAQwrTKYETdAIQRTEELEEA 1390
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELA--------ERYAAARERLAELEYLRAALRLWFAQ--RRLEL-LEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1391 KKKLAQRLQEAEEAVEAVNAKCSSLE--------KTKHRLQNEIEDLMVDVERSNAAAAALDKKQRN-----------FD 1451
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAAlglplpasaeeFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1452 KILAEWKQkyeesqselessqkEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEIsdltEQLGSSGKTI-HELEKV 1530
Cdd:COG4913 384 ALRAEAAA--------------LLEALEEELEALEEALAEAEAALRDLRRELRELEAEI----ASLERRKSNIpARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1531 RKQLE-------------AEKMEL-------QSALEEA---------------EASLEHEEGKILRAQLEFNQIKAeier 1575
Cdd:COG4913 446 RDALAealgldeaelpfvGELIEVrpeeerwRGAIERVlggfaltllvppehyAAALRWVNRLHLRGRLVYERVRT---- 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1576 klAEKDEEMEQAKRNHL-RVVDS----LQTSLDAETRSRNEALRVkkkmegdlnEMEIQLSHAnRMAAEAQKQVKSLQSL 1650
Cdd:COG4913 522 --GLPDPERPRLDPDSLaGKLDFkphpFRAWLEAELGRRFDYVCV---------DSPEELRRH-PRAITRAGQVKGNGTR 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1651 L-KDTQIQLD-------DAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAE--QELIETSERVQLLHSQ 1720
Cdd:COG4913 590 HeKDDRRRIRsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAERE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1721 NTSLINQKKKMDA---DLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELkkeqdtsahlermkKNMEQTIKDLQHR 1797
Cdd:COG4913 670 IAELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL--------------EQAEEELDELQDR 735
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 119586555 1798 LDEAEQIALKGGKKQLQKL------EARVRELENELEAEQKRNAESvkgMRKSERRI 1848
Cdd:COG4913 736 LEAAEDLARLELRALLEERfaaalgDAVERELRENLEERIDALRAR---LNRAEEEL 789
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
840-1256 |
2.93e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 840 LKSAERE-KEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQD--NLADAEERCDQLIKNKIQLE 916
Cdd:COG4717 73 LKELEEElKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 917 AKVKEMNERLEDEEEMNAELTAKKRKLEDEC-----------SELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL 985
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 986 DEIIAKLTKEKKALQE-----------AHQQALDDLQAEEDKV---------------NTLTKAKVKLEQQVDDLEGSLE 1039
Cdd:COG4717 233 ENELEAAALEERLKEArlllliaaallALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1040 QEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKkdfelnalnARIEDEQALGSQLQKKLKELQARIEELE 1119
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE---------AEELEEELQLEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1120 EELEAertARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKR--EAEFQKMRRDLEEATLQHEataaALRKKHA 1197
Cdd:COG4717 384 EEELR---AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELE----ELREELA 456
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119586555 1198 DSVAELG--EQIDNLQRVKQKLEKEKSEFKLELDDVtsnmeQIIKAKAANLEKMCRTLEDQ 1256
Cdd:COG4717 457 ELEAELEqlEEDGELAELLQELEELKAELRELAEEW-----AALKLALELLEEAREEYREE 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1474-1932 |
2.97e-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: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1474 EARSLSTELFKLKNAYEESLEhletfKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEasLE 1553
Cdd:COG4913 226 AADALVEHFDDLERAHEALED-----AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1554 HEEGKILRAQLEFNQIKAEIERkLAEKDEEMEQAKRNH-LRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSH 1632
Cdd:COG4913 299 ELRAELARLEAELERLEARLDA-LREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1633 A----NRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEN-------IAIVERRNNLLQAELEELRAVVEqteRSRK 1701
Cdd:COG4913 378 SaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRElreleaeIASLERRKSNIPARLLALRDALA---EALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1702 LAEQ------ELIETS----------ERVqlLHSQNTSL-------------INQKK----------------------- 1729
Cdd:COG4913 455 LDEAelpfvgELIEVRpeeerwrgaiERV--LGGFALTLlvppehyaaalrwVNRLHlrgrlvyervrtglpdperprld 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1730 ------KMDADLSQLQTEVEEAVQE------CRNAEE--KAKKAITDAAMMAeelkkeQDTSAHlermkknmeqtIKDLQ 1795
Cdd:COG4913 533 pdslagKLDFKPHPFRAWLEAELGRrfdyvcVDSPEElrRHPRAITRAGQVK------GNGTRH-----------EKDDR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1796 HRLDEAEQIalkGG--KKQLQKLEARVRELENELEAEQKRnaesvkgMRKSERRIKELtyqteEDRKNLLRLQDLVDKLQ 1873
Cdd:COG4913 596 RRIRSRYVL---GFdnRAKLAALEAELAELEEELAEAEER-------LEALEAELDAL-----QERREALQRLAEYSWDE 660
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119586555 1874 LKVKAYKRQAEEAEEQ---ANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKR 1932
Cdd:COG4913 661 IDVASAEREIAELEAElerLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL 722
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
851-1429 |
3.35e-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: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 851 SMKEEFTRLKEA---LEKSEARRK---ELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKI-QLEAKVKEMN 923
Cdd:COG4913 229 ALVEHFDDLERAheaLEDAREQIEllePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELeELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 924 ERLEDEEEMNAELTAKKRKLEDECSELK-RDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEA 1002
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1003 HQQALDDLQAEEDKV-NTLTKAKVKLEQQVDDLEgSLEQE------KKVRMD--LERAKRKLEGDLKLTQESIM---DLe 1070
Cdd:COG4913 389 AAALLEALEEELEALeEALAEAEAALRDLRRELR-ELEAEiaslerRKSNIParLLALRDALAEALGLDEAELPfvgEL- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1071 ndkqqLDERLKKKDFElNALnariedEQALGSQ----L--QKKLKE---------LQARIEELEEELEAERTARAK---- 1131
Cdd:COG4913 467 -----IEVRPEEERWR-GAI------ERVLGGFaltlLvpPEHYAAalrwvnrlhLRGRLVYERVRTGLPDPERPRldpd 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1132 --VEKLRSDLSRELEEISERLEEAGGATSV-----------------QIEMNKKReaeFQK-MRRDLEE----------- 1180
Cdd:COG4913 535 slAGKLDFKPHPFRAWLEAELGRRFDYVCVdspeelrrhpraitragQVKGNGTR---HEKdDRRRIRSryvlgfdnrak 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1181 -ATLQHEATAAALRKKHADS-VAELGEQIDNLQRVKQKLEKEKSEFKLELD------DVTSNMEQIIKAKAANLEkmCRT 1252
Cdd:COG4913 612 lAALEAELAELEEELAEAEErLEALEAELDALQERREALQRLAEYSWDEIDvasaerEIAELEAELERLDASSDD--LAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1253 LEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLT-RGKLTYTQQLEDLKRQLEEEvKAKNALA 1331
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdLARLELRALLEERFAAALGD-AVERELR 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1332 HALQSARHDCDLLREQYEEETEAKaeLQRVLSKANSEVAQWRTKYET----DAI---QRTEELEEAKKKLAQRLQEAEEa 1404
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERA--MRAFNREWPAETADLDADLESlpeyLALldrLEEDGLPEYEERFKELLNENSI- 845
|
650 660
....*....|....*....|....*
gi 119586555 1405 vEAVNAKCSSLEKTKHRLQNEIEDL 1429
Cdd:COG4913 846 -EFVADLLSKLRRAIREIKERIDPL 869
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
843-1301 |
4.04e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.53 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 843 AEREKEMASMKEEFTRLKEALEKSEARRKELEEKM-------VSLLQEKNDLQLQVQAEQDNLAD-------AEERCDQL 908
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEEcrvaaqaHNEEAESL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 909 IKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEI 988
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 989 IAKLTKEKKALQEAHQQALDDLQA---------------------EEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRmD 1047
Cdd:PRK02224 428 EAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetieeDRERVEELEAELEDLEEEVEEVEERLERAEDLV-E 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1048 LERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERT 1127
Cdd:PRK02224 507 AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1128 ARAKVEKLRSDLSrELEEISERLEEAGGATSVQIEMNKKRE---AEFQKMRRDLEEATLQHEATAAALRKKHADS-VAEL 1203
Cdd:PRK02224 587 RIESLERIRTLLA-AIADAEDEIERLREKREALAELNDERRerlAEKRERKRELEAEFDEARIEEAREDKERAEEyLEQV 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1204 GEQIDNLQRVKQKLEKEKSEFKLELDDVTSnmeqiIKAKAANLEKMCRTLEDQMNEhrskAEETQRSVNDLtsqRAKLQT 1283
Cdd:PRK02224 666 EEKLDELREERDDLQAEIGAVENELEELEE-----LRERREALENRVEALEALYDE----AEELESMYGDL---RAELRQ 733
|
490
....*....|....*....
gi 119586555 1284 EN-GELSRQLDEKEALISQ 1301
Cdd:PRK02224 734 RNvETLERMLNETFDLVYQ 752
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
901-1140 |
4.26e-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: 67.10 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 901 AEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTE 980
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 981 EMAGLDEIIAKLTKekkALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLK 1060
Cdd:COG4942 98 ELEAQKEELAELLR---ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1061 LTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIE--ELEEELEAERTARAKVEKLRSD 1138
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIArlEAEAAAAAERTPAAGFAALKGK 254
|
..
gi 119586555 1139 LS 1140
Cdd:COG4942 255 LP 256
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
844-1259 |
1.08e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.97 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 844 EREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMN 923
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 924 ERLEDE--EEMNAELTAKKRKLE-----------------DECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAG 984
Cdd:TIGR04523 302 NQKEQDwnKELKSELKNQEKKLEeiqnqisqnnkiisqlnEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 985 LDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQ--------------VDDLEGSLEQEKKVRMDLER 1050
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEierlketiiknnseIKDLTNQDSVKELIIKNLDN 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1051 AKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIedeqalgSQLQKKLKELQARIEELEEELEAERTARA 1130
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK-------KELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1131 KVEKLRSDLSRELEEISERLEEAGGATSVQ-----IEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHAD---SVAE 1202
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKENLEKEIDeknkeIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEkekKISS 614
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119586555 1203 LGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQI------IKAKAANLEKMCRTLEDQMNE 1259
Cdd:TIGR04523 615 LEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIketikeIRNKWPEIIKKIKESKTKIDD 677
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
841-1152 |
1.23e-10 |
|
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: 67.02 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVK 920
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 921 EMNERLEDEEEMNA-----ELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKE 995
Cdd:TIGR02169 776 KLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 996 KKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQ 1075
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1076 LD--------------------ERLKKKDFELNAL---NARIEDEQAlgsQLQKKLKELQARIEELEEELEAERTARAKV 1132
Cdd:TIGR02169 936 IEdpkgedeeipeeelsledvqAELQRVEEEIRALepvNMLAIQEYE---EVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
330 340
....*....|....*....|.
gi 119586555 1133 EKLRSDLSRE-LEEISERLEE 1152
Cdd:TIGR02169 1013 EKKKREVFMEaFEAINENFNE 1033
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
847-1696 |
1.64e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.52 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 847 KEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQliKNKIQ--------LEAK 918
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQ--QEKIEryqadleeLEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 919 VKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDL-------------------------------ELTLAKVEKE 967
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYqqaldvqqtraiqyqqavqalerakqlcglpDLTADNAEDW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 968 KHATENKVKNLTEEMAGL-------DEIIAKLTKEKKALQ---------EAHQQALDDL-QAEEDKVntLTKAKVKLEQQ 1030
Cdd:PRK04863 444 LEEFQAKEQEATEELLSLeqklsvaQAAHSQFEQAYQLVRkiagevsrsEAWDVARELLrRLREQRH--LAEQLQQLRMR 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1031 VDDLEGSLEQEKkvrmDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKkkdfelnALNARIEDEQALGSQLQKKLKE 1110
Cdd:PRK04863 522 LSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE-------SLSESVSEARERRMALRQQLEQ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1111 LQARIEELEEELEAERTARAKVEKLRSDLSRELEEiSERLEEAggatsvqiemnkkreaeFQKMRRDLEEATLQHEATAA 1190
Cdd:PRK04863 591 LQARIQRLAARAPAWLAAQDALARLREQSGEEFED-SQDVTEY-----------------MQQLLERERELTVERDELAA 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1191 ALRkkhadsvaELGEQIDNLQ--------RVKQKLEKEKSEFKLEL-DDVTSN------------MEQII----KAKAAN 1245
Cdd:PRK04863 653 RKQ--------ALDEEIERLSqpggsedpRLNALAERFGGVLLSEIyDDVSLEdapyfsalygpaRHAIVvpdlSDAAEQ 724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1246 LEKMCRTLED---------QMNEHRSKAEETQRSVNDLTSQRAklqtengelSRqldekealISQLTR----GKLTYTQQ 1312
Cdd:PRK04863 725 LAGLEDCPEDlyliegdpdSFDDSVFSVEELEKAVVVKIADRQ---------WR--------YSRFPEvplfGRAAREKR 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1313 LEDLKRQLEEEVkaknalahalqsarhdcdllrEQYEEETEAKAELQRVLSKANSEVA-------QWRTKYETDAIQRT- 1384
Cdd:PRK04863 788 IEQLRAEREELA---------------------ERYATLSFDVQKLQRLHQAFSRFIGshlavafEADPEAELRQLNRRr 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1385 -------EELEEAKKKLAQRLQEAEEAVEAVN--AKCSSLEKTKHrLQNEIEDLMVDVERSNAAAAALDKKQRNFDKI-- 1453
Cdd:PRK04863 847 veleralADHESQEQQQRSQLEQAKEGLSALNrlLPRLNLLADET-LADRVEEIREQLDEAEEAKRFVQQHGNALAQLep 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1454 -----------LAEWKQKYEESQSELESSQKEARSLsTELFKLKN--AYEESLEHLetfkrenknlqEEISDLTEQLgss 1520
Cdd:PRK04863 926 ivsvlqsdpeqFEQLKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAhfSYEDAAEML-----------AKNSDLNEKL--- 990
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1521 gktiheleKVR-KQLEAEKMELQSALEEAEAslEHEEGKILRAQLE-----FNQIKAEIERKLAE----KDEEMEQAKRN 1590
Cdd:PRK04863 991 --------RQRlEQAEQERTRAREQLRQAQA--QLAQYNQVLASLKssydaKRQMLQELKQELQDlgvpADSGAEERARA 1060
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1591 HlrvVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQV----KSLQSLLKdtqiqlddAVRAND 1666
Cdd:PRK04863 1061 R---RDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVvnakAGWCAVLR--------LVKDNG 1129
|
970 980 990
....*....|....*....|....*....|....*
gi 119586555 1667 dlkeniaiVERRnnLLQAEL-----EELRAVVEQT 1696
Cdd:PRK04863 1130 --------VERR--LHRRELaylsaDELRSMSDKA 1154
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1482-1910 |
1.77e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1482 LFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAE------ASLEHE 1555
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkeeiEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1556 EGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNhLRVVDSLQTslDAETRSRNEALRVKKKMEgdLNEMEIQLSHANR 1635
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKE--KAEEYIKLSEFYEEYLDE--LREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1636 MAAEAQKQVKSLQSLLKDTQiqlddavrandDLKENIAIVERRNNLLQA---ELEELRAVVEQTERSRK-LAEQELIETS 1711
Cdd:PRK03918 322 EINGIEERIKELEEKEERLE-----------ELKKKLKELEKRLEELEErheLYEEAKAKKEELERLKKrLTGLTPEKLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1712 ERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAvqecRNAEEKAKKAITDAAMMAEELKKEqdtsaHLERMKKNMEQTI 1791
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKEL----KKAIEELKKAKGKCPVCGRELTEE-----HRKELLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1792 KDLQHRLDEAEqialkggkKQLQKLEARVRELENELEAEQK--RNAESVKGMRKSERRIKELTYQT-EEDRKNLLRLQDL 1868
Cdd:PRK03918 462 KRIEKELKEIE--------EKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEK 533
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 119586555 1869 VDKLQLKVKAYKRQAEEAEEQANtnlsKFRKVQHELDEAEER 1910
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEE 571
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
841-1152 |
2.02e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVK 920
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 921 EMNERLEDEEEMNAE-------LTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLtEEMAGLDEIIAKLT 993
Cdd:PRK02224 437 TARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLE 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 994 KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDL-EGSLEQEKKVRMDLERAKrKLEGDLKLTQESIMDLEND 1072
Cdd:PRK02224 516 ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKrEAAAEAEEEAEEAREEVA-ELNSKLAELKERIESLERI 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1073 KQQLDERLKKKDfELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDlsRELEEISERLEE 1152
Cdd:PRK02224 595 RTLLAAIADAED-EIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAE--EYLEQVEEKLDE 671
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1104-1754 |
2.47e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 65.90 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1104 LQKKLKELQARIEELEEELEAERTArakveklRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDL---EE 1180
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKA-------IQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCarsAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1181 ATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSE--FKLELD-DVTSNMEQIIKAKAANLEKMCRTLEDQM 1257
Cdd:pfam05483 170 KTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEmhFKLKEDhEKIQHLEEEYKKEINDKEKQVSLLLIQI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1258 NEHRSKA-------EETQRSVNDLtSQRAKLQTENgelsrqldekealISQLTRGKLTYTQQLEDLKRQLEEEVKAKNAL 1330
Cdd:pfam05483 250 TEKENKMkdltfllEESRDKANQL-EEKTKLQDEN-------------LKELIEKKDHLTKELEDIKMSLQRSMSTQKAL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1331 AHALQSA-RHDCDLLRE---QYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQ----EAE 1402
Cdd:pfam05483 316 EEDLQIAtKTICQLTEEkeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QRLEKNEDQLKIITMELQkkssELE 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1403 EAVEAVNAKCSSLEKTKHRLqNEIEDLMVDVERSNAAAAALDKKQRNF-------DKILAEWKQKYEESQSELESSQKEA 1475
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKIL-AEDEKLLDEKKQFEKIAEELKGKEQELifllqarEKEIHDLEIQLTAIKTSEEHYLKEV 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1476 RSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTI----HELEKVRKQ---LEAEKMELQSALEEA 1548
Cdd:pfam05483 474 EDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIinckKQEERMLKQienLEEKEMNLRDELESV 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1549 EASL--EHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEG-DLNE 1625
Cdd:pfam05483 554 REEFiqKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENkQLNA 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1626 MEIQLSHANRMAAEAQKQ----VKSLQSLLKDTQIQ----LDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTE 1697
Cdd:pfam05483 634 YEIKVNKLELELASAKQKfeeiIDNYQKEIEDKKISeeklLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHK 713
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119586555 1698 RS------RKLAEQELIETSERVQ--LLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEE 1754
Cdd:pfam05483 714 HQydkiieERDSELGLYKNKEQEQssAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
914-1344 |
2.63e-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: 65.30 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 914 QLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 993
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 994 KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDK 1073
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1074 QQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSreleeiserleEA 1153
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS-----------SM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1154 GGATSvqiemnkKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKlelddvts 1233
Cdd:pfam07888 264 AAQRD-------RTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQ-------- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1234 NMEQIIKAKAANLEKMCRTLEDQMNEHRSKAEETQRsvnDLTSQRAKLQTENGELSRQLDEKEALisqltrgkLTYTQQL 1313
Cdd:pfam07888 329 RLEERLQEERMEREKLEVELGREKDCNRVQLSESRR---ELQELKASLRVAQKEKEQLQAEKQEL--------LEYIRQL 397
|
410 420 430
....*....|....*....|....*....|.
gi 119586555 1314 EdlkRQLEEEVKAKNALAHALQSARHDCDLL 1344
Cdd:pfam07888 398 E---QRLETVADAKWSEAALTSTERPDSPLS 425
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1038-1448 |
3.31e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1038 LEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQalgsqLQKKLKELQARIEE 1117
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-----LEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1118 LEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHA 1197
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1198 DSVAELgeqidNLQRVKQKLEKEKSEFKL---------ELDDVTSNMEQIIKAKAANLEKMCRTLEDQMNEHRSKAEETQ 1268
Cdd:COG4717 231 QLENEL-----EAAALEERLKEARLLLLIaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1269 RSvnDLTSQRAKLQTEngELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALahALQSARHDCDLLREQY 1348
Cdd:COG4717 306 EL--QALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1349 ----EEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKK-LAQRLQEAEEAVEAVNAKCSSLEKTKHRLQ 1423
Cdd:COG4717 380 gvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeLEEELEELEEELEELEEELEELREELAELE 459
|
410 420
....*....|....*....|....*
gi 119586555 1424 NEIEDLMVDVERSNAAAAALDKKQR 1448
Cdd:COG4717 460 AELEQLEEDGELAELLQELEELKAE 484
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1478-1924 |
3.38e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.43 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1478 LSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEA---EASLEH 1554
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIknkLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1555 ---------EEGKILRAQL-----EFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQ------TSLDAETRSRNEALR 1614
Cdd:TIGR04523 202 llsnlkkkiQKNKSLESQIselkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDeqnkikKQLSEKQKELEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1615 VKKKMEGDLNEMEIQLSHANRMAA-----EAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEEL 1689
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1690 RAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEE 1769
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1770 LKKEQDTSAHLERMKKNMEQTIKDLQHRLD-------------EAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAE 1836
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqnlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1837 SVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQL-KVKAYKRQAEEAEEQANTNLSKfrkvqhELDEAEERADIAE 1915
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLeKEIDEKNKEIEELKQTQKSLKK------KQEEKQELIDQKE 595
|
....*....
gi 119586555 1916 SQVNKLRAK 1924
Cdd:TIGR04523 596 KEKKDLIKE 604
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
967-1670 |
4.52e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 967 EKHATENKVKNLTEEMAGLDEIiakltkeKKALQEAHQQaLDDLQAEEDKVNTLTKAKVKLEQQVDDLEgsleqekkvRM 1046
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERA-------HEALEDAREQ-IELLEPIRELAERYAAARERLAELEYLRA---------AL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1047 DLERAKRKLEgdlkLTQESIMDLENDKQQLDERLKKKDFELNALNARIED-EQALGSQLQKKLKELQARIEELeeeleae 1125
Cdd:COG4913 282 RLWFAQRRLE----LLEAELEELRAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERL------- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1126 RTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnkkrEAEFQKMRRDLEEATlqheATAAALRKKHADSVAELGE 1205
Cdd:COG4913 351 ERELEERERRRARLEALLAALGLPLPAS--------------AEEFAALRAEAAALL----EALEEELEALEEALAEAEA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1206 QIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKAANLEKMcrtlEDQMN------EHRSKAEETQRSVND-LTSQR 1278
Cdd:COG4913 413 ALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD----EAELPfvgeliEVRPEEERWRGAIERvLGGFA 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1279 AKLqtengeLSRQLDEKEAL--ISQL-TRGKLTYtQQLEDLKRQLEEEVKAKNALAHALQSARHDC-DLLREQYEEET-- 1352
Cdd:COG4913 489 LTL------LVPPEHYAAALrwVNRLhLRGRLVY-ERVRTGLPDPERPRLDPDSLAGKLDFKPHPFrAWLEAELGRRFdy 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1353 ---EAKAELQRV--------LSKANSEVAQ------WRTKYET--DAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCS 1413
Cdd:COG4913 562 vcvDSPEELRRHpraitragQVKGNGTRHEkddrrrIRSRYVLgfDNRAKLAALEAELAELEEELAEAEERLEALEAELD 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1414 SLEKTKHRLQN--EIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQkyeesqselessqkearsLSTELFKLKNAYEE 1491
Cdd:COG4913 642 ALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDASSDDLAA------------------LEEQLEELEAELEE 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1492 SLEHLETFKRENKNLQEEISDLTEqlgssgktihELEKVRKQLE-AEKMELQSALEEAEASLEHEEGKILRAQL--EFNQ 1568
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEE----------ELDELQDRLEaAEDLARLELRALLEERFAAALGDAVERELreNLEE 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1569 IKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGD------------LNEMEIQ-----LS 1631
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDglpeyeerfkelLNENSIEfvadlLS 853
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 119586555 1632 HANRMAAEAQKQVKSLQSLLK------DTQIQLDDAVRANDDLKE 1670
Cdd:COG4913 854 KLRRAIREIKERIDPLNDSLKripfgpGRYLRLEARPRPDPEVRE 898
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1424-1928 |
4.76e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1424 NEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSlSTELFKLKNAYE-ESLEHLETFKRE 1502
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARK-AEDARKAEEARKaEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1503 NKNLQEEISDLTEQlGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASleHEEGKILRAQLEFNQIKAEIERKLAEKDE 1582
Cdd:PTZ00121 1161 EDARKAEEARKAED-AKKAEAARKAEEVRKAEELRKAEDARKAEAARKA--EEERKAEEARKAEDAKKAEAVKKAEEAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1583 EMEQAKR----NHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDlnemEIQLSHANRMAAEAQK--QVKSLQSLLKDTQi 1656
Cdd:PTZ00121 1238 DAEEAKKaeeeRNNEEIRKFEEARMAHFARRQAAIKAEEARKAD----ELKKAEEKKKADEAKKaeEKKKADEAKKKAE- 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1657 qlddAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSlinQKKKMDadls 1736
Cdd:PTZ00121 1313 ----EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE---AKKKAD---- 1381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1737 qlqtEVEEAVQECRNAEEKAKKAITDAAMmAEELKKEQDTSAHLERMKKNMEQTIKdlqhrLDEAEQialkggkkqlqKL 1816
Cdd:PTZ00121 1382 ----AAKKKAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKK-----ADEAKK-----------KA 1440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1817 EARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKnllrlqdlVDKLQLKVKAYKRQAEEAE--EQANTNL 1894
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK--------ADEAKKKAEEAKKKADEAKkaAEAKKKA 1512
|
490 500 510
....*....|....*....|....*....|....*....
gi 119586555 1895 SKFRKVQH-----ELDEAEERADIAESQVNKLRAKSRDI 1928
Cdd:PTZ00121 1513 DEAKKAEEakkadEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
839-1259 |
6.16e-10 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 64.46 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 839 LLKSAEREKEMAS----------MKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQL 908
Cdd:pfam10174 264 LLHTEDREEEIKQmevykshskfMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 909 iknkiqlEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEI 988
Cdd:pfam10174 344 -------QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 989 IAKLTKEKKALQEAHQQA------LDDLQAEEDKV-NTLTKAKVKLEQQVDDlegSLEQEKKVRMDLERAKRKLEGDLKL 1061
Cdd:pfam10174 417 LAGLKERVKSLQTDSSNTdtalttLEEALSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1062 TQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQarieeleeelEAERTARAKVEklRSDLSR 1141
Cdd:pfam10174 494 KESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH----------NAEEAVRTNPE--INDRIR 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1142 ELE-EISERLEEAGGA-TSVQIEMNKKREAEFQKMRRDLEEATLQHEATAA----------------ALRKKHADSVAEL 1203
Cdd:pfam10174 562 LLEqEVARYKEESGKAqAEVERLLGILREVENEKNDKDKKIAELESLTLRQmkeqnkkvanikhgqqEMKKKGAQLLEEA 641
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119586555 1204 GEQIDNLQRVKQKLEKEK-----SEFKLELDDVT---SNMEQIIKAKAANLEKMCRTLEDQMNE 1259
Cdd:pfam10174 642 RRREDNLADNSQQLQLEElmgalEKTRQELDATKarlSSTQQSLAEKDGHLTNLRAERRKQLEE 705
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
862-1568 |
8.50e-10 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 64.07 E-value: 8.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 862 ALEKSEARRKE-LEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKK 940
Cdd:pfam10174 46 ALRKEEAARISvLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 941 RKLEDECSELKRDIDDLELtlaKVEKEKHATENKvknlteemaglDEIIAKLtkekkaLQEAHQQALDDLQAEEDkvNTL 1020
Cdd:pfam10174 126 ERQAKELFLLRKTLEEMEL---RIETQKQTLGAR-----------DESIKKL------LEMLQSKGLPKKSGEED--WER 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1021 TKAKVKLEQQVDDLEGSLEQEKKVRMDL-ERAKRKLEGDLKLTQESIMdlendkQQLDERLKKKDFELNALNARIEDE-Q 1098
Cdd:pfam10174 184 TRRIAEAEMQLGHLEVLLDQKEKENIHLrEELHRRNQLQPDPAKTKAL------QTVIEMKDTKISSLERNIRDLEDEvQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1099 ALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSR---ELEEISERLEEAGGATS---VQIEMNKKREAEfq 1172
Cdd:pfam10174 258 MLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKkesELLALQTKLETLTNQNSdckQHIEVLKESLTA-- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1173 kmrRDLEEATLQHEATAAALRKKHADSVaeLGEQIDNLQRvkqkLEKEKSEFKLELDDVtSNMEQIIKAKAANLEKMCRT 1252
Cdd:pfam10174 336 ---KEQRAAILQTEVDALRLRLEEKESF--LNKKTKQLQD----LTEEKSTLAGEIRDL-KDMLDVKERKINVLQKKIEN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1253 LEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLtrgkltyTQQLEDLKRQLEEEVKaknALAH 1332
Cdd:pfam10174 406 LQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERL-------KEQREREDRERLEELE---SLKK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1333 ALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKK-----KLAQRLQEAEEAVEA 1407
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKlenqlKKAHNAEEAVRTNPE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1408 VNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELfKLKN 1487
Cdd:pfam10174 556 INDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEM-KKKG 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1488 AYEESLEHLETFKRENKNLQEEISDLTEqlgssgktihELEKVRKQLEAEKMEL---QSALEEAEA---SLEHEEGKILR 1561
Cdd:pfam10174 635 AQLLEEARRREDNLADNSQQLQLEELMG----------ALEKTRQELDATKARLsstQQSLAEKDGhltNLRAERRKQLE 704
|
....*..
gi 119586555 1562 AQLEFNQ 1568
Cdd:pfam10174 705 EILEMKQ 711
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1616-1837 |
9.29e-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: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1616 KKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQ 1695
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1696 TER--SRKLAEQELIETSERVQLLHSQNTS--LINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELK 1771
Cdd:COG4942 102 QKEelAELLRALYRLGRQPPLALLLSPEDFldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119586555 1772 KEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKRNAES 1837
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1441-1881 |
1.11e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1441 AALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLtEQLGSS 1520
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1521 GKTIHELEKVRKQLEAEKMELQsALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQT 1600
Cdd:COG4717 128 LPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1601 SLDAETRSRNEALRVKKKMEGDLNEMEIQLshanrMAAEAQKQVKSLQSLLK--DTQIQLDDAVRANDDLKENIA----- 1673
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARLLLLiaAALLALLGLGGSLLSLILTIAgvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1674 ------IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQ 1747
Cdd:COG4717 282 vlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1748 ECRNAEEKAKKA----------ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALkggKKQLQKLE 1817
Cdd:COG4717 362 ELQLEELEQEIAallaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL---EEELEELE 438
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119586555 1818 ARVRELENELEAEQKRnaesvkgMRKSERRIKELTyQTEEDRKNLLRLQDLVDKLQLKVKAYKR 1881
Cdd:COG4717 439 EELEELEEELEELREE-------LAELEAELEQLE-EDGELAELLQELEELKAELRELAEEWAA 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1102-1338 |
2.54e-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: 61.32 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1102 SQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnkkrEAEFQKMRRDLEEA 1181
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------------EQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1182 TLQheatAAALRKKHADSVAELGEQIDNLQRVKQKlekEKSEFKLELDDV--TSNMEQIIKAKAANLEKMCRTLEDQMNE 1259
Cdd:COG4942 89 EKE----IAELRAELEAQKEELAELLRALYRLGRQ---PPLALLLSPEDFldAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119586555 1260 HRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSAR 1338
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1488-1932 |
3.22e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1488 AYEESLEHLETFKRENKNLQEEISDLTEQLGSSgktihelEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFN 1567
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKTETGKAEEARKAEEAKKKA-------EDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1568 qiKAEIERKlAEKDEEMEQAKRnhlrvvdSLQTSLDAETRSRNEAlrvkKKMEGDLNEMEIQLSHANRMAAEAQK--QVK 1645
Cdd:PTZ00121 1165 --KAEEARK-AEDAKKAEAARK-------AEEVRKAEELRKAEDA----RKAEAARKAEEERKAEEARKAEDAKKaeAVK 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1646 SLQSLLKDTQiqldDAVRANddlKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNtsli 1725
Cdd:PTZ00121 1231 KAEEAKKDAE----EAKKAE---EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE---- 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1726 nQKKKMDadlsqlqtEVEEAVQECRNAEEKAKKAiTDAAMMAEELKKEQdtsahlERMKKNMEQTIKDLQHRLDEAEQIA 1805
Cdd:PTZ00121 1300 -EKKKAD--------EAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKA------EEAKKAAEAAKAEAEAAADEAEAAE 1363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1806 LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQlKVKAYKRQAEE 1885
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEE 1442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 119586555 1886 AE--EQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKR 1932
Cdd:PTZ00121 1443 AKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
831-1145 |
7.87e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 831 KLYFKIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIK 910
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 911 NKIQLEAKVKEMNERLedeeemnAELTAKKRKLEDEC-SELKRDIDDLE------LTLAKVEKEKHATENKVKNLTEEma 983
Cdd:PRK03918 557 KLAELEKKLDELEEEL-------AELLKELEELGFESvEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEE-- 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 984 gLDEIIAKLTKEKKALQEAHQQaLDDLQAEEDKvntltkakvkleqqvDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQ 1063
Cdd:PRK03918 628 -LDKAFEELAETEKRLEELRKE-LEELEKKYSE---------------EEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1064 ESIMDLENDKQQLDERLKKKDfELNALNARIEDEQAlgsqLQKKLKELQARIeeleeeleaERTARAKVEKLRSDLSREL 1143
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKK-ELEKLEKALERVEE----LREKVKKYKALL---------KERALSKVGEIASEIFEEL 756
|
..
gi 119586555 1144 EE 1145
Cdd:PRK03918 757 TE 758
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
858-1327 |
8.51e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.89 E-value: 8.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 858 RLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERL----EDEEEMN 933
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLkeliEKKDHLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 934 AELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAE 1013
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1014 EDKVNTLTkakVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIM------DLENDKQQLDERLKKKDFEL 1087
Cdd:pfam05483 376 EDQLKIIT---MELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfekiaeELKGKEQELIFLLQAREKEI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1088 NALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEaggaTSVQIEMNKKR 1167
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKK----HQEDIINCKKQ 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1168 EAEFQKMRRDLEEATLQheataaaLRkkhadsvaelgeqiDNLQRVKQKLEKEKSEFKLELDDVTSNMEQiIKAKAANLE 1247
Cdd:pfam05483 529 EERMLKQIENLEEKEMN-------LR--------------DELESVREEFIQKGDEVKCKLDKSEENARS-IEYEVLKKE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1248 KMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAK 1327
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
945-1152 |
1.07e-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: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 945 DECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQeahqqalDDLQAEEDKVNTLTKAK 1024
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-------QELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1025 VKLEQQVDDLEGSLEQEKKVrmdLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQL 1104
Cdd:COG4942 93 AELRAELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 119586555 1105 QKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEE 1152
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1205-1899 |
1.33e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.12 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1205 EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQ----------IIKAKAANL-------EKMCRTLEDQMNEHRSKAEEt 1267
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQkenklqenrkIIEAQRKAIqelqfenEKVSLKLEEEIQENKDLIKE- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1268 qrsvNDLTSQRAKLQTENGELSRQLDEKEALISQLTRgkltytQQLEDLKRQLEEEVKAKNALAHALQSARHDCDL-LRE 1346
Cdd:pfam05483 150 ----NNATRHLCNLLKETCARSAEKTKKYEYEREETR------QVYMDLNNNIEKMILAFEELRVQAENARLEMHFkLKE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1347 QYEEETEAKAELQRVLSKANSEVAQW---RTKYETDAIQRTEELEEAKKKLAQrlqeAEEAVEAVNAKCSSLEKTKHRLQ 1423
Cdd:pfam05483 220 DHEKIQHLEEEYKKEINDKEKQVSLLliqITEKENKMKDLTFLLEESRDKANQ----LEEKTKLQDENLKELIEKKDHLT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1424 NEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKyEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKREN 1503
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEE-KEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1504 KNLQEEIsdLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEasleheegKILRAQLEFNQIKAEierkLAEKDEE 1583
Cdd:pfam05483 375 NEDQLKI--ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDE--------KLLDEKKQFEKIAEE----LKGKEQE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1584 MEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQ----LSHANRMAAEAQKQVKSLQSL---LKDTQI 1656
Cdd:pfam05483 441 LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKnielTAHCDKLLLENKELTQEASDMtleLKKHQE 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1657 QLDDAVRANDDLKENIAIVERRNNLLQAELE-----------ELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLI 1725
Cdd:pfam05483 521 DIINCKKQEERMLKQIENLEEKEMNLRDELEsvreefiqkgdEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1726 NQKKKMDADLSQLQTEveeavqecrNAEEKAKKAITDAAMMAEELKKEQdTSAHLERMKKNMEQTIKDLQHRLdEAEQIA 1805
Cdd:pfam05483 601 KQIENKNKNIEELHQE---------NKALKKKGSAENKQLNAYEIKVNK-LELELASAKQKFEEIIDNYQKEI-EDKKIS 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1806 LKGGKKQLQKLEARVRE---LENELEAE-QKRNAESVKGMRKS--------ERRIKEL-TYQTEEDRKNLLR------LQ 1866
Cdd:pfam05483 670 EEKLLEEVEKAKAIADEavkLQKEIDKRcQHKIAEMVALMEKHkhqydkiiEERDSELgLYKNKEQEQSSAKaaleieLS 749
|
730 740 750
....*....|....*....|....*....|....*...
gi 119586555 1867 DLVDKL-----QLKVKAYKRQAEEAEEQANTNLSKFRK 1899
Cdd:pfam05483 750 NIKAELlslkkQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1226-1922 |
1.37e-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: 60.24 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1226 LELDDVTSNMEQIIKAKAANLEKMCRTLEDQMNEhRSKAEETQRSVNDLTSQRAKLQTengeLSRQLDEKEALISQLTRG 1305
Cdd:pfam12128 206 LEDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKI-RPEFTKLQQEFNTLESAELRLSH----LHFGYKSDETLIASRQEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1306 KLTYTQQLEDLKRQLEEEVKAK--------NALAHALQSARHDCDLLREQYEEETEAKAElqrVLSKANSEVAQWRTKye 1377
Cdd:pfam12128 281 RQETSAELNQLLRTLDDQWKEKrdelngelSAADAAVAKDRSELEALEDQHGAFLDADIE---TAAADQEQLPSWQSE-- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1378 tdaiqrTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSlektkhRLQNEIEDLMVDVERSNAAAAALDKKQRN-FDKILAE 1456
Cdd:pfam12128 356 ------LENLEERLKALTGKHQDVTAKYNRRRSKIKE------QNNRDIAGIKDKLAKIREARDRQLAVAEDdLQALESE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1457 WKQKYEESQSELESSQKEARSLSTELFKLKN---AYEESLEHLETFkrenknlQEEISDLTEQLGSSGKTIHELEKVRKQ 1533
Cdd:pfam12128 424 LREQLEAGKLEFNEEEYRLKSRLGELKLRLNqatATPELLLQLENF-------DERIERAREEQEAANAEVERLQSELRQ 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1534 LEAEKMELQSALEEAEASLEHEEGKILRAQ----------LEFNQIKAEIERKLAEKDEEMEQAKRNHLR-VVDSLQTS- 1601
Cdd:pfam12128 497 ARKRRDQASEALRQASRRLEERQSALDELElqlfpqagtlLHFLRKEAPDWEQSIGKVISPELLHRTDLDpEVWDGSVGg 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1602 --------LDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRAnddLKENIA 1673
Cdd:pfam12128 577 elnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA---LKNARL 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1674 IVERRNNLLQAELeelRAVVEQTERSRKLAEqelietsERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAE 1753
Cdd:pfam12128 654 DLRRLFDEKQSEK---DKKNKALAERKDSAN-------ERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVV 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1754 EKAKKAiTDAAMMAEELKKEQDTSAHLERMKKNMEqtiKDLQHRLDEAEQIAlkggkkqlqKLEARVRELENELEAEQKR 1833
Cdd:pfam12128 724 EGALDA-QLALLKAAIAARRSGAKAELKALETWYK---RDLASLGVDPDVIA---------KLKREIRTLERKIERIAVR 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1834 NAESVKGMRKSERRI----KELTYQTEEDRKNLLRLQDLVDKLQLKVKAyKRQAEEAEEQANtnlskfRKVQHELDEAEE 1909
Cdd:pfam12128 791 RQEVLRYFDWYQETWlqrrPRLATQLSNIERAISELQQQLARLIADTKL-RRAKLEMERKAS------EKQQVRLSENLR 863
|
730
....*....|...
gi 119586555 1910 RADIAESQVNKLR 1922
Cdd:pfam12128 864 GLRCEMSKLATLK 876
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1593-1895 |
1.61e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.65 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1593 RVVDSLQ--TSLDAETRSRNEAL-----RVKKKMEGDLNEMEIQLSHANrmAAEAQKQVKSLQSLLKDTQIQLddavran 1665
Cdd:COG3206 98 RVVDKLNldEDPLGEEASREAAIerlrkNLTVEPVKGSNVIEISYTSPD--PELAAAVANALAEAYLEQNLEL------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1666 ddlkeNIAIVERRNNLLQAELEELRAVVEQTERSRK--LAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVE 1743
Cdd:COG3206 169 -----RREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1744 eAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNMEQTIKDLQHRLDEAEQIALKGGKKQL 1813
Cdd:COG3206 244 -ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1814 QKLEARVRELENELEAEQKRnaesVKGMRKSERRIKELTYQTEEDRKNllrLQDLVDKLQlkvkaykrQAEEAEEQANTN 1893
Cdd:COG3206 323 EALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVAREL---YESLLQRLE--------EARLAEALTVGN 387
|
..
gi 119586555 1894 LS 1895
Cdd:COG3206 388 VR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1045-1284 |
2.18e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1045 RMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIeeleeelea 1124
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1125 ertarakvEKLRSDLSRELEEISERLEEA---GGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRkkhadsva 1201
Cdd:COG4942 93 --------AELRAELEAQKEELAELLRALyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR-------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1202 elgEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKAANlEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKL 1281
Cdd:COG4942 157 ---ADLAELAALRAELEAERAELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
...
gi 119586555 1282 QTE 1284
Cdd:COG4942 233 EAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
861-1082 |
3.32e-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: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 861 EALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKK 940
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 941 RKLEDECSELKRDIddleltlakvekEKHATENKVKNLT-----EEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEED 1015
Cdd:COG4942 100 EAQKEELAELLRAL------------YRLGRQPPLALLLspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119586555 1016 KVNTLTKAKVKLEQQVDDLEGSLEQEKKVRmdlERAKRKLEGDLKLTQESIMDLENDKQQLDERLKK 1082
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1648-1898 |
3.32e-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: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1648 QSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQllhsqntSLINQ 1727
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1728 KKKMDADLSQLQTEVEEAVqecRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQI--A 1805
Cdd:COG4942 92 IAELRAELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALraE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1806 LKGGKKQLQKLEARVRELENELEAEQKRNAESVKgmrKSERRIKELTYQTEEDRKNLLRLQDLVDKLQlkvkayKRQAEE 1885
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLE------AEAAAA 239
|
250
....*....|...
gi 119586555 1886 AEEQANTNLSKFR 1898
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1197-1414 |
3.41e-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: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1197 ADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIiKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTS 1276
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1277 QRAKLQTENGELSRQL------DEKEALIS-----QLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLR 1345
Cdd:COG4942 98 ELEAQKEELAELLRALyrlgrqPPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119586555 1346 EQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSS 1414
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1682-1929 |
3.90e-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: 58.65 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1682 LQAELEELRAVVEQteRSRKLaEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEavQECRNAEEKAKKAIT 1761
Cdd:pfam01576 55 LCAEAEEMRARLAA--RKQEL-EEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE--EEAARQKLQLEKVTT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1762 DAAM--MAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlKGGKKQLQKLEARVRELENELEAEQKRNAESVK 1839
Cdd:pfam01576 130 EAKIkkLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA-KSLSKLKNKHEAMISDLEERLKKEEKGRQELEK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1840 GMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVN 1919
Cdd:pfam01576 209 AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN 288
|
250
....*....|
gi 119586555 1920 KLRAKSRDIG 1929
Cdd:pfam01576 289 KAEKQRRDLG 298
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
859-1875 |
3.98e-08 |
|
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: 58.91 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 859 LKEALEKSEARRKeLEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIK--NKIQLEAKVKEMNerLEDEEEMNAEL 936
Cdd:TIGR01612 546 LKESYELAKNWKK-LIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIyiNKLKLELKEKIKN--ISDKNEYIKKA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 937 TAKKRKLEDECSElkrdIDDleltLAKVEKEKhatenkvknLTEEMAGLDEIIAKLTKEkkaLQEAHQQALDDLQ----- 1011
Cdd:TIGR01612 623 IDLKKIIENNNAY----IDE----LAKISPYQ---------VPEHLKNKDKIYSTIKSE---LSKIYEDDIDALYnelss 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1012 --AEEDKVNTLTKAKvkleqqVDDLEGSLEQEKKVRMDLERAKRKLegdlkltqeSIMDLENDKQQLDE---RLKKKDF- 1085
Cdd:TIGR01612 683 ivKENAIDNTEDKAK------LDDLKSKIDKEYDKIQNMETATVEL---------HLSNIENKKNELLDiivEIKKHIHg 747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1086 ELNA-LNARIEDeqalgsqLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMN 1164
Cdd:TIGR01612 748 EINKdLNKILED-------FKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYI 820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1165 KK---REAEFQKM---RRDLEEATLQHEATAAALRKKHADSVAELGEQIDNL-QRVKQKLEKEK-SEFKLELDDVTSNME 1236
Cdd:TIGR01612 821 KTisiKEDEIFKIineMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELtNKIKAEISDDKlNDYEKKFNDSKSLIN 900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1237 QIIKA------------KAANLEKMCRTLEDQMNEHRSKaeetQRSVNDLTSQRAKLQTENGELSRQLDEK--EALISQL 1302
Cdd:TIGR01612 901 EINKSieeeyqnintlkKVDEYIKICENTKESIEKFHNK----QNILKEILNKNIDTIKESNLIEKSYKDKfdNTLIDKI 976
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1303 TRGKLTYTQ-QLEDLKRQLEEEVKAKNALAHALQSARHdcDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAI 1381
Cdd:TIGR01612 977 NELDKAFKDaSLNDYEAKNNELIKYFNDLKANLGKNKE--NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIY 1054
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1382 QRTEELEEAKKKLAQRLQeaEEAVEAVNAKCSSLEKTKHRLQ----------------NEIEDLMVDVErsnaaaaALDK 1445
Cdd:TIGR01612 1055 NIIDEIEKEIGKNIELLN--KEILEEAEINITNFNEIKEKLKhynfddfgkeenikyaDEINKIKDDIK-------NLDQ 1125
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1446 KQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKN--AYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKT 1523
Cdd:TIGR01612 1126 KIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDpeEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKD 1205
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1524 IHELEKVR---------------KQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKlaekdEEMEQAK 1588
Cdd:TIGR01612 1206 KTSLEEVKginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIK-----AEMETFN 1280
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1589 RNHLRVVDSLQTSLDAE---TRSRNEALRVKKKM--EGDLNEMEIQLshaNRMAAEAQKQVKSLQSLLKDTQ-----IQL 1658
Cdd:TIGR01612 1281 ISHDDDKDHHIISKKHDeniSDIREKSLKIIEDFseESDINDIKKEL---QKNLLDAQKHNSDINLYLNEIAniyniLKL 1357
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1659 DDAVRANDDLKENIAIVERRNNLLQAE----------------LEELRAVVEQTERSRKLAE--QELIETSERVQLLHSQ 1720
Cdd:TIGR01612 1358 NKIKKIIDEVKEYTKEIEENNKNIKDEldkseklikkikddinLEECKSKIESTLDDKDIDEciKKIKELKNHILSEESN 1437
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1721 NTSLINQKKKMDADLSQLQTEVEEAVQECRN-AEEKAKKAITDAAMMAEELKKEQDTS-----------AHLERMKKNME 1788
Cdd:TIGR01612 1438 IDTYFKNADENNENVLLLFKNIEMADNKSQHiLKIKKDNATNDHDFNINELKEHIDKSkgckdeadknaKAIEKNKELFE 1517
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1789 QTIKDLQHRLDEAEQIALKGG----KKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLR 1864
Cdd:TIGR01612 1518 QYKKDVTELLNKYSALAIKNKfaktKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAID 1597
|
1130
....*....|.
gi 119586555 1865 LQDLVDKLQLK 1875
Cdd:TIGR01612 1598 IQLSLENFENK 1608
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1357-1931 |
4.33e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1357 ELQRVLSKANSEVA---QWRTKYETDAIQRTEELEEAKKKLAQRLQE---AEEAVEAVNAKCSSLEKTKHRLQNEIEDLM 1430
Cdd:TIGR04523 100 KLNSDLSKINSEIKndkEQKNKLEVELNKLEKQKKENKKNIDKFLTEikkKEKELEKLNNKYNDLKKQKEELENELNLLE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1431 VDversnaaaaaLDKKQRNFDKILAEWKQKYEESQSELESSQKEaRSLSTELFKLKNAYEESLEHLETFKRENKNLQEEI 1510
Cdd:TIGR04523 180 KE----------KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1511 SDLTEQLGSsgkTIHELEKVRKQLEAEKMELQSAleeaeasleheEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRN 1590
Cdd:TIGR04523 249 SNTQTQLNQ---LKDEQNKIKKQLSEKQKELEQN-----------NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1591 HLRVVDS----LQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRAND 1666
Cdd:TIGR04523 315 ELKNQEKkleeIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1667 DLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAV 1746
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1747 QECRNAEEKAKKaitdaamMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDE--AEQIALKGGKKQLQK--------- 1815
Cdd:TIGR04523 475 RSINKIKQNLEQ-------KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSlkEKIEKLESEKKEKESkisdledel 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1816 -----------LEARVRELENELEaEQKRNAESVKgmrKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVkayKRQAE 1884
Cdd:TIGR04523 548 nkddfelkkenLEKEIDEKNKEIE-ELKQTQKSLK---KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL---EKELE 620
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 119586555 1885 EAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTK 1931
Cdd:TIGR04523 621 KAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKK 667
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1205-1442 |
4.88e-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: 57.47 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1205 EQIDNLQRVKQKLEKEKSEFKLELDDvtsnmeqiIKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTE 1284
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA--------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1285 NGELSRQLDEKEALISQLTRgkltyTQQLEDLKRQLEEEVKAKNA--LAHALQSARHDCDLLREQYEEETEAKAELQRVL 1362
Cdd:COG4942 92 IAELRAELEAQKEELAELLR-----ALYRLGRQPPLALLLSPEDFldAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1363 SKANSEVAQWRTKYETDAIQRtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAA 1442
Cdd:COG4942 167 AELEAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
969-1199 |
5.38e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 969 HATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQekkvrmdL 1048
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1049 ERAKRKLEGDLKLTQESIMDLENDKQQLDER------LKKKDFE-----LNALNARIEDEQALGSQLQKKLKELQARIEE 1117
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQpplallLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1118 LEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHA 1197
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARL----EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
..
gi 119586555 1198 DS 1199
Cdd:COG4942 245 AA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1010-1223 |
5.62e-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: 57.08 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1010 LQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNA 1089
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1090 LNARIEDEQALGSQLQKKL--KELQARIEELEEELEAERTARA-----KVEKLRSDLSRELEEISERLEEAGGATSVQIE 1162
Cdd:COG4942 95 LRAELEAQKEELAELLRALyrLGRQPPLALLLSPEDFLDAVRRlqylkYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119586555 1163 MNKKREAEFQKMRRDLEEATLQHEATAAALRKK---HADSVAELGEQIDNLQRVKQKLEKEKSE 1223
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKElaeLAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1185-1927 |
6.36e-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: 57.93 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1185 HEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKlELDDVTSNMEQIIKAKAANLEKMCRTLEDQMNEHRSKA 1264
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYK-SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDEL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1265 EetqrsvNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQsarhdcDLL 1344
Cdd:pfam12128 307 N------GELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQ------DVT 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1345 REQYEEETEAKAELQRVLSKANSEVAQwrtKYETDAIQRTEElEEAKKKLAQRLQEAEEAVEAvnakcsSLEKTKHRLQN 1424
Cdd:pfam12128 375 AKYNRRRSKIKEQNNRDIAGIKDKLAK---IREARDRQLAVA-EDDLQALESELREQLEAGKL------EFNEEEYRLKS 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1425 EIEDLMVdveRSNAAAAALDKK--QRNFDKILAEWKQKyeesqseLESSQKEARSLSTELFKLKNAYEESLEHLETFKRE 1502
Cdd:pfam12128 445 RLGELKL---RLNQATATPELLlqLENFDERIERAREE-------QEAANAEVERLQSELRQARKRRDQASEALRQASRR 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1503 NKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAE---KMELQSALEEAEASLEHEEGKIlRAQLEFNQIKAEIERKLAE 1579
Cdd:pfam12128 515 LEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQsigKVISPELLHRTDLDPEVWDGSV-GGELNLYGVKLDLKRIDVP 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1580 KDEEMEQAKRNHLrvvDSLQTSLDAEtRSRNEALrvkkkmegdlnemEIQLSHANRMAAEAQKQVKSLQSLLK---DTQI 1656
Cdd:pfam12128 594 EWAASEEELRERL---DKAEEALQSA-REKQAAA-------------EEQLVQANGELEKASREETFARTALKnarLDLR 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1657 QLDDAVRANDDLKENiaIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETServqllhSQNTSLINQKKK-----M 1731
Cdd:pfam12128 657 RLFDEKQSEKDKKNK--ALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQK-------REARTEKQAYWQvvegaL 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1732 DADLSQLQTEVeEAVQECRNAEEKAKKaitdaAMMAEELKK---EQDTSAHLERMKKNMEQTIKDLQHRLDEA---EQIA 1805
Cdd:pfam12128 728 DAQLALLKAAI-AARRSGAKAELKALE-----TWYKRDLASlgvDPDVIAKLKREIRTLERKIERIAVRRQEVlryFDWY 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1806 LKGGKKQLQKLEARVRELEN---ELEAEQKRNAESVKgmrkseRRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQ 1882
Cdd:pfam12128 802 QETWLQRRPRLATQLSNIERaisELQQQLARLIADTK------LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATL 875
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 119586555 1883 AEEAE-EQANTNLSkfrkvqHELDEAEERADIAESQVNKLRAKSRD 1927
Cdd:pfam12128 876 KEDANsEQAQGSIG------ERLAQLEDLKLKRDYLSESVKKYVEH 915
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
851-1033 |
7.71e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.32 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 851 SMKEEFTRLKEaLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLE-DE 929
Cdd:COG1579 1 AMPEDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 930 EEMNAELTAKKRK-LEDECSELKRDIDDLEltlakvEKEKHATEnKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALD 1008
Cdd:COG1579 80 EQLGNVRNNKEYEaLQKEIESLKRRISDLE------DEILELME-RIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180
....*....|....*....|....*
gi 119586555 1009 DLQAEEDKvntLTKAKVKLEQQVDD 1033
Cdd:COG1579 153 ELEAELEE---LEAEREELAAKIPP 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1241-1456 |
7.98e-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: 56.70 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1241 AKAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQL 1320
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1321 EEEVKA-KNALAHALQSARHDCDLLREQYEEETEAKAELQRVlskanSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQ 1399
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL-----KYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 119586555 1400 EAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAE 1456
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
833-1409 |
8.32e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.60 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 833 YFKIKPLLKSAERE-KEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQA---EQDNLADAEERCDQL 908
Cdd:PRK01156 168 YDKLKDVIDMLRAEiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNamdDYNNLKSALNELSSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 909 IKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLedecselkrdiddLELTLAKVEKEKHATeNKVKNLTEEMAGLDEI 988
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYKELEERH-------------MKIINDPVYKNRNYI-NDYFKYKNDIENKKQI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 989 IAKLTKEKKALQEAHQQaLDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSleqekkvRMDLERAKRKLEGDLKLTQESIMD 1068
Cdd:PRK01156 314 LSNIDAEINKYHAIIKK-LSVLQKDYNDYIKKKSRYDDLNNQILELEGY-------EMDYNSYLKSIESLKKKIEEYSKN 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1069 LENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARA------------------ 1130
Cdd:PRK01156 386 IERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlgee 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1131 KVEKLRSDLSRELEEISE---RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQI 1207
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEkirEIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKH 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1208 DnlqrvkqKLEKEKSEFK-LELDDVTSNMEQIIKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENG 1286
Cdd:PRK01156 546 D-------KYEEIKNRYKsLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYID 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1287 ELSRQLDEKealiSQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKAN 1366
Cdd:PRK01156 619 KSIREIENE----ANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAK 694
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 119586555 1367 SEVAQWRTKYETDaIQRTEELEEAKKKLAQRLQEAEEAVEAVN 1409
Cdd:PRK01156 695 ANRARLESTIEIL-RTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
833-1284 |
1.09e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 56.77 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 833 YFKIKPLLKSAER-----EKEMASMKEEFTRLKEALEKSEARRKELEEKMvsllqekNDLQLQVQAEQDNLADAEErcdq 907
Cdd:PRK04778 100 FRKAKHEINEIESlldliEEDIEQILEELQELLESEEKNREEVEQLKDLY-------RELRKSLLANRFSFGPALD---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 908 liknkiQLEAKVKEMNERLEDEEEMNAE---LTAKK--RKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKN----L 978
Cdd:PRK04778 169 ------ELEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 979 TEEMAGLDEIiaKLTKEKKALQEAHQQALDDLQAEEdkvntLTKAKVKLEQ---QVDDLEGSLEQEKKVRMDLERAKRKL 1055
Cdd:PRK04778 243 VEEGYHLDHL--DIEKEIQDLKEQIDENLALLEELD-----LDEAEEKNEEiqeRIDQLYDILEREVKARKYVEKNSDTL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1056 EGDLKLTQESIMDLENDKQQLDERlkkkdFELNalnariEDEQALGSQLQKKLKELQARIEELEEELeaertarAKVEKL 1135
Cdd:PRK04778 316 PDFLEHAKEQNKELKEEIDRVKQS-----YTLN------ESELESVRQLEKQLESLEKQYDEITERI-------AEQEIA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1136 RSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsvaelgeqidnLQRVKQ 1215
Cdd:PRK04778 378 YSELQEELEEILKQLEEI-----------EKEQEKLSEMLQGLRKDELEAREKLERYRNK--------------LHEIKR 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119586555 1216 KLEKEK-----SEFKLELDDVTSNMEQiikakaanlekmcrtLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTE 1284
Cdd:PRK04778 433 YLEKSNlpglpEDYLEMFFEVSDEIEA---------------LAEELEEKPINMEAVNRLLEEATEDVETLEEE 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1318-1776 |
1.24e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1318 RQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWrtkyetDAIQRTEELEEAKKKLAQR 1397
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL------PLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1398 LQEAEEAVEAVN---AKCSSLEKTKHRLQNEIEDLMVDVerSNAAAAALDKKQRNFDKILAEWKQkyeesqselesSQKE 1474
Cdd:COG4717 148 LEELEERLEELReleEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEELEELQQRLAE-----------LEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1475 ARSLSTELfklkNAYEESLEHLETfKRENKNLQEEISDLTEQLGSSGkTIHELEKVRKQLEAEKMELQSALEEAEASLEH 1554
Cdd:COG4717 215 LEEAQEEL----EELEEELEQLEN-ELEAAALEERLKEARLLLLIAA-ALLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1555 EEGKILRAQLEFNQIKAEIERKLAEKDEEMEQakrnhlrvVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHAN 1634
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEE--------LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1635 RmAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLA---------EQ 1705
Cdd:COG4717 361 E-ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeleeeleelEE 439
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119586555 1706 ELIETSERVQLLHSQNTSLINQKKKM--DADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT 1776
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
839-1056 |
1.27e-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: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 839 LLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAK 918
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 919 VKEMNERLEDEEEMNAELTAKKRKLEDEcSELK-----RDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 993
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQ-PPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119586555 994 KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLE 1056
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
929-1360 |
1.39e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 929 EEEMNAELTAKKRKLEDECSELKRDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALqEAHQQALD 1008
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1009 DLQAEEDKVNTLTKAKVKLEQqvddlegsLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDK-QQLDERLKKKDFEL 1087
Cdd:COG4717 130 LYQELEALEAELAELPERLEE--------LEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1088 NALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRS--------DLSRELEEISERLEEAGGATSV 1159
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1160 QIEM----------------NKKREAEFQKMRRDLEEATLQHEATAAAL-RKKHADSVAELGEQIDNLQRVKQKLEKEKS 1222
Cdd:COG4717 282 VLGLlallflllarekaslgKEAEELQALPALEELEEEELEELLAALGLpPDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1223 EFKLelddvtsnmEQIIKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLD--EKEALIS 1300
Cdd:COG4717 362 ELQL---------EELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEE 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1301 QLTRgkltYTQQLEDLKRQLEEEVKAKNALAHALQSARHDcDLLREQYEEETEAKAELQR 1360
Cdd:COG4717 433 ELEE----LEEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRE 487
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1482-1928 |
1.46e-07 |
|
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: 56.40 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1482 LFKLKNAYEEsLEHLETFKRE--NKNLQEEISDLtEQLGSSGKTIHELEKVRKQ---LEAEKM-ELQSALEEAEASLEhe 1555
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddIVTKSLpDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1556 EGKILRAQLEFNqikaEIERKLAEKDEEMEQakrnhlrVVDSLQTSLDAETRSRNEALRVKKK----------------- 1618
Cdd:pfam06160 78 KYRFKKAKKALD----EIEELLDDIEEDIKQ-------ILEELDELLESEEKNREEVEELKDKyrelrktllanrfsygp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1619 ----MEGDLNEMEIQLSHA-NRMAA----EAQKQVKSLQSLLKDTQIQLDDavranddlkenI-AIVERRNNLLQAELEE 1688
Cdd:pfam06160 147 aideLEKQLAEIEEEFSQFeELTESgdylEAREVLEKLEEETDALEELMED-----------IpPLYEELKTELPDQLEE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1689 LRAVVEQTERSR-KLAEQELIETSERVQLLHSQNTSLINQK--KKMDADLSQLQTEVEEaVQECRNAEEKAKKaitdaam 1765
Cdd:pfam06160 216 LKEGYREMEEEGyALEHLNVDKEIQQLEEQLEENLALLENLelDEAEEALEEIEERIDQ-LYDLLEKEVDAKK------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1766 maeELKKEQDT-SAHLERMKKNMEQTIKDLQH-----RLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVK 1839
Cdd:pfam06160 288 ---YVEKNLPEiEDYLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1840 GMRKSERRIKELTYQTEEDRKNL-------LRLQDLVDKLQLKVKAYKRQAE----------------EAEEQANTNLSK 1896
Cdd:pfam06160 365 ELEEILEQLEEIEEEQEEFKESLqslrkdeLEAREKLDEFKLELREIKRLVEksnlpglpesyldyffDVSDEIEDLADE 444
|
490 500 510
....*....|....*....|....*....|..
gi 119586555 1897 FRKVQHELDEAEERADIAESQVNKLRAKSRDI 1928
Cdd:pfam06160 445 LNEVPLNMDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
845-1836 |
1.60e-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: 56.98 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 845 REKEMASMKEEFTRLKEALEKSEARRKELeekmvsllqeKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNE 924
Cdd:TIGR01612 763 KEKELSNKINDYAKEKDELNKYKSKISEI----------KNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFK 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 925 RLEDEEEMNAELTAKKRK---LEDECSElkrDIDDLELTLAKVEkekhateNKVKNLTEEmAGLDEIIAKLTKEKKALQE 1001
Cdd:TIGR01612 833 IINEMKFMKDDFLNKVDKfinFENNCKE---KIDSEHEQFAELT-------NKIKAEISD-DKLNDYEKKFNDSKSLINE 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1002 AHQQalddLQAEEDKVNTLTKakvkLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLK 1081
Cdd:TIGR01612 902 INKS----IEEEYQNINTLKK----VDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLI 973
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1082 KKDFELNAL--NARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAkvEKLRSDLSRELEE-------------- 1145
Cdd:TIGR01612 974 DKINELDKAfkDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFDEK--EKATNDIEQKIEDanknipnieiaiht 1051
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1146 ----ISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEK 1221
Cdd:TIGR01612 1052 siynIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHI 1131
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1222 SEFKlELDDVTSNMEQIIKAKAANLEKMCRTLedQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQ 1301
Cdd:TIGR01612 1132 KALE-EIKKKSENYIDEIKAQINDLEDVADKA--ISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTS 1208
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1302 LTRGK---LTYTQQLEDL-KRQLEEEVKAKNALAHALQSARHDCDLLREQYEE-------ETEAKAELQrVLSKANSEva 1370
Cdd:TIGR01612 1209 LEEVKginLSYGKNLGKLfLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEienemgiEMDIKAEME-TFNISHDD-- 1285
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1371 qwRTKYETDAIQRTEELEEAKKKLAQRLQEaeeaveavNAKCSSLEKTKHRLQNEIedlmVDVERSNAAAAALDKKQRNF 1450
Cdd:TIGR01612 1286 --DKDHHIISKKHDENISDIREKSLKIIED--------FSEESDINDIKKELQKNL----LDAQKHNSDINLYLNEIANI 1351
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1451 DKILaewkqkyeesqselessqkearslstELFKLKNAYEESLEHLETFKRENKNLQEEISDlTEQLGssgKTIHElekv 1530
Cdd:TIGR01612 1352 YNIL--------------------------KLNKIKKIIDEVKEYTKEIEENNKNIKDELDK-SEKLI---KKIKD---- 1397
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1531 RKQLEAEKMELQSALEEAEAsleheEGKILRAQLEFNQIKAEierkLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRN 1610
Cdd:TIGR01612 1398 DINLEECKSKIESTLDDKDI-----DECIKKIKELKNHILSE----ESNIDTYFKNADENNENVLLLFKNIEMADNKSQH 1468
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1611 eALRVKKK-----MEGDLNEMEIQLSHANRMAAEAQKQVKSLQS---LLKdtQIQLDDAVRAND----DLKENIAIVERR 1678
Cdd:TIGR01612 1469 -ILKIKKDnatndHDFNINELKEHIDKSKGCKDEADKNAKAIEKnkeLFE--QYKKDVTELLNKysalAIKNKFAKTKKD 1545
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1679 NNLLQAELEELRAVV----EQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQ--TEVEEAVQECRNA 1752
Cdd:TIGR01612 1546 SEIIIKEIKDAHKKFileaEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLkiSDIKKKINDCLKE 1625
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1753 EEKAKKAITDAAMMAEE--LKKEQDTSAHLERMKKNMEQTIKDLQHRldeaeqialkggKKQLQKLEARVRELENELEaE 1830
Cdd:TIGR01612 1626 TESIEKKISSFSIDSQDteLKENGDNLNSLQEFLESLKDQKKNIEDK------------KKELDELDSEIEKIEIDVD-Q 1692
|
....*.
gi 119586555 1831 QKRNAE 1836
Cdd:TIGR01612 1693 HKKNYE 1698
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
651-675 |
2.04e-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: 2.04e-07
10 20
....*....|....*....|....*
gi 119586555 651 HRENLNKLMTNLRSTHPHFVRCIIP 675
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
853-1429 |
2.07e-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: 56.50 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 853 KEEFTRLKEALEK--SEARRKELEEKMVSLLQEKNDLQLQVQAEQD---NLADAEERCDQLIKNKIQLEAKVKEMNERLE 927
Cdd:COG3096 471 RRQFEKAYELVCKiaGEVERSQAWQTARELLRRYRSQQALAQRLQQlraQLAELEQRLRQQQNAERLLEEFCQRIGQQLD 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 928 DEEEmnaeltakkrkLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL----------DEIIAKLTKE-- 995
Cdd:COG3096 551 AAEE-----------LEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELaarapawlaaQDALERLREQsg 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 996 -----KKALQEAHQQALDD---LQAEEDKvntLTKAKVKLEQQV------------------------------DD---- 1033
Cdd:COG3096 620 ealadSQEVTAAMQQLLERereATVERDE---LAARKQALESQIerlsqpggaedprllalaerlggvllseiyDDvtle 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1034 -------LEGSLEQEKKVRmDLERAKRKLEGdLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQK 1106
Cdd:COG3096 697 dapyfsaLYGPARHAIVVP-DLSAVKEQLAG-LEDCPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSDRQWRYSRFPE 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1107 klkelqarieeleeeleAERTARAKVEKLRSDLSRELEEISERLEEAggATSVQiemnkkreaEFQKMRRDLEEATLQH- 1185
Cdd:COG3096 775 -----------------VPLFGRAAREKRLEELRAERDELAEQYAKA--SFDVQ---------KLQRLHQAFSQFVGGHl 826
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1186 --------EATAAALRKKHADSVAELGEQIDNLQRVKQKLEkeksEFKLELDDVTSNMEQIIKAKAANLEKMCRTLEdqm 1257
Cdd:COG3096 827 avafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLD----QLKEQLQLLNKLLPQANLLADETLADRLEELR--- 899
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1258 nEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKltytQQLEDLKRQ---LEEEVKAKNALAH-- 1332
Cdd:COG3096 900 -EELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAK----EQQRRLKQQifaLSEVVQRRPHFSYed 974
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1333 ALQSARHDCDL---LREQYEEETEAKAELQRVLSKANSEVAQW-----------RTKYET--DAIQRTEELE-----EAK 1391
Cdd:COG3096 975 AVGLLGENSDLnekLRARLEQAEEARREAREQLRQAQAQYSQYnqvlaslkssrDAKQQTlqELEQELEELGvqadaEAE 1054
|
650 660 670
....*....|....*....|....*....|....*...
gi 119586555 1392 KKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDL 1429
Cdd:COG3096 1055 ERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSL 1092
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
854-1231 |
2.26e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.06 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 854 EEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIK----NKIQLEAKVKEMNERLEDE 929
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKiqeiDPDAIKKELNEINVKLQDI 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 930 EEMNAELTAKKRKLEDECSELKRD-------------------------IDDLELTLAKVEKEKHATENKVKNLTEEMAG 984
Cdd:PRK01156 422 SSKVSSLNQRIRALRENLDELSRNmemlngqsvcpvcgttlgeeksnhiINHYNEKKSRLEEKIREIEIEVKDIDEKIVD 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 985 LDEIIAKLTKEKKALQEAHQQALDDLQAE----EDKVNTLTKAKVKLEQ--------QVDDLEGSLEQEKK--------- 1043
Cdd:PRK01156 502 LKKRKEYLESEEINKSINEYNKIESARADlediKIKINELKDKHDKYEEiknrykslKLEDLDSKRTSWLNalavislid 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1044 ---VRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNAR---IEDEQALGSQLQKKLKELQARIEE 1117
Cdd:PRK01156 582 ietNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKyneIQENKILIEKLRGKIDNYKKQIAE 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1118 LEEELEAERTARAKVEKLRSDL---SRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRK 1194
Cdd:PRK01156 662 IDSIIPDLKEITSRINDIEDNLkksRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRL 741
|
410 420 430
....*....|....*....|....*....|....*....
gi 119586555 1195 KHADSVAELGEQI--DNLQRVKQKLEKEKSEFKLELDDV 1231
Cdd:PRK01156 742 REAFDKSGVPAMIrkSASQAMTSLTRKYLFEFNLDFDDI 780
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1139-1792 |
2.27e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 55.98 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1139 LSRELEEISERLEEaggaTSVQIEMNKKR-EAEFQKMRRDLEeaTLQHEATAAALRKKHADSVAELGE---QIDNLQRVK 1214
Cdd:pfam10174 128 QAKELFLLRKTLEE----MELRIETQKQTlGARDESIKKLLE--MLQSKGLPKKSGEEDWERTRRIAEaemQLGHLEVLL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1215 QKLEKEKSEFKLEL---------DDVTSNMEQIIKAK---AANLEKMCRTLEDQMNEHRSKA-------EETQRSVNDLT 1275
Cdd:pfam10174 202 DQKEKENIHLREELhrrnqlqpdPAKTKALQTVIEMKdtkISSLERNIRDLEDEVQMLKTNGllhtedrEEEIKQMEVYK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1276 SQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLE---EEVKAKNALAHALQSarhDCDLLREQYEEEt 1352
Cdd:pfam10174 282 SHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEvlkESLTAKEQRAAILQT---EVDALRLRLEEK- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1353 eakaelQRVLSKansevaqwrtkyETDAIQRteeLEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVD 1432
Cdd:pfam10174 358 ------ESFLNK------------KTKQLQD---LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1433 VERSNAAAAALDKKQRNFDKILAEWKQKyEESQSELESSQKEARSLSTElfklknayeESLEHLETFKRENKNLQEEISD 1512
Cdd:pfam10174 417 LAGLKERVKSLQTDSSNTDTALTTLEEA-LSEKERIIERLKEQREREDR---------ERLEELESLKKENKDLKEKVSA 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1513 LTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEH--EEGKILRAQLEFNQIKAEIERK---LAEKDEEMEQA 1587
Cdd:pfam10174 487 LQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQkkEECSKLENQLKKAHNAEEAVRTnpeINDRIRLLEQE 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1588 KRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQ-LDDAVRAND 1666
Cdd:pfam10174 567 VARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQlLEEARRRED 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1667 DLKENIAiverrnnllQAELEELRAVVEQTersrklaEQELIETSERV----QLLHSQNTSLINQKKKMDADLSqlqtEV 1742
Cdd:pfam10174 647 NLADNSQ---------QLQLEELMGALEKT-------RQELDATKARLsstqQSLAEKDGHLTNLRAERRKQLE----EI 706
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 119586555 1743 EEAVQECRNAEEKAKKA-ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIK 1792
Cdd:pfam10174 707 LEMKQEALLAAISEKDAnIALLELSSSKKKKTQEEVMALKREKDRLVHQLK 757
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
840-1097 |
2.48e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 840 LKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLlqeknDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKV 919
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 920 KEMNERLEDEEEMNAELTAkkrklEDECSELKRDIDDLELTLAkvEKEKHATEN--KVKNLTEEMAGLdeiiakltkeKK 997
Cdd:COG3206 243 AALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL----------RA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 998 ALQEAHQQALDDLQAEedkVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRklegDLKLTQESIMDLENDKQQLD 1077
Cdd:COG3206 306 QLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLER----EVEVARELYESLLQRLEEAR 378
|
250 260
....*....|....*....|
gi 119586555 1078 ERLkkkdfELNALNARIEDE 1097
Cdd:COG3206 379 LAE-----ALTVGNVRVIDP 393
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1620-1837 |
2.72e-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: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1620 EGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERS 1699
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1700 rklAEQELIETSERVQLLHSQNTS-LINQKKKMDAdLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsa 1778
Cdd:COG3883 95 ---LYRSGGSVSYLDVLLGSESFSdFLDRLSALSK-IADADADLLEELKADKAELEAKKAELEAKLAELEALKAE----- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 119586555 1779 hLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENELEAEQKRNAES 1837
Cdd:COG3883 166 -LEAAKAELEAQQAEQEALLAQLSA--------EEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
849-1322 |
2.86e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 55.96 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 849 MASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQliknkiqleakvkemNERLED 928
Cdd:PRK10246 428 LVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQ---------------EARIKD 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 929 EEEMNAELTAKK----------------RKLEDECSELKRdiDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKL 992
Cdd:PRK10246 493 LEAQRAQLQAGQpcplcgstshpaveayQALEPGVNQSRL--DALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSL 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 993 TKEKKALQEAHQQALDDL---QAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRmDLERAKRKLEGDLKLTQESimdL 1069
Cdd:PRK10246 571 RQEEQALTQQWQAVCASLnitLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIA-AHNQQIIQYQQQIEQRQQQ---L 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1070 ENDKQQLDERLKKKDFELNALNARiEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISER 1149
Cdd:PRK10246 647 LTALAGYALTLPQEDEEASWLATR-QQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQ 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1150 leeaggATSVQIEMNKKREAEFQKMRRdLEEATLQHEATAAALRkkHADSVAELGEQIDNLQRvkQKLEKEKSEFKLELD 1229
Cdd:PRK10246 726 ------CLSLHSQLQTLQQQDVLEAQR-LQKAQAQFDTALQASV--FDDQQAFLAALLDEETL--TQLEQLKQNLENQRQ 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1230 DVTSNMEQIIKAKAANLEKMCRTLEDQmnehrSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLtrgkLTY 1309
Cdd:PRK10246 795 QAQTLVTQTAQALAQHQQHRPDGLDLT-----VTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQ----QAL 865
|
490
....*....|...
gi 119586555 1310 TQQLEDLKRQLEE 1322
Cdd:PRK10246 866 MQQIAQATQQVED 878
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
841-1273 |
4.11e-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: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 841 KSAEREkEMASMKE----EFTRLKEALEKSEA---RRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKI 913
Cdd:pfam05483 389 KSSELE-EMTKFKNnkevELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 914 QLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 993
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 994 KEKKALQEAHQQALDDLQAEEDKVntltkakvklEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDK 1073
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLDKS----------EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1074 QQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELqarieeleeeleaERTARAKVEKLRSDLSRELEEISERLEEA 1153
Cdd:pfam05483 618 KALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEI-------------IDNYQKEIEDKKISEEKLLEEVEKAKAIA 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1154 GGATSVQIEMNKKREAEFQKMrrdleeatlqheataAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTS 1233
Cdd:pfam05483 685 DEAVKLQKEIDKRCQHKIAEM---------------VALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELS 749
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 119586555 1234 NmeqiIKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVND 1273
Cdd:pfam05483 750 N----IKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1352-1588 |
4.32e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1352 TEAKAELQRVLSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMv 1431
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE--------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1432 dvERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEIS 1511
Cdd:COG4942 90 --KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119586555 1512 DLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAK 1588
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
846-1013 |
4.38e-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: 53.00 E-value: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 846 EKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKiQLEAKVKEMner 925
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKEI--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 926 ledeeemnAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKhatENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQ 1005
Cdd:COG1579 99 --------ESLKRRISDLEDEILELMERIEELEEELAELEAEL---AELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
....*...
gi 119586555 1006 ALDDLQAE 1013
Cdd:COG1579 168 LAAKIPPE 175
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
835-1200 |
5.12e-07 |
|
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: 55.12 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 835 KIKPLLKSAEREKEM-ASMKEEFTRLKEALEKSE-------------ARRKELEEKMVSLLQEKNDLQLQ----VQAEQD 896
Cdd:pfam15921 462 KVSSLTAQLESTKEMlRKVVEELTAKKMTLESSErtvsdltaslqekERAIEATNAEITKLRSRVDLKLQelqhLKNEGD 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 897 NLADAEERCDQLiknKIQLEAK---VKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATEN 973
Cdd:pfam15921 542 HLRNVQTECEAL---KLQMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 974 KVKNLTEEMAGLDEIIAKLT-------KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQE-KKVR 1045
Cdd:pfam15921 619 KIRELEARVSDLELEKVKLVnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTtNKLK 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1046 MDLERAKRKLEGdlklTQESIMDLENDkqqlderlkkkdfELNALNARIEDEQALGSQlQKKLKELQARIEELEEELEAE 1125
Cdd:pfam15921 699 MQLKSAQSELEQ----TRNTLKSMEGS-------------DGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNA 760
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119586555 1126 RTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSV 1200
Cdd:pfam15921 761 NKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESV 835
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1001-1162 |
5.31e-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: 52.62 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1001 EAHQQALDDLQAEEDKVNTLTKAK-------VKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESImdlENDK 1073
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLkelpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI---KKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1074 QQLDERLKKKdfELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEA 1153
Cdd:COG1579 80 EQLGNVRNNK--EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
....*....
gi 119586555 1154 GGATSVQIE 1162
Cdd:COG1579 158 LEELEAERE 166
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
921-1340 |
8.41e-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: 53.53 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 921 EMNERLEDEEEMNAELTAKKRKLEDECSEL---KRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKK 997
Cdd:pfam19220 14 EMADRLEDLRSLKADFSQLIEPIEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 998 ALQEAHQQAldDLQAEEDKVNTLTKakvklEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLD 1077
Cdd:pfam19220 94 KLEAALREA--EAAKEELRIELRDK-----TAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1078 ERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARieeleeeleaERTARAKVEKLRSDLSRELEEiSERLEEAggat 1157
Cdd:pfam19220 167 ERLALLEQENRRLQALSEEQAAELAELTRRLAELETQ----------LDATRARLRALEGQLAAEQAE-RERAEAQ---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1158 svqiemnkkreaefqkmrRDLEEATLQHEATAAALRKKHADSVAE-----LGEQIDNLQRVK---QKLEKEKSEFKLELD 1229
Cdd:pfam19220 232 ------------------LEEAVEAHRAERASLRMKLEALTARAAateqlLAEARNQLRDRDeaiRAAERRLKEASIERD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1230 DVTSNMEQiIKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQltrGKLTY 1309
Cdd:pfam19220 294 TLERRLAG-LEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEV---ERAAL 369
|
410 420 430
....*....|....*....|....*....|..
gi 119586555 1310 TQQLEDLKRQLEEEvKAKNALAH-ALQSARHD 1340
Cdd:pfam19220 370 EQANRRLKEELQRE-RAERALAQgALEIARES 400
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
847-1549 |
9.33e-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: 54.19 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 847 KEMASMKEEFTRLKEALEKSEARRKELEEKMVS------LLQEKNDLQLQVQAEQDNLADAEERcdqliknkiqLEakvk 920
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAasdhlnLVQTALRQQEKIERYQEDLEELTER----------LE---- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 921 EMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDL-------------------------------ELTLAKVEKEKH 969
Cdd:COG3096 365 EQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYqqaldvqqtraiqyqqavqalekaralcglpDLTPENAEDYLA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 970 ATENKVKNLTEEMAGLDE--IIAKLTKEK--KALQ------------EAHQQALDDLQAEEDKVNTLTKAkVKLEQQVDD 1033
Cdd:COG3096 445 AFRAKEQQATEEVLELEQklSVADAARRQfeKAYElvckiageversQAWQTARELLRRYRSQQALAQRL-QQLRAQLAE 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1034 LEGSLEQEKKVRMDLERAKRKLEGDLkltqESIMDLENDKQQLDERLKKkdfelnaLNARIEDEQALGSQLQKKLKELQA 1113
Cdd:COG3096 524 LEQRLRQQQNAERLLEEFCQRIGQQL----DAAEELEELLAELEAQLEE-------LEEQAAEAVEQRSELRQQLEQLRA 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1114 RIEELEEELEAERTARAKVEKLRsdlsrelEEISERLEEAGGATS-VQIEMNKKREAEFQKmrrdlEEATLQHEATAAAL 1192
Cdd:COG3096 593 RIKELAARAPAWLAAQDALERLR-------EQSGEALADSQEVTAaMQQLLEREREATVER-----DELAARKQALESQI 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1193 RKKHADSVAE------LGEQ---------------------------------IDNLQRVKQKLEK-------------- 1219
Cdd:COG3096 661 ERLSQPGGAEdprllaLAERlggvllseiyddvtledapyfsalygparhaivVPDLSAVKEQLAGledcpedlyliegd 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1220 ----EKSEFKL-ELDD---VTSNMEQI------------IKAKAANLEKMcRTLEDQMNEHRSKA----EETQR---SVN 1272
Cdd:COG3096 741 pdsfDDSVFDAeELEDavvVKLSDRQWrysrfpevplfgRAAREKRLEEL-RAERDELAEQYAKAsfdvQKLQRlhqAFS 819
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1273 DLTSQR-------------AKLQTENGELSRQLDEKEALISQLtrgkltyTQQLEDLKRQLeEEVKAKNALAHALQSARH 1339
Cdd:COG3096 820 QFVGGHlavafapdpeaelAALRQRRSELERELAQHRAQEQQL-------RQQLDQLKEQL-QLLNKLLPQANLLADETL 891
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1340 D--CDLLREQYEEETEAKAELQRvlskanseVAQWRTKYET--DAIQRTEELEEAkkkLAQRLQEAEEAVEAVNAKCSSL 1415
Cdd:COG3096 892 AdrLEELREELDAAQEAQAFIQQ--------HGKALAQLEPlvAVLQSDPEQFEQ---LQADYLQAKEQQRRLKQQIFAL 960
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1416 EKTKHRLQNEIEDlmvDVERSNAAAAALDKKQRnfdKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEH 1495
Cdd:COG3096 961 SEVVQRRPHFSYE---DAVGLLGENSDLNEKLR---ARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQT 1034
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119586555 1496 LETFKRENKNL------------QEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAE 1549
Cdd:COG3096 1035 LQELEQELEELgvqadaeaeeraRIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAE 1100
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
841-1111 |
1.18e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 53.75 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 841 KSAEREKEMASMKEEFTRLKEALEKS-----EARRKELEEkMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKI-- 913
Cdd:PLN02939 118 NSKDGEQLSDFQLEDLVGMIQNAEKNilllnQARLQALED-LEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIhv 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 914 -----QLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKekhaTENKVKNLTEEMAGLDEI 988
Cdd:PLN02939 197 eileeQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAE----TEERVFKLEKERSLLDAS 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 989 IAKLTKEKKALQEAHQQaLDDLQAEE--DKVNTLTKAKVKLEQQVDDLEGSLEQEKkvrmDLERAKRKLEGDL------K 1060
Cdd:PLN02939 273 LRELESKFIVAQEDVSK-LSPLQYDCwwEKVENLQDLLDRATNQVEKAALVLDQNQ----DLRDKVDKLEASLkeanvsK 347
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 119586555 1061 LTQESIMDLENDKQQLDERLKKKDFElnaLNARIEDEQALGSQLQKKLKEL 1111
Cdd:PLN02939 348 FSSYKVELLQQKLKLLEERLQASDHE---IHSYIQLYQESIKEFQDTLSKL 395
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1474-1830 |
1.67e-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: 52.76 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1474 EARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLE 1553
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1554 HEEGKILRAQLEFNQ---IKAEIERKLAEKDEEME------QAKRNHLRVVDSLQTSLDAETRSRNEALRV----KKKME 1620
Cdd:pfam19220 101 EAEAAKEELRIELRDktaQAEALERQLAAETEQNRaleeenKALREEAQAAEKALQRAEGELATARERLALleqeNRRLQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1621 GDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAV----RANDDLKENIAIVERRNNLLQAELEELRAVVEQT 1696
Cdd:pfam19220 181 ALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQaereRAEAQLEEAVEAHRAERASLRMKLEALTARAAAT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1697 ERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQEcRNAEEKAKKAITD-AAMMAEELKkeqD 1775
Cdd:pfam19220 261 EQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQ-FQEMQRARAELEErAEMLTKALA---A 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 119586555 1776 TSAHLERMkknmEQTIKDLQHRLDEAEQIALKggkkQLQKLEARVRELENELEAE 1830
Cdd:pfam19220 337 KDAALERA----EERIASLSDRIAELTKRFEV----ERAALEQANRRLKEELQRE 383
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1669-1932 |
1.90e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1669 KENIAIVERRNNLLQAELEELRAVVEQTERSRKlaeqELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQE 1748
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1749 CRNAEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENEle 1828
Cdd:PRK03918 275 IEELEEKVKEL--------KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEE--------EINGIEERIKELEEK-- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1829 aeqkrnaesvkgmrksERRIKELTYQTEEDRKNLLRLQDLVDKLQlKVKAYKRQAEEAEEQAnTNLSKfRKVQHELDEAE 1908
Cdd:PRK03918 337 ----------------EERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRL-TGLTP-EKLEKELEELE 397
|
250 260
....*....|....*....|....
gi 119586555 1909 ERADIAESQVNKLRAKSRDIGTKR 1932
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEI 421
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
934-1130 |
2.15e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 934 AELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQ-- 1011
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1012 -AEEDKVNTLTKAK---------VKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLK 1081
Cdd:COG3883 99 gGSVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 119586555 1082 KKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARA 1130
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1246-1447 |
2.59e-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: 52.55 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1246 LEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVK 1325
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1326 AKNALAHALQSARHdcdllREQYEEETEAKAELQRVLSKANSevaqwrtkyeTDAI-QRTEELEEAKKKLAQRLQEAEEA 1404
Cdd:pfam09726 480 ARASAEKQLAEEKK-----RKKEEEATAARAVALAAASRGEC----------TESLkQRKRELESEIKKLTHDIKLKEEQ 544
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 119586555 1405 VEAVNAKCSSLEKTKHRlQNEIEDLMvdversNAAAAALDKKQ 1447
Cdd:pfam09726 545 IRELEIKVQELRKYKES-EKDTEVLM------SALSAMQDKNQ 580
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
883-1532 |
2.72e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 883 EKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELtakkRKLEDECSELKRDIDDLELTLA 962
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKL----KSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 963 KVEKEKHATENKVKNLTEEMAGLDEIIAKLT---KEKKALQEAHQQALDDLQAEEDKVNtltkakvkleqqvdDLEGSLE 1039
Cdd:PRK01156 215 ITLKEIERLSIEYNNAMDDYNNLKSALNELSsleDMKNRYESEIKTAESDLSMELEKNN--------------YYKELEE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1040 QEKKVRMDLERAKRklegdlkltqESIMDLENDKQQLD---ERLKKKDFELNALNARIedeqalgsqlqKKLKELQArie 1116
Cdd:PRK01156 281 RHMKIINDPVYKNR----------NYINDYFKYKNDIEnkkQILSNIDAEINKYHAII-----------KKLSVLQK--- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1117 eleeeleaERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRR---DLEEATLQHEATAAALR 1193
Cdd:PRK01156 337 --------DYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERmsaFISEILKIQEIDPDAIK 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1194 KKHadsvAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIikaKAANLEKMCRT------LEDQMNEHRSKAEET 1267
Cdd:PRK01156 409 KEL----NEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEML---NGQSVCPVCGTtlgeekSNHIINHYNEKKSRL 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1268 QRSVNDLTSQRAKLqteNGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQ 1347
Cdd:PRK01156 482 EEKIREIEIEVKDI---DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSL 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1348 YEEETEAKAElqrVLSKANSEvaqwRTKYETDAIQ-RTEELEEAKKKLAQRLQEAEEAVEAVNakcSSLEKTKHRLQNEI 1426
Cdd:PRK01156 559 KLEDLDSKRT---SWLNALAV----ISLIDIETNRsRSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEA 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1427 EDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKeARSLSTELFKLKNAYEESLEHLETFKRENKNL 1506
Cdd:PRK01156 629 NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSR-INDIEDNLKKSRKALDDAKANRARLESTIEIL 707
|
650 660
....*....|....*....|....*.
gi 119586555 1507 QEEISDLTEQLGSSGKTIHELEKVRK 1532
Cdd:PRK01156 708 RTRINELSDRINDINETLESMKKIKK 733
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1669-1926 |
3.26e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1669 KENIAIVE--RRNNLLQAELEELRAVVEQ-------TERsRKLAEQELIETSERVQLLHSQNTSLINQKKKMdadlsQLQ 1739
Cdd:TIGR02168 135 KRSYSIIEqgKISEIIEAKPEERRAIFEEaagiskyKER-RKETERKLERTRENLDRLEDILNELERQLKSL-----ERQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1740 TEVEEAVQECRNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEAR 1819
Cdd:TIGR02168 209 AEKAERYKELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEELRLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1820 VRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRK 1899
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
250 260
....*....|....*....|....*..
gi 119586555 1900 VQHELDEAEERADIAESQVNKLRAKSR 1926
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLE 382
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1263-1930 |
3.57e-06 |
|
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: 52.36 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1263 KAEETQRSVndLTSQRAKLQTEngELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAK-NALAHALQSARHDC 1341
Cdd:TIGR00606 186 KALETLRQV--RQTQGQKVQEH--QMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENElDPLKNRLKEIEHNL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1342 DLLREqYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAK----KKLAQRLQEAEEAVEAVNAKCSSLEK 1417
Cdd:TIGR00606 262 SKIMK-LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHqrtvREKERELVDCQRELEKLNKERRLLNQ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1418 TKHRLQNEIEDLMVDVER-------------SNAAAAALDKKQRNFDKIlaewKQKYEESQSELESSQKEARSLSTELFK 1484
Cdd:TIGR00606 341 EKTELLVEQGRLQLQADRhqehirardsliqSLATRLELDGFERGPFSE----RQIKNFHTLVIERQEDEAKTAAQLCAD 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1485 LKNAYEESLEHLETFKRENKNLQEEISDLTEQLGssgKTIHELEKVRKQLEAEK------MELQSALEEAEASLEHEEGK 1558
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTIELKKEILE---KKQEELKFVIKELQQLEgssdriLELDQELRKAERELSKAEKN 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1559 -----ILRAQLEFNQIKAEIERKLAEKDEEMEQakrnhlrvvdslqtsLDAETRSRNEALRV-KKKMEGDLNEMEIQLSH 1632
Cdd:TIGR00606 494 sltetLKKEVKSLQNEKADLDRKLRKLDQEMEQ---------------LNHHTTTRTQMEMLtKDKMDKDEQIRKIKSRH 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1633 ANRMAAEA-----QKQV-KSLQSLLKDTQIQLDDAVrandDLKENIAIVERRNNLLQAELEELRAVVEQTER------SR 1700
Cdd:TIGR00606 559 SDELTSLLgyfpnKKQLeDWLHSKSKEINQTRDRLA----KLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcGS 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1701 KLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECR---NAEEKAKKAITDAAMMAEELKKEQ-DT 1776
Cdd:TIGR00606 635 QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQrvfQTEAELQEFISDLQSKLRLAPDKLkST 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1777 SAHLERMKKNMEQTIKDLQHRLDEAEQIA--LKGGKKQLQKLEARVRELENELEAEQKR------NAESVKGMRKSERRI 1848
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLAPGRQSIIDLKEkeIPELRNKLQKVNRDIQRLKNDIEEQETLlgtimpEEESAKVCLTDVTIM 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1849 KELTYQTEEDRKnllRLQDLVDKLQ-----LKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRA 1923
Cdd:TIGR00606 795 ERFQMELKDVER---KIAQQAAKLQgsdldRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKS 871
|
....*..
gi 119586555 1924 KSRDIGT 1930
Cdd:TIGR00606 872 EKLQIGT 878
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1252-1410 |
3.60e-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: 50.31 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1252 TLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAK--NA 1329
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1330 LAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVN 1409
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
.
gi 119586555 1410 A 1410
Cdd:COG1579 174 P 174
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1262-1589 |
3.80e-06 |
|
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: 51.94 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1262 SKAEETQRSVNDLTsqRAKLQTENGELSRQLDEKE-----ALISQLTRGKLTYTQQLEDLKRQLEEEV--KAKNALAHAL 1334
Cdd:NF033838 50 SSGNESQKEHAKEV--ESHLEKILSEIQKSLDKRKhtqnvALNKKLSDIKTEYLYELNVLKEKSEAELtsKTKKELDAAF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1335 QSARHDCDLLREQYEEETEAKAELQRvlsKANSEVAQWRTKYETDAIqRTEELEEAKKKLaqRLQEAEEAVEAVNAKCSS 1414
Cdd:NF033838 128 EQFKKDTLEPGKKVAEATKKVEEAEK---KAKDQKEEDRRNYPTNTY-KTLELEIAESDV--EVKKAELELVKEEAKEPR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1415 LEKTkhrlqneIEDLMVDVERSNAAAAALDKKQRnfDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLE 1494
Cdd:NF033838 202 DEEK-------IKQAKAKVESKKAEATRLEKIKT--DREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1495 HLETFKRENKNLQEEISDLTEQLGS----SGKTIHELEK-----------------------VRKQLEAEKMELQSALEE 1547
Cdd:NF033838 273 PATPDKKENDAKSSDSSVGEETLPSpslkPEKKVAEAEKkveeakkkakdqkeedrrnyptnTYKTLELEIAESDVKVKE 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 119586555 1548 AEASLEHEEGKILRAQLEFNQIKAEIERKLAE----------KDEEMEQAKR 1589
Cdd:NF033838 353 AELELVKEEAKEPRNEEKIKQAKAKVESKKAEatrlekiktdRKKAEEEAKR 404
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
867-1335 |
3.94e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 52.06 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 867 EARRKELEEKMVSLLQEKNDLQLQVQAEQDNLadaeercdQLIKNKIQLEAkvKEMNERLEDEEEMNAELTAKKRKLede 946
Cdd:pfam07111 241 ELERQELLDTMQHLQEDRADLQATVELLQVRV--------QSLTHMLALQE--EELTRKIQPSDSLEPEFPKKCRSL--- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 947 cseLKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTL------ 1020
Cdd:pfam07111 308 ---LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLqmelsr 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1021 -TKAKVKLEQQVDDLEgslEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKkdfelnalnariedeqa 1099
Cdd:pfam07111 385 aQEARRRQQQQTASAE---EQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRK----------------- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1100 lgsqlQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISE---RL--EEAGGATSVQIEMNKKREaEFQKM 1174
Cdd:pfam07111 445 -----VHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREernRLdaELQLSAHLIQQEVGRARE-QGEAE 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1175 RRDLEEATLQHEATAaalrKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKAANLEKMCRT-- 1252
Cdd:pfam07111 519 RQQLSEVAQQLEQEL----QRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREql 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1253 --LEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEalisqltrgkltyTQQLEDLKRQLEEEVKAKNAL 1330
Cdd:pfam07111 595 sdTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEAR-------------KEEGQRLARRVQELERDKNLM 661
|
....*
gi 119586555 1331 AHALQ 1335
Cdd:pfam07111 662 LATLQ 666
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1042-1869 |
4.32e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1042 KKVRMDLERAKRKLegdlKLTQESIMDLENDKQQLDERLKK------KDFELNALNARIEDEQALGSQlqkklKELQAri 1115
Cdd:PRK04863 229 RKAFQDMEAALREN----RMTLEAIRVTQSDRDLFKHLITEstnyvaADYMRHANERRVHLEEALELR-----RELYT-- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1116 eeleeeleaERTARAKVEKLRSDLSRELEEISER---LEEAGGATS--VQIEMNKKREAE-FQKMRRDLEEATLQHEATA 1189
Cdd:PRK04863 298 ---------SRRQLAAEQYRLVEMARELAELNEAesdLEQDYQAASdhLNLVQTALRQQEkIERYQADLEELEERLEEQN 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1190 AAlrkkhadsVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNME-------QIIKAKAAnLEK---MCRT------- 1252
Cdd:PRK04863 369 EV--------VEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDvqqtraiQYQQAVQA-LERakqLCGLpdltadn 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1253 LEDQMNEHRSKAEETQRSVNDL-----TSQRAKLQTENG---------------------ELSRQLDEKEALISQLTRGK 1306
Cdd:PRK04863 440 AEDWLEEFQAKEQEATEELLSLeqklsVAQAAHSQFEQAyqlvrkiagevsrseawdvarELLRRLREQRHLAEQLQQLR 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1307 ltytQQLEDLKRQLEEEVKAKNALAHALQSARHDCDlLREQYEEETEAKAELQRVLSKANSEVAQWRTKYEtdaiQRTEE 1386
Cdd:PRK04863 520 ----MRLSELEQRLRQQQRAERLLAEFCKRLGKNLD-DEDELEQLQEELEARLESLSESVSEARERRMALR----QQLEQ 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1387 LEEAKKKLAQRLQE---AEEAVEAVNAKCSSLEKTKHRLQNEIEDLmvdVERSNAAAAALDKKQRNFDKILAEWKQKYEE 1463
Cdd:PRK04863 591 LQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQL---LERERELTVERDELAARKQALDEEIERLSQP 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1464 SQSELESSQKEARSLSTELfkLKNAYEE-SLEH-------------------LETFKRENKNLQEEISDL------TEQL 1517
Cdd:PRK04863 668 GGSEDPRLNALAERFGGVL--LSEIYDDvSLEDapyfsalygparhaivvpdLSDAAEQLAGLEDCPEDLyliegdPDSF 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1518 GSSGKTIHELEK----------VR----------------KQLEAEKMELQSaLEEAEASLEHEEGKILRAQLEFNQIKA 1571
Cdd:PRK04863 746 DDSVFSVEELEKavvvkiadrqWRysrfpevplfgraareKRIEQLRAEREE-LAERYATLSFDVQKLQRLHQAFSRFIG 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1572 E-IERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMeiqLSHANRMAAEaqkqvkSLQSL 1650
Cdd:PRK04863 825 ShLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRL---LPRLNLLADE------TLADR 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1651 LKDTQIQLDDAVRANDDLKEN---IAIVERRNNLLQA---ELEELRAVVEQTERSRKLAEQELIETSERVQLLH----SQ 1720
Cdd:PRK04863 896 VEEIREQLDEAEEAKRFVQQHgnaLAQLEPIVSVLQSdpeQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyED 975
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1721 NTSLINQkkkmDADLS-QLQTEVEEAVQECRNAEEKAKKA---ITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQH 1796
Cdd:PRK04863 976 AAEMLAK----NSDLNeKLRQRLEQAEQERTRAREQLRQAqaqLAQYNQVLASLKSSYDA---KRQMLQELKQELQDLGV 1048
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119586555 1797 RLDEAEQIALKGGKKQLQKLEARVRELENELEAE---QKRNAES-VKGMRKSERRIKELTYQTEEDRKNLLRLQDLV 1869
Cdd:PRK04863 1049 PADSGAEERARARRDELHARLSANRSRRNQLEKQltfCEAEMDNlTKKLRKLERDYHEMREQVVNAKAGWCAVLRLV 1125
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1350-1910 |
4.34e-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: 52.03 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1350 EETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKL-AQR--LQEAEEAVEAVNAKCSSLEKTKHRL--QN 1424
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIeAQRkaIQELQFENEKVSLKLEEEIQENKDLikEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1425 EIEDLMVDVERSNAAAAALDKKQRNFDKilAEWKQKYEESQSELESSQKEARSLSTEL--------FKLKNAYEEsLEHL 1496
Cdd:pfam05483 151 NATRHLCNLLKETCARSAEKTKKYEYER--EETRQVYMDLNNNIEKMILAFEELRVQAenarlemhFKLKEDHEK-IQHL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1497 ET-FKRENKNLQEEIS--------------DLTEQLGSSGKTIHELEKVRK-------QLEAEKMELQSALEEAEASLEH 1554
Cdd:pfam05483 228 EEeYKKEINDKEKQVSllliqitekenkmkDLTFLLEESRDKANQLEEKTKlqdenlkELIEKKDHLTKELEDIKMSLQR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1555 EEGKILRAQLEFNQIKAEIERKLAEKDEEMEQ---AKRNHLRVVdslqTSLDAETRSRNEALRV-KKKMEGDLNEMEIql 1630
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEElnkAKAAHSFVV----TEFEATTCSLEELLRTeQQRLEKNEDQLKI-- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1631 shanrMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERrNNLLQAELEELRAVVEQTERSRKLAEQELIET 1710
Cdd:pfam05483 382 -----ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDE-KKQFEKIAEELKGKEQELIFLLQAREKEIHDL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1711 SERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMeqt 1790
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM--- 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1791 ikdlqhrldeaeqialkggKKQLQKLEARVRELENELEA---EQKRNAESVK-GMRKSERRIKELTYQTEEDRKNLLRLQ 1866
Cdd:pfam05483 533 -------------------LKQIENLEEKEMNLRDELESvreEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILE 593
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 119586555 1867 DL--------------VDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEER 1910
Cdd:pfam05483 594 NKcnnlkkqienknknIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK 651
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1274-1698 |
4.41e-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: 51.43 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1274 LTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAknaLAHALQSARHDCDLLREQYEEETE 1353
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAE---LKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1354 AKAELqrvlskanSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDV 1433
Cdd:pfam07888 109 SSEEL--------SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1434 ERSnaaaaaldkkqrnfdkilaewkqkyeesqselessQKEARSLSTELFKLKNAYEESLEHLETfkrenknLQEEISDL 1513
Cdd:pfam07888 181 QQT-----------------------------------EEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1514 TEQLGSSGKTIHELEKVRKqleaekmELQSALEEAEASLEHEEGkilraqlefnqIKAEIERKLAEKDEEMEQAKRNHLR 1593
Cdd:pfam07888 219 TQKLTTAHRKEAENEALLE-------ELRSLQERLNASERKVEG-----------LGEELSSMAAQRDRTQAELHQARLQ 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1594 VVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQ--------------IQLD 1659
Cdd:pfam07888 281 AAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREklevelgrekdcnrVQLS 360
|
410 420 430
....*....|....*....|....*....|....*....
gi 119586555 1660 DAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTER 1698
Cdd:pfam07888 361 ESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1240-1885 |
5.46e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.72 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1240 KAKAANLEKmcrtLEDQMNEHRSKAEETQRSVND----LTSQRAKLQTENGELSRQ---LDEKEALISQLTRgkltyTQQ 1312
Cdd:PRK10246 194 KSARTELEK----LQAQASGVALLTPEQVQSLTAslqvLTDEEKQLLTAQQQQQQSlnwLTRLDELQQEASR-----RQQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1313 LedLKRQLEEEVKAKNALAhALQSARHDCDL--LREQYEEETEAKAELQRVLSKANS---EVAQWRTKYETDAIQRTEEL 1387
Cdd:PRK10246 265 A--LQQALAAEEKAQPQLA-ALSLAQPARQLrpHWERIQEQSAALAHTRQQIEEVNTrlqSTMALRARIRHHAAKQSAEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1388 EEAKKKLAQRLQEAE------EAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNA------------AAAALDK--KQ 1447
Cdd:PRK10246 342 QAQQQSLNTWLAEHDrfrqwnNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltadeVAAALAQhaEQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1448 RNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKnayeeslEHLETFKRENKNLQEEISDLteqlgssgKTIHEL 1527
Cdd:PRK10246 422 RPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRN-------AALNEMRQRYKEKTQQLADV--------KTICEQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1528 EKVRKQLEAEKMELQS-------------------------------ALEEAEASLEhEEGKILRAQLE--FNQIK---- 1570
Cdd:PRK10246 487 EARIKDLEAQRAQLQAgqpcplcgstshpaveayqalepgvnqsrldALEKEVKKLG-EEGAALRGQLDalTKQLQrdes 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1571 -----AEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEgdlneMEIQLSHANRMAAEAQKQVK 1645
Cdd:PRK10246 566 eaqslRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHE-----LQGQIAAHNQQIIQYQQQIE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1646 SLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKL-----AEQELIETSERVQL---- 1716
Cdd:PRK10246 641 QRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLletlpQSDDLPHSEETVALdnwr 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1717 -LHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEK---AKKAITDAAMMAEElkkeqdTSAHLERMKKNMEQTIK 1792
Cdd:PRK10246 721 qVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQAsvfDDQQAFLAALLDEE------TLTQLEQLKQNLENQRQ 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1793 DLQHRLDEAEQialkggkKQLQKLEARVRELENELEAE--QKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVd 1870
Cdd:PRK10246 795 QAQTLVTQTAQ-------ALAQHQQHRPDGLDLTVTVEqiQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALM- 866
|
730
....*....|....*
gi 119586555 1871 klqLKVKAYKRQAEE 1885
Cdd:PRK10246 867 ---QQIAQATQQVED 878
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
860-1682 |
5.70e-06 |
|
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: 51.98 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 860 KEALEK--SEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLA------------DAEERCDQLIKN----KIQLEAKVKE 921
Cdd:TIGR01612 976 INELDKafKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLyhqfdekekatnDIEQKIEDANKNipniEIAIHTSIYN 1055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 922 MNERLEDEEEMNAELTAKK--RKLEDECSELKRDIDDLEL----TLAKVEKEKHATE-NKVKNlteEMAGLDEIIAKLTK 994
Cdd:TIGR01612 1056 IIDEIEKEIGKNIELLNKEilEEAEINITNFNEIKEKLKHynfdDFGKEENIKYADEiNKIKD---DIKNLDQKIDHHIK 1132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 995 EKKALQEAHQQALDDLQAEEDKVNTLTKAKVkleqQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQEsIMDLENDK- 1073
Cdd:TIGR01612 1133 ALEEIKKKSENYIDEIKAQINDLEDVADKAI----SNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNE-IAEIEKDKt 1207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1074 ---------------------QQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAeRTARAKV 1132
Cdd:TIGR01612 1208 sleevkginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETF-NISHDDD 1286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1133 EKLRSDLSRELEEISERLEEaggatSVQIEMNKKREAEFQKMRRDLEEATLQHEataaalrkKHADSVAELGEQIDN--- 1209
Cdd:TIGR01612 1287 KDHHIISKKHDENISDIREK-----SLKIIEDFSEESDINDIKKELQKNLLDAQ--------KHNSDINLYLNEIANiyn 1353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1210 ---LQRVKQKLEKEKsEFKLELDDVTSNmeqiIKAKAANLEKMCRTLEDQMN--EHRSKAEETQ---------RSVNDLT 1275
Cdd:TIGR01612 1354 ilkLNKIKKIIDEVK-EYTKEIEENNKN----IKDELDKSEKLIKKIKDDINleECKSKIESTLddkdideciKKIKELK 1428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1276 SQRAKLQTENGELSRQLDEKEALISQLTRgkltyTQQLEDLKRQLEEEVKAKNAlahalqSARHDCDL--LREQYEEETE 1353
Cdd:TIGR01612 1429 NHILSEESNIDTYFKNADENNENVLLLFK-----NIEMADNKSQHILKIKKDNA------TNDHDFNIneLKEHIDKSKG 1497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1354 AKAELQR----------VLSKANSEVAQWRTKYETDAIQrtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQ 1423
Cdd:TIGR01612 1498 CKDEADKnakaieknkeLFEQYKKDVTELLNKYSALAIK--NKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIK 1575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1424 NE---IEDLMVDVERSNAAAAALDKKQRNFDkilaewkqkyeesqselessqkearslsTELFKLKNAYEESLEHLetfk 1500
Cdd:TIGR01612 1576 KEkfrIEDDAAKNDKSNKAAIDIQLSLENFE----------------------------NKFLKISDIKKKINDCL---- 1623
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1501 RENKNLQEEISDLT-----EQLGSSGKTIHELEKVRKQLEAEKMELqsalEEAEASLEHEEGKILRAQLEFNQIKAEIER 1575
Cdd:TIGR01612 1624 KETESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQKKNI----EDKKKELDELDSEIEKIEIDVDQHKKNYEI 1699
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1576 KLAEKDEEMEQAKRNHL------------RVVDSLQTSlDAETRSRNEALRVKKKMEGDLNEMEIQLSH--ANRMAAEAQ 1641
Cdd:TIGR01612 1700 GIIEKIKEIAIANKEEIesikelieptieNLISSFNTN-DLEGIDPNEKLEEYNTEIGDIYEEFIELYNiiAGCLETVSK 1778
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 119586555 1642 KQVKSLQslLKDTQIQlddavrANDDLKENIAIVERRNNLL 1682
Cdd:TIGR01612 1779 EPITYDE--IKNTRIN------AQNEFLKIIEIEKKSKSYL 1811
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1438-1678 |
7.43e-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: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1438 AAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQl 1517
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1518 gssgktiheLEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQI--KAEIERKLAEKDEEMEQAKRNHLRVV 1595
Cdd:COG4942 92 ---------IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1596 DSLQTSLDAEtrsrnealrvKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIV 1675
Cdd:COG4942 163 AALRAELEAE----------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
...
gi 119586555 1676 ERR 1678
Cdd:COG4942 233 EAE 235
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1311-1579 |
9.04e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.92 E-value: 9.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1311 QQLEDLKRQLEEEVKAKNALAHALQSARHDC-----DLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTE 1385
Cdd:pfam00038 21 RFLEQQNKLLETKISELRQKKGAEPSRLYSLyekeiEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1386 eLEEAKKKLAQRLQEAEEAVEAVNAKCSSLE------KTKHR-----LQNEIEDLMVDVERSNAaaaaldkKQRNFDKIL 1454
Cdd:pfam00038 101 -AENDLVGLRKDLDEATLARVDLEAKIESLKeelaflKKNHEeevreLQAQVSDTQVNVEMDAA-------RKLDLTSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1455 AEWKQKYEEsqselessqkearslstelfkLKNAYEESLEhlETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQL 1534
Cdd:pfam00038 173 AEIRAQYEE---------------------IAAKNREEAE--EWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSL 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 119586555 1535 EAE-------KMELQSALEEAEASLEHE----EGKILRAQLEFNQIKAEIERKLAE 1579
Cdd:pfam00038 230 EIElqslkkqKASLERQLAETEERYELQladyQELISELEAELQETRQEMARQLRE 285
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1011-1193 |
9.75e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 9.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1011 QAEEDKVNTLTKAKVKLEQQVDDLEGSLEQ-EKKvrmdLERAKRK-----LEGDLKLTQESIMDLENDKQQLDERLKKKD 1084
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAA----LEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1085 FELNALNARIED---------EQALGSQLQKKLKELQARIEELEEELEAE----RTARAKVEKLRSDLSRELEEISERLE 1151
Cdd:COG3206 240 ARLAALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 119586555 1152 eaggatsVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALR 1193
Cdd:COG3206 320 -------AELEALQAREASLQAQLAQLEARLAELPELEAELR 354
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1486-1921 |
9.96e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.60 E-value: 9.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1486 KNAYEEsLEHLETFKRE--NKNLQEEISDLtEQLGSSGKTIHELEKVRKQ----------------LEAEK-------ME 1540
Cdd:PRK04778 25 KRNYKR-IDELEERKQEleNLPVNDELEKV-KKLNLTGQSEEKFEEWRQKwdeivtnslpdieeqlFEAEElndkfrfRK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1541 LQSALEEAEASLEHEEGKILRAQLEFNQIKaEIERKLaekDEEMEQAKRNHlrvvDSLQTSLDAETRSRNEALrvkKKME 1620
Cdd:PRK04778 103 AKHEINEIESLLDLIEEDIEQILEELQELL-ESEEKN---REEVEQLKDLY----RELRKSLLANRFSFGPAL---DELE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1621 GDLNEMEIQLSHANRMAA-----EAQKQVKSLQSLLKDTQIQLDDavranddlkenI-AIVERRNNLLQAELEELRAVVE 1694
Cdd:PRK04778 172 KQLENLEEEFSQFVELTEsgdyvEAREILDQLEEELAALEQIMEE-----------IpELLKELQTELPDQLQELKAGYR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1695 Q-TERSRKLAEQELIETSERVQLLHSQNTSLINQ-------------KKKMDADLSQLQTEVEeavqeCRNAEEKAKKAI 1760
Cdd:PRK04778 241 ElVEEGYHLDHLDIEKEIQDLKEQIDENLALLEEldldeaeekneeiQERIDQLYDILEREVK-----ARKYVEKNSDTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1761 TDAAMMAEELKKEqdTSAHLERMKKN-------------MEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENEL 1827
Cdd:PRK04778 316 PDFLEHAKEQNKE--LKEEIDRVKQSytlneselesvrqLEKQLESLEKQYDEITE-RIAEQEIAYSELQEELEEILKQL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1828 ---EAEQKRNAESVKGMRKSERRIKEltyQTEEDRKNLLRLQDLVDKLQL-----KVKAYKRQAEEAEEQANTNLSKFR- 1898
Cdd:PRK04778 393 eeiEKEQEKLSEMLQGLRKDELEARE---KLERYRNKLHEIKRYLEKSNLpglpeDYLEMFFEVSDEIEALAEELEEKPi 469
|
490 500
....*....|....*....|....*.
gi 119586555 1899 ---KVQHELDEAEERADIAESQVNKL 1921
Cdd:PRK04778 470 nmeAVNRLLEEATEDVETLEEETEEL 495
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1311-1907 |
1.19e-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: 50.72 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1311 QQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLR---------EQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAI 1381
Cdd:COG3096 306 YRLVEMARELEELSARESDLEQDYQAASDHLNLVQtalrqqekiERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1382 QRTEELEEAKKKLA--------------------QRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDL---MVDVER--- 1435
Cdd:COG3096 386 AAEEEVDSLKSQLAdyqqaldvqqtraiqyqqavQALEKARALCGLPDLTPENAEDYLAAFRAKEQQAteeVLELEQkls 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1436 -SNAAAAALDKKQRNFDKILAE------WKQkyeesqseLESSQKEARSLSTELFKLkNAYEESLEHLETFKRENKNLQE 1508
Cdd:COG3096 466 vADAARRQFEKAYELVCKIAGEversqaWQT--------ARELLRRYRSQQALAQRL-QQLRAQLAELEQRLRQQQNAER 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1509 EISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEA---SLEHEEGKiLRAQLEFNQIKAEIERKLAEK----D 1581
Cdd:COG3096 537 LLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEqrsELRQQLEQ-LRARIKELAARAPAWLAAQDAlerlR 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1582 EEMEQAKRNHLRVVDSLQTSLDAE---TRSRNEALRVKKKMEGDLNEmeiqLSHAN-----RMAAEAQKQVKSLQSLLKD 1653
Cdd:COG3096 616 EQSGEALADSQEVTAAMQQLLEREreaTVERDELAARKQALESQIER----LSQPGgaedpRLLALAERLGGVLLSEIYD 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1654 tQIQLDDA-------------------------VRANDDLKENIAIVERR-----NNLLQAELEELRAVVEQTERS---- 1699
Cdd:COG3096 692 -DVTLEDApyfsalygparhaivvpdlsavkeqLAGLEDCPEDLYLIEGDpdsfdDSVFDAEELEDAVVVKLSDRQwrys 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1700 ---------RKLAEQELIETSE-----------------RVQLLHSQNTSLINQKKKM--DAD-------LSQLQTEVEE 1744
Cdd:COG3096 771 rfpevplfgRAAREKRLEELRAerdelaeqyakasfdvqKLQRLHQAFSQFVGGHLAVafAPDpeaelaaLRQRRSELER 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1745 AVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmKKNMEQTIKDLQHRLDEAEQ----IALKGgkKQLQKLEARV 1820
Cdd:COG3096 851 ELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLA--DETLADRLEELREELDAAQEaqafIQQHG--KALAQLEPLV 926
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1821 RELEN-------------ELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRknLLRLQDLVDKLQLKVkaykRQAEEAE 1887
Cdd:COG3096 927 AVLQSdpeqfeqlqadylQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGL--LGENSDLNEKLRARL----EQAEEAR 1000
|
730 740
....*....|....*....|
gi 119586555 1888 EQANTNLskfRKVQHELDEA 1907
Cdd:COG3096 1001 REAREQL---RQAQAQYSQY 1017
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1258-1929 |
1.20e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1258 NEHRSKAEETQRSVNDLTSQRAKLQTEN---GELSRQLDEKEALISQLTrgkltytQQLEDLKRQLEeevKAKNALAHAL 1334
Cdd:PRK04863 279 NERRVHLEEALELRRELYTSRRQLAAEQyrlVEMARELAELNEAESDLE-------QDYQAASDHLN---LVQTALRQQE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1335 QSARHDCDL--LREQYEEETEAKAElqrvlskANSEVAQWRTKYEtdaiQRTEELEEAKKKLA---QRL----------Q 1399
Cdd:PRK04863 349 KIERYQADLeeLEERLEEQNEVVEE-------ADEQQEENEARAE----AAEEEVDELKSQLAdyqQALdvqqtraiqyQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1400 EAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKE----- 1474
Cdd:PRK04863 418 QAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSeawdv 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1475 ARSLSTELFKLKN------AYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEA 1548
Cdd:PRK04863 498 ARELLRRLREQRHlaeqlqQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEA 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1549 easleHEEGKILRAQLEfnQIKAEIERKLAEKDEEME-QAKRNHLR------------VVDSLQTSLDAE---TRSRNEA 1612
Cdd:PRK04863 578 -----RERRMALRQQLE--QLQARIQRLAARAPAWLAaQDALARLReqsgeefedsqdVTEYMQQLLERErelTVERDEL 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1613 LRVKKKMEGDLNEmeiqLSHAN-----RMAAEAQKQVKSLQSLLKDtQIQLDDA---------------VR--------- 1663
Cdd:PRK04863 651 AARKQALDEEIER----LSQPGgsedpRLNALAERFGGVLLSEIYD-DVSLEDApyfsalygparhaivVPdlsdaaeql 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1664 -ANDDLKENIAIVER-----RNNLLQAELEElRAVV----------------------------EQTERSRKLAEQELIE 1709
Cdd:PRK04863 726 aGLEDCPEDLYLIEGdpdsfDDSVFSVEELE-KAVVvkiadrqwrysrfpevplfgraarekriEQLRAEREELAERYAT 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1710 TSERVQL---LHSQNTSLINQK-------------KKMDADLSQLQTEV---EEAVQECRNAEEKAKKAITDAAMMAEEL 1770
Cdd:PRK04863 805 LSFDVQKlqrLHQAFSRFIGSHlavafeadpeaelRQLNRRRVELERALadhESQEQQQRSQLEQAKEGLSALNRLLPRL 884
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1771 KKEQDTSaHLERmkknmeqtIKDLQHRLDEAEQ----IALKGGK-KQLQKLEARVRELENELEAEQKRNAESVKGMRKSE 1845
Cdd:PRK04863 885 NLLADET-LADR--------VEEIREQLDEAEEakrfVQQHGNAlAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAK 955
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1846 RRIKELTYQTE-------EDRKNLL-RLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQ 1917
Cdd:PRK04863 956 QQAFALTEVVQrrahfsyEDAAEMLaKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQM 1035
|
810
....*....|..
gi 119586555 1918 VNKLRAKSRDIG 1929
Cdd:PRK04863 1036 LQELKQELQDLG 1047
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1745-1928 |
1.44e-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: 49.38 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1745 AVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELE 1824
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-ELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1825 NELEAEQKRNAESVKGMRKSERR---------------IKELTY----------QTEEDRKNLLRLQDLVDKLQLKVKAY 1879
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQpplalllspedfldaVRRLQYlkylaparreQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 119586555 1880 KRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1928
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1048-1202 |
1.45e-05 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 50.14 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1048 LERAKRKLEGDLKLTQESIMDLENDKQQLDERLKkkdfELNALNARIEDEQAlgsQLQKKLKELQARieeleeELEAERT 1127
Cdd:COG1193 502 IERARELLGEESIDVEKLIEELERERRELEEERE----EAERLREELEKLRE---ELEEKLEELEEE------KEEILEK 568
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119586555 1128 ARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAE 1202
Cdd:COG1193 569 AREEAEEILREARKEAEELIRELREA-----------QAEEEELKEARKKLEELKQELEEKLEKPKKKAKPAKPP 632
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1382-1612 |
1.58e-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: 49.38 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1382 QRTEELEEAKKKLAQ---RLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWK 1458
Cdd:COG4942 24 EAEAELEQLQQEIAElekELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1459 QKYeesQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLgssgktiHELEKVRKQLEAEK 1538
Cdd:COG4942 104 EEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-------AELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119586555 1539 MELQSALEEAEAslehEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQtSLDAETRSRNEA 1612
Cdd:COG4942 174 AELEALLAELEE----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA-RLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1433-1835 |
1.62e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1433 VERSNAAAAALDKKQRNFDKILAEwKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEhLETFKRENKNLQEEISD 1512
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1513 LTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHL 1592
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1593 RVVDSLQTSLDAETRSRNEAL------------RVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDD 1660
Cdd:COG4717 231 QLENELEAAALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1661 AVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQ--ELIETSERVQLLHSQNTSLINQKKKMDADLSQL 1738
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1739 QTEVEEAVQ---ECRNAEEKAKKAITDAAMMAEELKKEQ--DTSAHLERMKKNMEQTIKDLQHRLDEAE-QIALKGGKKQ 1812
Cdd:COG4717 391 LEQAEEYQElkeELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEELEEELEELREELAELEaELEQLEEDGE 470
|
410 420
....*....|....*....|...
gi 119586555 1813 LQKLEARVRELENELEAEQKRNA 1835
Cdd:COG4717 471 LAELLQELEELKAELRELAEEWA 493
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1473-1931 |
1.63e-05 |
|
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: 50.11 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1473 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASL 1552
Cdd:pfam05483 120 KAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAF 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1553 EHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSH 1632
Cdd:pfam05483 200 EELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1633 ANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSE 1712
Cdd:pfam05483 280 QDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTC 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1713 RVQ-LLHSQNTSLIN---QKKKMDADLSQLQTEVEEAVQECRNAE---EKAKKAITDAAMMAEELKKEQDTSahlERMKK 1785
Cdd:pfam05483 360 SLEeLLRTEQQRLEKnedQLKIITMELQKKSSELEEMTKFKNNKEvelEELKKILAEDEKLLDEKKQFEKIA---EELKG 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1786 NMEQTIKDLQHRLDEAE--QIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLL 1863
Cdd:pfam05483 437 KEQELIFLLQAREKEIHdlEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELK 516
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119586555 1864 RLQDLVDKLQLKVKAYKRQAE---EAEEQANTNLSKFRK--------VQHELDEAEERADIAESQVNKLRAKSRDIGTK 1931
Cdd:pfam05483 517 KHQEDIINCKKQEERMLKQIEnleEKEMNLRDELESVREefiqkgdeVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1091-1646 |
1.69e-05 |
|
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: 49.74 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1091 NARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELE----EISERLEEAGGATSVQIEMNKK 1166
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQkrirLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1167 REAEFQKMRRDLEEATLQhEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDdvtsnmeqIIKAKAANL 1246
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQ-LADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLD--------LLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1247 EKMCRTLEDQMNEhrskaeetqrsvndLTSQRAKLQTENGELSRQLDEKEalISQLTRGKLTYTQQLEDLKRQLEEEVKa 1326
Cdd:pfam05557 152 EQLRQNLEKQQSS--------------LAEAEQRIKELEFEIQSQEQDSE--IVKNSKSELARIPELEKELERLREHNK- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1327 knalahALQSARHDCDLLREQ----------YEEETEAKAELQRVLSKANSEVAQWRTKYETDA--IQRTEELEEAKKKL 1394
Cdd:pfam05557 215 ------HLNENIENKLLLKEEvedlkrklerEEKYREEAATLELEKEKLEQELQSWVKLAQDTGlnLRSPEDLSRRIEQL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1395 AQRLQEAEEAVEAVNAKCSSLEKTKHRLQNE-------IEDLMVDVERSNAAAAALDK------KQRNFDKILAEWKQKY 1461
Cdd:pfam05557 289 QQREIVLKEENSSLTSSARQLEKARRELEQElaqylkkIEDLNKKLKRHKALVRRLQRrvllltKERDGYRAILESYDKE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1462 EESQSELESSQKEARSLSTELFKLKNAYEES-------LEHLETFKRENKNLQEEISDLTEQ-----LGSSGKTIHELEK 1529
Cdd:pfam05557 369 LTMSNYSPQLLERIEEAEDMTQKMQAHNEEMeaqlsvaEEELGGYKQQAQTLERELQALRQQesladPSYSKEEVDSLRR 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1530 VRKQLEAEKMELQSALEEAEASLEHEEgkiLRAQLEFNQIKAeierkLAEKDEEMEQAKRNHLRVVDSLQTSLDAeTRSR 1609
Cdd:pfam05557 449 KLETLELERQRLREQKNELEMELERRC---LQGDYDPKKTKV-----LHLSMNPAAEAYQQRKNQLEKLQAEIER-LKRL 519
|
570 580 590
....*....|....*....|....*....|....*..
gi 119586555 1610 NEALRVKKKMEGDLNEMEIQLshANRMAAEAQKQVKS 1646
Cdd:pfam05557 520 LKKLEDDLEQVLRLPETTSTM--NFKEVLDLRKELES 554
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
843-1014 |
2.12e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 843 AEREKEMASMKEEFTRLKEALEKseaRRKELEEKMVSLLQEKNDLQ-LQVQAEQDNLADAEERCDQLikNKIqleakVKE 921
Cdd:COG3883 61 EALQAEIDKLQAEIAEAEAEIEE---RREELGERARALYRSGGSVSyLDVLLGSESFSDFLDRLSAL--SKI-----ADA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 922 MNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQE 1001
Cdd:COG3883 131 DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
170
....*....|...
gi 119586555 1002 AHQQALDDLQAEE 1014
Cdd:COG3883 211 AAAAAAAAAAAAA 223
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1056-1301 |
2.29e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1056 EGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEeleeeleaerTARAKVEKL 1135
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA----------EAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1136 RSdlsrELEEISERLEEAGGATSvqiemnkkreaefqkmrrdLEEATLQHEATAAALRKkhADSVAELGEQ----IDNLQ 1211
Cdd:COG3883 85 RE----ELGERARALYRSGGSVS-------------------YLDVLLGSESFSDFLDR--LSALSKIADAdadlLEELK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1212 RVKQKLEKEKSEfklelddvtsnmeqiIKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQ 1291
Cdd:COG3883 140 ADKAELEAKKAE---------------LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
250
....*....|
gi 119586555 1292 LDEKEALISQ 1301
Cdd:COG3883 205 LAAAEAAAAA 214
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1341-1553 |
2.86e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.16 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1341 CDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKH 1420
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1421 RLQNEIEDLM------VDVER----SNAAAAALDKKQRNFDKILAEWKQKYEESQSELESS-------QKEARSLSTELF 1483
Cdd:PRK05771 118 ELEQEIERLEpwgnfdLDLSLllgfKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvvLKELSDEVEEEL 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119586555 1484 KlKNAYEE-SLEHLETFKRENKNLQEEISDLTEQLGSsgkTIHELEKVRKQLEAEKM----ELQSALEEAEASLE 1553
Cdd:PRK05771 198 K-KLGFERlELEEEGTPSELIREIKEELEEIEKERES---LLEELKELAKKYLEELLalyeYLEIELERAEALSK 268
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1084-1331 |
3.11e-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: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1084 DFELNALNARIEDEQALGSQLQKKLKELQARIeeleeeleaertarakveklrSDLSRELEEISERLEEAggatsvqiem 1163
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAEL---------------------EELNEEYNELQAELEAL---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1164 nkkrEAEFQKMRRDLEEATLQHEATAAALrKKHADSVAELGEQIDNLQRVkqkLEKEksefklELDDVTSNMEQIIKAKA 1243
Cdd:COG3883 64 ----QAEIDKLQAEIAEAEAEIEERREEL-GERARALYRSGGSVSYLDVL---LGSE------SFSDFLDRLSALSKIAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1244 ANLEKMcRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEE 1323
Cdd:COG3883 130 ADADLL-EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
....*...
gi 119586555 1324 VKAKNALA 1331
Cdd:COG3883 209 EAAAAAAA 216
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
955-1340 |
3.81e-05 |
|
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: 49.07 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 955 DDLELTLAKVEKEKHATENKVKNLTEEMA----GLDEIIAKLTKEKKALQEAH---QQALDDLQAEEDKVN-TLTKAKVK 1026
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVqangELEKASREETFARTALKNARldlRRLFDEKQSEKDKKNkALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1027 LEQQVDDLEGSLEQ-EKKVRMDLERAKRKLEGDLKLTQESIMDLENDKqqlderlkkkDFELNALNARIEDEQALGSQLQ 1105
Cdd:pfam12128 680 ANERLNSLEAQLKQlDKKHQAWLEEQKEQKREARTEKQAYWQVVEGAL----------DAQLALLKAAIAARRSGAKAEL 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1106 KKLKELQARieeleeeleaERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQH 1185
Cdd:pfam12128 750 KALETWYKR----------DLASLGVDPDVIAKLKREIRTLERKIERI-----------AVRRQEVLRYFDWYQETWLQR 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1186 EataaalrkkhadsvaelgeqiDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKAANLeKMCRTLEDQMNEHRSKAE 1265
Cdd:pfam12128 809 R---------------------PRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMER-KASEKQQVRLSENLRGLR 866
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119586555 1266 ETQRSVNDLTSQRAKLQTEnGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEevKAKNALAHALQSARHD 1340
Cdd:pfam12128 867 CEMSKLATLKEDANSEQAQ-GSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIAD--HSGSGLAETWESLREE 938
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1313-1888 |
3.95e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1313 LEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYE--TDAIQRTEELEEA 1390
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1391 KKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLqNEIEDLMVDVERSNAAAAALDKKQ-RNFDKILAEWK---QKYeesqs 1466
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYKELEERH-MKIINDPVYKNRNYINDYFKYKNDiENKKQILSNIDaeiNKY----- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1467 elessqKEARSLSTELFKLKNAYEESlehletfKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALE 1546
Cdd:PRK01156 325 ------HAIIKKLSVLQKDYNDYIKK-------KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1547 EAEASLEHEEGKilraQLEFNQIKAEIERKLAEKDEEmeqakrnhlrvVDSLQTSLDAETRSRNEALRVKKKMEG----- 1621
Cdd:PRK01156 392 FISEILKIQEID----PDAIKKELNEINVKLQDISSK-----------VSSLNQRIRALRENLDELSRNMEMLNGqsvcp 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1622 ----DLNEMEIqlshaNRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEniaiveRRNNLLQAELEELRAVVEQTE 1697
Cdd:PRK01156 457 vcgtTLGEEKS-----NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKK------RKEYLESEEINKSINEYNKIE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1698 RSRklAEQELIETSE-RVQLLHSQNTSLINQKKKMD-ADLSQLQTEVEEA--------VQECRNAEEKAKKAITDAAMMA 1767
Cdd:PRK01156 526 SAR--ADLEDIKIKInELKDKHDKYEEIKNRYKSLKlEDLDSKRTSWLNAlavislidIETNRSRSNEIKKQLNDLESRL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1768 EELKKE-QDTSAHLERMKKNMEQTIKDLQHRLDEAEqiALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSER 1846
Cdd:PRK01156 604 QEIEIGfPDDKSYIDKSIREIENEANNLNNKYNEIQ--ENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIED 681
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 119586555 1847 RIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEE 1888
Cdd:PRK01156 682 NLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1385-1920 |
4.17e-05 |
|
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: 48.49 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1385 EELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKhrlqNEIEDLMVDVERsnaaaAALDKKQRNFDKILAEWKQKyees 1464
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTK----RLIEELKLNLER-----AQTEEAQAKQDSELAKLRVE---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1465 QSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDL----------TEQLGSSGKtihELEKVRKQL 1534
Cdd:pfam05701 109 EMEQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLvserdiaikrAEEAVSASK---EIEKTVEEL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1535 EAEKMELQSALEEAEAS-LEHEEGKIlRAQLEFNQIKAEIERKLAEKDEEMEQAkRNHLRVVDSLQTSLDAetrsrNEAL 1613
Cdd:pfam05701 186 TIELIATKESLESAHAAhLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-----ASAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1614 RVKKK------MEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDdavRANDDLKENIAIVERrnnlLQAELE 1687
Cdd:pfam05701 259 LLDLKaelaayMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIE---KAKDEVNCLRVAAAS----LRSELE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1688 ELRAVVEQTERSRKLAEqelietservqllhsqntslinqkkkmdADLSQLQTEVEEAVQECRNAEEKAKKAitdAAMMA 1767
Cdd:pfam05701 332 KEKAELASLRQREGMAS----------------------------IAVSSLEAELNRTKSEIALVQAKEKEA---REKMV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1768 EELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkgGKKQLQKLEARVRELENELEA---EQKRNAESVKGMRKS 1844
Cdd:pfam05701 381 ELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQ-----AKAAASTVESRLEAVLKEIEAakaSEKLALAAIKALQES 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119586555 1845 ERRiKELTYQTEEDRKNLLRLQDLvdklqlkvKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNK 1920
Cdd:pfam05701 456 ESS-AESTNQEDSPRGVTLSLEEY--------YELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNR 522
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1536-1921 |
4.28e-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: 48.80 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1536 AEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERK-LAEKDEEME-QAKRNHLRVVdslqtsldaetrsrNEAL 1613
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELsARESDLEQDyQAASDHLNLV--------------QTAL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1614 RVKKKME---GDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRN----NLLQAeL 1686
Cdd:COG3096 344 RQQEKIEryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyqQAVQA-L 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1687 EELRAVVEQTERSRKLAEQELIETSERVQLLHSqntSLINQKKKM-DADLSQLQTE-VEEAVQ------ECRNAEEKAKK 1758
Cdd:COG3096 423 EKARALCGLPDLTPENAEDYLAAFRAKEQQATE---EVLELEQKLsVADAARRQFEkAYELVCkiagevERSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1759 AITDAAMMAEELKKEQDTSAHLERMKKNMEQtikdlQHRLDE-AEQIALKGGKK--QLQKLEARVRELENELEAEQKRNA 1835
Cdd:COG3096 500 LLRRYRSQQALAQRLQQLRAQLAELEQRLRQ-----QQNAERlLEEFCQRIGQQldAAEELEELLAELEAQLEELEEQAA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1836 ESVKGMRKSERRIKELTYQTEEDRK---NLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERAD 1912
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAArapAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQ 654
|
....*....
gi 119586555 1913 IAESQVNKL 1921
Cdd:COG3096 655 ALESQIERL 663
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
931-1221 |
4.31e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 931 EMNAELTAKKRkledecsELKRDIDDLELTLAKVEkEKHATENKVKNLTEEMAG--LDEIIAKLTKEKKALQEAHQQald 1008
Cdd:PHA02562 167 EMDKLNKDKIR-------ELNQQIQTLDMKIDHIQ-QQIKTYNKNIEEQRKKNGenIARKQNKYDELVEEAKTIKAE--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1009 dlqaeedkVNTLTKAKVKLEQQVDDLEGSLeqeKKVRMDLERAKRKLEgdlKLTQESIMDLEND-----KQQLDERlkkk 1083
Cdd:PHA02562 236 --------IEELTDELLNLVMDIEDPSAAL---NKLNTAAAKIKSKIE---QFQKVIKMYEKGGvcptcTQQISEG---- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1084 dfelnalNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiem 1163
Cdd:PHA02562 298 -------PDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKA---------- 360
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 119586555 1164 nKKREAEFQKmrrdleeatlqheatAAALRKKHADSVAELGEQIDNLQRVKQKLEKEK 1221
Cdd:PHA02562 361 -KKVKAAIEE---------------LQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1497-1852 |
4.99e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1497 ETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQsalEEAEASLEHEEGKILRAQLEFNQIKAEIERK 1576
Cdd:pfam07888 69 EQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS---EEKDALLAQRAAHEARIRELEEDIKTLTQRV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1577 LaEKDEEMEQAKRNHLRVVDSLQtsldaETRSRNEALRVK-KKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQ 1655
Cdd:pfam07888 146 L-ERETELERMKERAKKAGAQRK-----EEEAERKQLQAKlQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1656 IQLDDAvranddlkeniaivERRNNLLQAELEELRAVveqtersrklaeQELIETSER-VQLLHSQNTSLINQKKKMDAD 1734
Cdd:pfam07888 220 QKLTTA--------------HRKEAENEALLEELRSL------------QERLNASERkVEGLGEELSSMAAQRDRTQAE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1735 LSQLQTEVEE----------AVQECRNAEEKAKKAITDAAMMAEElkKEQDTSAHLERMKKNMEQTIKDLQH------RL 1798
Cdd:pfam07888 274 LHQARLQAAQltlqladaslALREGRARWAQERETLQQSAEADKD--RIEKLSAELQRLEERLQEERMEREKlevelgRE 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 119586555 1799 DEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELT 1852
Cdd:pfam07888 352 KDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
765-1110 |
5.13e-05 |
|
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: 48.40 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 765 FKAGLLGLLEEMR---------DERLSRIITRIQaqsrgvlaRMEYKK--LLERRDSLlvIQWNIRAFMGVKNWPWMKLY 833
Cdd:pfam15818 5 FKTSLLEALEELRmrreaetqyEEQIGKIIVETQ--------ELKWQKetLQNQKETL--AKQHKEAMAVFKKQLQMKMC 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 834 F----KIKPLLKSAEREKEMASmkeeftrLKEALEKSEARRKELEEKmVSLLQEKNDLQLQVQAEQDNLADAEERCDQLI 909
Cdd:pfam15818 75 AleeeKGKYQLATEIKEKEIEG-------LKETLKALQVSKYSLQKK-VSEMEQKLQLHLLAKEDHHKQLNEIEKYYATI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 910 KNKIQLeakVKEMNERLE----DEEEMNAELTAKKRKLEDECSELKRDIDDL--ELTLAKVE-KEKHATEN--------K 974
Cdd:pfam15818 147 TGQFGL---VKENHGKLEqnvqEAIQLNKRLSALNKKQESEICSLKKELKKVtsDLIKSKVTcQYKMGEENinltikeqK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 975 VKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEgslEQEKKVRMDLERAKRK 1054
Cdd:pfam15818 224 FQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALK---ENNQTLERDNELQREK 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 119586555 1055 LegdlKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKE 1110
Cdd:pfam15818 301 V----KENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
871-1223 |
5.35e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 871 KELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSEL 950
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 951 KRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQ 1030
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1031 VDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKE 1110
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1111 LQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1190
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350
....*....|....*....|....*....|...
gi 119586555 1191 ALRKKHADSVAELGEQIDNLQRVKQKLEKEKSE 1223
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1020-1170 |
6.03e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1020 LTKAKVKLEQQVDDLEGSLEQEKK-----VRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARI 1094
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKealleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1095 EDEQALGSQLQKKLKELQARIEELEEEleaertARAKVEKLrSDLSRE------LEEISERLEEAGGATSVQIEMNKKRE 1168
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEE------QLQELERI-SGLTAEeakeilLEKVEEEARHEAAVLIKEIEEEAKEE 185
|
..
gi 119586555 1169 AE 1170
Cdd:PRK12704 186 AD 187
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1596-1808 |
6.31e-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: 47.45 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1596 DSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIV 1675
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1676 ER------RNNLLQ--------AELEELRAVVEQTERSRKLAEQELIETSERvqlLHSQNTSLINQKKKMDADLSQLQTE 1741
Cdd:COG4942 110 LRalyrlgRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAE---LAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119586555 1742 VEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKG 1808
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1423-1923 |
7.35e-05 |
|
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: 47.81 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1423 QNEIEDLMVDVERSNAAAAALDKKQRNFDKILAewKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLEtfkRE 1502
Cdd:pfam05557 20 QMELEHKRARIELEKKASALKRQLDRESDRNQE--LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL---NE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1503 NKNLQEEISDLTEQLGSsgktihELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQlEFNQIKAEIERKLAEKDE 1582
Cdd:pfam05557 95 KESQLADAREVISCLKN------ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS-EAEQLRQNLEKQQSSLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1583 EMEQAKrnHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMaaeaqkqvKSLQSLLKDTQIQLDDAV 1662
Cdd:pfam05557 168 AEQRIK--ELEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNEN--------IENKLLLKEEVEDLKRKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1663 RANDDLKENIAIVERRNNLLQAELEELravvEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEV 1742
Cdd:pfam05557 238 EREEKYREEAATLELEKEKLEQELQSW----VKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1743 EEAVQECRNAEEKakkaITDAAMMAEELK--------------KEQD-TSAHLERMKK--NMEQTIKDLQHRLDEAEQIA 1805
Cdd:pfam05557 314 RELEQELAQYLKK----IEDLNKKLKRHKalvrrlqrrvllltKERDgYRAILESYDKelTMSNYSPQLLERIEEAEDMT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1806 LKGgKKQLQKLEARVRELENELEAEQKRNA--ESVKGMRKSERRIKELTYQTEED---RKNLLRLQDLVDKLQLKVKAYK 1880
Cdd:pfam05557 390 QKM-QAHNEEMEAQLSVAEEELGGYKQQAQtlERELQALRQQESLADPSYSKEEVdslRRKLETLELERQRLREQKNELE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 119586555 1881 RQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRA 1923
Cdd:pfam05557 469 MELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQA 511
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1071-1242 |
8.50e-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: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1071 NDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERL 1150
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1151 EEAGG-----ATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFK 1225
Cdd:COG1579 83 GNVRNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|....*..
gi 119586555 1226 LELDDVTSNMEQIIKAK 1242
Cdd:COG1579 163 AEREELAAKIPPELLAL 179
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1170-1906 |
8.53e-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: 48.12 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1170 EFQKMRRDLEEATLQHEATAAALRKKhadSVAELGEQIDNLQRVKQKLEKEKSE-FKLELDDVTSNMEQIIKAKAANlek 1248
Cdd:TIGR01612 617 EYIKKAIDLKKIIENNNAYIDELAKI---SPYQVPEHLKNKDKIYSTIKSELSKiYEDDIDALYNELSSIVKENAID--- 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1249 mcrtledqMNEHRSKAEETQRSVNDLTSQRAKLQTENGE--LSRQLDEKEALISQLTR-GKLTYTQQLEDLKRQLEEEVK 1325
Cdd:TIGR01612 691 --------NTEDKAKLDDLKSKIDKEYDKIQNMETATVElhLSNIENKKNELLDIIVEiKKHIHGEINKDLNKILEDFKN 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1326 AKNALAHALQSarhdcdllreqYEEETEAkaelqrvLSKANSEVAQWRTKY-ETDAIQRTEElEEAKkklaQRLQEAEEA 1404
Cdd:TIGR01612 763 KEKELSNKIND-----------YAKEKDE-------LNKYKSKISEIKNHYnDQINIDNIKD-EDAK----QNYDKSKEY 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1405 VEAVNAKCSSLEKTKHRLQNEIEDLMVDVER----SNAAAAALDKKQRNFDKILAEWKQKYEESQSEL-ESSQKEARSLS 1479
Cdd:TIGR01612 820 IKTISIKEDEIFKIINEMKFMKDDFLNKVDKfinfENNCKEKIDSEHEQFAELTNKIKAEISDDKLNDyEKKFNDSKSLI 899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1480 TELfklKNAYEESLEHLETFKREN------KNLQEEISD-------LTEQLGSSGKTIHELEKVRK----QLEAEKMELQ 1542
Cdd:TIGR01612 900 NEI---NKSIEEEYQNINTLKKVDeyikicENTKESIEKfhnkqniLKEILNKNIDTIKESNLIEKsykdKFDNTLIDKI 976
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1543 SALEEA--EASLEHEEGKILRAQLEFNQIKAEI----ERKLAEKDEEMEQAKRNHL-RVVDSLQTSLDAETRSRNEALRV 1615
Cdd:TIGR01612 977 NELDKAfkDASLNDYEAKNNELIKYFNDLKANLgknkENMLYHQFDEKEKATNDIEqKIEDANKNIPNIEIAIHTSIYNI 1056
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1616 KKKMEGD------------LNEMEIQLSHANRMaaEAQKQVKSLQSLLKDTQIQLDDAV-RANDDLK-------ENIAIV 1675
Cdd:TIGR01612 1057 IDEIEKEigkniellnkeiLEEAEINITNFNEI--KEKLKHYNFDDFGKEENIKYADEInKIKDDIKnldqkidHHIKAL 1134
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1676 ERRNNLLQAELEELRAVVEQTER-SRKLAEQELIETSERVQllhsQN-TSLINQKKKMDADLSQLQTEVEE------AVQ 1747
Cdd:TIGR01612 1135 EEIKKKSENYIDEIKAQINDLEDvADKAISNDDPEEIEKKI----ENiVTKIDKKKNIYDEIKKLLNEIAEiekdktSLE 1210
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1748 ECRNAEEKAKKAItdAAMMAEELKKEQDTSAHlerMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENEL 1827
Cdd:TIGR01612 1211 EVKGINLSYGKNL--GKLFLEKIDEEKKKSEH---MIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD 1285
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1828 EAE----QKRNAESVKGMRKSERRI--------------KEL-TYQTEEDRKN------LLRLQDLVDKLQL-------- 1874
Cdd:TIGR01612 1286 DKDhhiiSKKHDENISDIREKSLKIiedfseesdindikKELqKNLLDAQKHNsdinlyLNEIANIYNILKLnkikkiid 1365
|
810 820 830
....*....|....*....|....*....|..
gi 119586555 1875 KVKAYKRQAEEAEEQANTNLSKFRKVQHELDE 1906
Cdd:TIGR01612 1366 EVKEYTKEIEENNKNIKDELDKSEKLIKKIKD 1397
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1703-1890 |
8.66e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1703 AEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT-SAHLE 1781
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1782 RMKKNMEQT-----------IKDLQHRLDEAEQIAlKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKE 1850
Cdd:COG3883 94 ALYRSGGSVsyldvllgsesFSDFLDRLSALSKIA-DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 119586555 1851 LTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQA 1890
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
839-1083 |
8.68e-05 |
|
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: 46.98 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 839 LLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQ---------EKNDLQLQVQAEQDNLADAEERCDQLI 909
Cdd:pfam15742 99 VLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQQKLEHAHKvcltdtcilEKKQLEERIKEASENEAKLKQQYQEEQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 910 KNKIQLEAKVKEMNERLEDeeemnaeLTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEemagLDEII 989
Cdd:pfam15742 179 QKRKLLDQNVNELQQQVRS-------LQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQE----LSEKL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 990 AKLTKEKKALQEAHQQALDDLQAEEDKVNtltkakvkleqqvddlegslEQEKKVRMDLERAKRKLEGDLKLTQESIMDL 1069
Cdd:pfam15742 248 SSLQQEKEALQEELQQVLKQLDVHVRKYN--------------------EKHHHHKAKLRRAKDRLVHEVEQRDERIKQL 307
|
250
....*....|....
gi 119586555 1070 ENDKQQLDERLKKK 1083
Cdd:pfam15742 308 ENEIGILQQQSEKE 321
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
837-1281 |
9.01e-05 |
|
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: 47.73 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 837 KPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQlQVQAEQDNLADAEERCDQLIKNKIQLE 916
Cdd:TIGR00606 703 KLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ-KVNRDIQRLKNDIEEQETLLGTIMPEE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 917 AKVKEMNERLEDEEEMNAELTAKKRKLEDECSELkrDIDDLELTLAKVEKEKHATENKVKNLTEEMagldEIIAKLTKEK 996
Cdd:TIGR00606 782 ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKL--QGSDLDRTVQQVNQEKQEKQHELDTVVSKI----ELNRKLIQDQ 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 997 KALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQvddlegSLEQEKKVRMDLERAKRKLEGDLKLTQEsimdLENDKQQL 1076
Cdd:TIGR00606 856 QEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQ------LVELSTEVQSLIREIKDAKEQDSPLETF----LEKDQQEK 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1077 DERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERtaRAKVEKLRSDLSrELEEISERLEEAGGA 1156
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK--ETELNTVNAQLE-ECEKHQEKINEDMRL 1002
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1157 TSVQIEMNKKREAEFQK--MRRDLEEATLQHEATaaalRKKHADSVAELgeQIDNLQRVKQKLEKE----KSEFKLELDD 1230
Cdd:TIGR00606 1003 MRQDIDTQKIQERWLQDnlTLRKRENELKEVEEE----LKQHLKEMGQM--QVLQMKQEHQKLEENidliKRNHVLALGR 1076
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 119586555 1231 VTSNMEQIIKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKL 1281
Cdd:TIGR00606 1077 QKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTL 1127
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1494-1923 |
9.34e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1494 EHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSAL--------EEAEASLEHEEGKILRAQLE 1565
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1566 FNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVK 1645
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1646 SLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLI 1725
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1726 NQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIA 1805
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1806 LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEE 1885
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430
....*....|....*....|....*....|....*...
gi 119586555 1886 AEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRA 1923
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAA 513
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
981-1152 |
9.57e-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: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 981 EMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEgSLEQEKKVRMDLERAKRKLEGdlk 1060
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-ARIKKYEEQLGNVRNNKEYEA--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1061 LTQEsIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIeeleeeleaeRTARAKVEKLRSDLS 1140
Cdd:COG1579 94 LQKE-IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL----------DEELAELEAELEELE 162
|
170
....*....|..
gi 119586555 1141 RELEEISERLEE 1152
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1478-1657 |
1.21e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1478 LSTELFKLKNAYEESLEHLETFKRENKnlqeeISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEG 1557
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1558 KI--LRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVV------DSLQTSLDAET--------------RSRNEALR- 1614
Cdd:COG3206 255 ALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIalraqiAALRAQLQQEAqrilasleaelealQAREASLQa 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 119586555 1615 ----VKKKMEgDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQ 1657
Cdd:COG3206 335 qlaqLEARLA-ELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
859-995 |
1.21e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 859 LKEALEKSEARRKELEEKmvsllqeknDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTA 938
Cdd:COG2433 378 IEEALEELIEKELPEEEP---------EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119586555 939 KKRKL----------EDECSELKRDIDDLELTLAKVEKEKHATENKVKNLtEEMAGLDE--------IIAKLTKE 995
Cdd:COG2433 449 ELSEArseerreirkDREISRLDREIERLERELEEERERIEELKRKLERL-KELWKLEHsgelvpvkVVEKFTKE 522
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1375-1889 |
1.21e-04 |
|
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: 47.27 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1375 KYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRnfdkiL 1454
Cdd:TIGR00618 177 QYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE-----A 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1455 AEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEES------LEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELE 1528
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRArkaaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1529 KVRKQ---LEAEKMELQSAL-EEAEASLEHEEGKILRAQLEfnQIKAEIERKLA-----EKDEEMEQAKRNHLRVVDSLQ 1599
Cdd:TIGR00618 332 AHVKQqssIEEQRRLLQTLHsQEIHIRDAHEVATSIREISC--QQHTLTQHIHTlqqqkTTLTQKLQSLCKELDILQREQ 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1600 TSLDAETRSRNEALRVKKKMEGdlnEMEIQLSHANRMAAEAQKQVKSLqsllKDTQIQLDDAVRANDDLKENIAIVErrn 1679
Cdd:TIGR00618 410 ATIDTRTSAFRDLQGQLAHAKK---QQELQQRYAELCAAAITCTAQCE----KLEKIHLQESAQSLKEREQQLQTKE--- 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1680 NLLQAELE----ELRAVVEQTERSRKLAEQELIETSERVQLLHSQ-NTSLINQKKKMDADLSQLQTEVEEAVQECRNAEE 1754
Cdd:TIGR00618 480 QIHLQETRkkavVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1755 KAKKAITDAamMAEELKKEQDTSAHLERMKK--NMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQK 1832
Cdd:TIGR00618 560 SLKEQMQEI--QQSFSILTQCDNRSKEDIPNlqNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQC 637
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 119586555 1833 RNAESVKGMRKsERRIKELTYQTEEDRKNLLRLQDlvdklqlKVKAYKRQAEEAEEQ 1889
Cdd:TIGR00618 638 SQELALKLTAL-HALQLTLTQERVREHALSIRVLP-------KELLASRQLALQKMQ 686
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
911-1180 |
1.32e-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: 47.04 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 911 NKIQLEAKVKEM-NERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDeiI 989
Cdd:pfam17380 285 SERQQQEKFEKMeQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRE--L 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 990 AKLTKEKKALQEAHQQALDDLQAEEDKVN--------TLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAK----RKLEG 1057
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELERLQMERQQKNervrqeleAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARqrevRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1058 DLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQalgsQLQKKLKELQARIEELEEEleAERTARAKVEKLRS 1137
Cdd:pfam17380 443 ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK----RDRKRAEEQRRKILEKELE--ERKQAMIEEERKRK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 119586555 1138 DLSRELEEIS------ERLEEAGGATSVQIEMNKKREAEfQKMRRDLEE 1180
Cdd:pfam17380 517 LLEKEMEERQkaiyeeERRREAEEERRKQQEMEERRRIQ-EQMRKATEE 564
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
873-1111 |
1.42e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 873 LEEKMVSLLQEKNDLQLqVQAEQDNLADAEERcdqlIKNKIQLEAKVKEMNERLEDEeeMNAELTAKKRKLEDECSELKR 952
Cdd:PRK05771 14 LKSYKDEVLEALHELGV-VHIEDLKEELSNER----LRKLRSLLTKLSEALDKLRSY--LPKLNPLREEKKKVSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 953 DIDDLELTLAKVEKEkhatenkVKNLTEEMAGLDEIIAKLTKEKKALQ--EAHQQALDDLQAEED---KVNTLTKAKVKL 1027
Cdd:PRK05771 87 LIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvFVGTVPEDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1028 EQQVDDLEGSLEQEKK------VRMDLERAKRKLEGDLKLTQESIMDLENDKqQLDERLKKKDFELNALNARIEDeqalg 1101
Cdd:PRK05771 160 LKLESDVENVEYISTDkgyvyvVVVVLKELSDEVEEELKKLGFERLELEEEG-TPSELIREIKEELEEIEKERES----- 233
|
250
....*....|
gi 119586555 1102 sqLQKKLKEL 1111
Cdd:PRK05771 234 --LLEELKEL 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1535-1764 |
1.43e-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: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1535 EAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQakrnhlrvVDSLQTSLDaetrsrnealr 1614
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE--------IDKLQAEIA----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1615 vkkKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIqlDDAVRANDDLKeniAIVERRNNLLQaELEELRAVVE 1694
Cdd:COG3883 76 ---EAEAEIEERREELGERARALYRSGGSVSYLDVLLGSESF--SDFLDRLSALS---KIADADADLLE-ELKADKAELE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1695 QTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAA 1764
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1379-1924 |
1.48e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1379 DAIQRTEELEEAKKKLaqrlqeaEEAVEAVNAKCSSLEKTKHRLQNEIEDlmvdVERSNAAAAALDKKQRNFDKILAEWK 1458
Cdd:PRK01156 156 DEILEINSLERNYDKL-------KDVIDMLRAEISNIDYLEEKLKSSNLE----LENIKKQIADDEKSHSITLKEIERLS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1459 QKYEESQSELESSQKEARSLSTeLFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLG--------SSGKTIHELEKV 1530
Cdd:PRK01156 225 IEYNNAMDDYNNLKSALNELSS-LEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMkiindpvyKNRNYINDYFKY 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1531 RKQLEAEKMELQSAleEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRN 1610
Cdd:PRK01156 304 KNDIENKKQILSNI--DAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1611 EALRVKK---KMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRN-------- 1679
Cdd:PRK01156 382 YSKNIERmsaFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgtt 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1680 ----------NLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTS-LINQKKKMDADLSQLqTEVEEAVQE 1748
Cdd:PRK01156 462 lgeeksnhiiNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADL-EDIKIKINE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1749 CRNAEEKAKKAITDAAMMAEELKKEQDTSaHLERMKKNMEQTIKDLQHRLDEAeqialkggKKQLQKLEARVRELENELE 1828
Cdd:PRK01156 541 LKDKHDKYEEIKNRYKSLKLEDLDSKRTS-WLNALAVISLIDIETNRSRSNEI--------KKQLNDLESRLQEIEIGFP 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1829 AEQKRNAESVkgmrkseRRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQA---EEAEEQANTNLSKFRKVQHELD 1905
Cdd:PRK01156 612 DDKSYIDKSI-------REIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIaeiDSIIPDLKEITSRINDIEDNLK 684
|
570
....*....|....*....
gi 119586555 1906 EAEERADIAESQVNKLRAK 1924
Cdd:PRK01156 685 KSRKALDDAKANRARLEST 703
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1090-1365 |
1.60e-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: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1090 LNARIEDEQALGSQLQKKLKELQARIeeleeeleaeRTARAKVEKLRS-----DLSRELEEISERLEEAggatsvqiemn 1164
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKEL----------EEAEAALEEFRQknglvDLSEEAKLLLQQLSEL----------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1165 kkrEAEFQKMRRDLEEAtlqhEATAAALRKKHADSVAELGEQIDN--LQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAK 1242
Cdd:COG3206 225 ---ESQLAEARAELAEA----EARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALR 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1243 A--ANLEkmcrtledqmnehRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRgkltYTQQLEDLKRQL 1320
Cdd:COG3206 298 AqiAALR-------------AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREV 360
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 119586555 1321 EeevkaknalahalqsarhdcdLLREQYE------EETEAKAELQ----RVLSKA 1365
Cdd:COG3206 361 E---------------------VARELYEsllqrlEEARLAEALTvgnvRVIDPA 394
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1322-1624 |
1.71e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.99 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1322 EEVKAKNALAHALQSARHDCDLLREQYEEETEAKAE--LQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLaQRLQ 1399
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEvlIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQL-QELK 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1400 EAEEAVEAVNAKCSSLEKTKHRLQNEIE-DLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKeaRSL 1478
Cdd:COG5022 889 IDVKSISSLKLVNLELESEIIELKKSLSsDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVE--SKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1479 STELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGkTIHELEKVRKQLEAEKMELQSAleEAEASLEHEEGK 1558
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYG-ALQESTKQLKELPVEVAELQSA--SKIISSESTELS 1043
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119586555 1559 ILR--AQLEFNQIKAeiERKLAEKDEEMEQAKRNHLRvvDSLQTSLDAETRSRNEALRVKKKMEGDLN 1624
Cdd:COG5022 1044 ILKplQKLKGLLLLE--NNQLQARYKALKLRRENSLL--DDKQLYQLESTENLLKTINVKDLEVTNRN 1107
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
777-1261 |
1.81e-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: 46.58 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 777 RDERLSRIITRIQAQSRGVLARMEYKKLLER------------RDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAE 844
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYFPNKKQLEDwlhskskeinqtRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 845 REKEMASMKEEFTRLKEALEKSEARRKELeekmvSLLQEKNDLQLQVQAEqdnLADAEERCDQLIKNKIQLEakvKEMNE 924
Cdd:TIGR00606 627 KLFDVCGSQDEESDLERLKEEIEKSSKQR-----AMLAGATAVYSQFITQ---LTDENQSCCPVCQRVFQTE---AELQE 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 925 RLEDEEEMNAELTAKKRKLEDECSELKRDIDDL-------ELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKK 997
Cdd:TIGR00606 696 FISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG 775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 998 AL---QEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEG-----SLEQEKKVRMDLERAKRKLEGDLKLTQESImdl 1069
Cdd:TIGR00606 776 TImpeEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGsdldrTVQQVNQEKQEKQHELDTVVSKIELNRKLI--- 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1070 eNDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISER 1149
Cdd:TIGR00606 853 -QDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISS 931
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1150 LEEAGGATSVQIEMNKKREAEFQKMRRDLEEATlqhEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELD 1229
Cdd:TIGR00606 932 KETSNKKAQDKVNDIKEKVKNIHGYMKDIENKI---QDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDID 1008
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 119586555 1230 dvTSNMEQ----------IIKAKAANLEKMCRTLEDQMNEHR 1261
Cdd:TIGR00606 1009 --TQKIQErwlqdnltlrKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
843-1086 |
1.82e-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: 46.43 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 843 AEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM 922
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 923 NER-------LEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAK---L 992
Cdd:pfam07888 156 KERakkagaqRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEneaL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 993 TKEKKALQE---AHQQA-------LDDLQAEEDKVNT-LTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKL 1061
Cdd:pfam07888 236 LEELRSLQErlnASERKveglgeeLSSMAAQRDRTQAeLHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEA 315
|
250 260
....*....|....*....|....*
gi 119586555 1062 TQESIMDLENDKQQLDERLKKKDFE 1086
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERME 340
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
843-967 |
1.89e-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: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 843 AEREKEMASMKEEFTRLKEALEKSEARRKELEEKM--VSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVK 920
Cdd:COG1579 48 EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELA 127
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 119586555 921 EMNERLEDEEEmnaELTAKKRKLEDECSELKRDIDDLELTLAKVEKE 967
Cdd:COG1579 128 ELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1235-1448 |
1.94e-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: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1235 MEQIIKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQR--AKLQTENGELSRQLDEKEALISQLTRGKLTYTQQ 1312
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1313 LEDLKRQLEEEVKAKNALAH---------ALQSARHDCDLLREQYEEE----TEAKAELQRVLSKANSEVAQWRTKYETD 1379
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQspviqqlraQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119586555 1380 AiqrtEELEEAKKKLAQRLQEAEEAVEAVNAKcsslektkhrlQNEIEDLMVDVERSNAAAAALDKKQR 1448
Cdd:COG3206 322 L----EALQAREASLQAQLAQLEARLAELPEL-----------EAELRRLEREVEVARELYESLLQRLE 375
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
868-1022 |
1.98e-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: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 868 ARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQL---------------IKNKI--------QLEAKVKEMNE 924
Cdd:pfam15934 41 ENKNEQEQQLKEFTVQNQRLACQIDNLHETLKDRDHQIKQLqsmitgysdisennrLKEEIhdlkqkncVQARVVRKMGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 925 RLEDEEEMNAELTAKKRKL----EDECSELK---RDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLdeiiakltKEKK 997
Cdd:pfam15934 121 ELKGQEEQRVELCDKYESLlgsfEEQCQELKranRRVQSLQTRLSQVEKLQEELRTERKILREEVIAL--------KEKD 192
|
170 180
....*....|....*....|....*....
gi 119586555 998 ALQEAHQQALDD----LQAEEDKVNTLTK 1022
Cdd:pfam15934 193 AKSNGRERALQDqlkcCQTEIEKSRTLIR 221
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
859-1085 |
2.13e-04 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 46.30 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 859 LKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDnladaEERCDQLIKNKIQLEAKVKEMNERLEdeeemnaeltA 938
Cdd:pfam18971 619 LEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQ-----KDEIFALINKEANRDARAIAYTQNLK----------G 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 939 KKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAkLTKEKKALQEAHQQALDDLQAEEDK-V 1017
Cdd:pfam18971 684 IKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLG-INPEWISKVENLNAALNEFKNGKNKdF 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119586555 1018 NTLTKAKVKLEQQVDDLEGSLEQEKKV-RMDLERAKRKLEGDLKLTQESIMDLEN-DKQQLDERLKK-KDF 1085
Cdd:pfam18971 763 SKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfSKEQLAQQAQKnEDF 833
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1490-1629 |
2.16e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1490 EESLEHLeTFKRENKNLQEEISDLTEQ---LGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEF 1566
Cdd:COG2433 379 EEALEEL-IEKELPEEEPEAEREKEHEereLTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE 457
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119586555 1567 NQiKAEIERKLAEKDEEmeqakrnhlrvVDSLQTSLDaETRSRNEALRVKKKMEGDLNEMEIQ 1629
Cdd:COG2433 458 RR-EIRKDREISRLDRE-----------IERLERELE-EERERIEELKRKLERLKELWKLEHS 507
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1326-1460 |
2.21e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1326 AKNALAHALQSARHDCDLLREqyEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAV 1405
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 119586555 1406 EAVNAKCSSLEKTKHRLQNEIEDlmvdversnaaaaaLDKKQRNFDKILAEWKQK 1460
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQE--------------LEKKEEELEELIEEQLQE 143
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1254-1447 |
2.29e-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: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1254 EDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHA 1333
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1334 LQSARHDCDLL---------------REQYEEETEAKAELQRVLSKANSEVAQwrtkYETDAIQRTEELEEAKKKLAQRL 1398
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEA----KKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 119586555 1399 QEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQ 1447
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1670-1918 |
2.51e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1670 ENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQEC 1749
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1750 RNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNMEQTIKDLQHRLDE--AEQIALKGGKKQLQKLEARVREL 1823
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1824 ENELEAEQKRnaesvkgmrkserrikeltyqteedrknllrLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHE 1903
Cdd:COG4942 180 LAELEEERAA-------------------------------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|....*
gi 119586555 1904 LDEAEERADIAESQV 1918
Cdd:COG4942 229 IARLEAEAAAAAERT 243
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1048-1587 |
3.14e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1048 LERAKRKLEGDLKLTQESIMDLENdkqqLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERT 1127
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1128 A--------------RAKVEKLRSDLSRELEE---ISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1190
Cdd:PRK01156 240 AlnelssledmknryESEIKTAESDLSMELEKnnyYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1191 ALRKKHAD--SVAELG---EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQI--IKAKAANLEKMCRTLEDQMNEHRSK 1263
Cdd:PRK01156 320 EINKYHAIikKLSVLQkdyNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIesLKKKIEEYSKNIERMSAFISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1264 AEETQRSVNdltsqraklqTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLE---------------EEVKAKN 1328
Cdd:PRK01156 400 QEIDPDAIK----------KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlGEEKSNH 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1329 ALAH---ALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAqRLQEAEEAV 1405
Cdd:PRK01156 470 IINHyneKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKIN-ELKDKHDKY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1406 EAVNAKCSSLEKTKHRLQNEiEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKL 1485
Cdd:PRK01156 549 EEIKNRYKSLKLEDLDSKRT-SWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1486 KNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQL---EAEKMELQSALEEAEASLEHEEG--KIL 1560
Cdd:PRK01156 628 ANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIndiEDNLKKSRKALDDAKANRARLEStiEIL 707
|
570 580
....*....|....*....|....*...
gi 119586555 1561 RAQL-EFNQIKAEIERKLaEKDEEMEQA 1587
Cdd:PRK01156 708 RTRInELSDRINDINETL-ESMKKIKKA 734
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1674-1812 |
3.73e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1674 IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDAdlsQLQTEVEEAVQECRNAE 1753
Cdd:PRK00409 503 IIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQE---EEDKLLEEAEKEAQQAI 579
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 119586555 1754 EKAKKAITDAAMMAEELKKEQDTSAHLermkKNMEQTIKDLQHRLDEAEQIALKGGKKQ 1812
Cdd:PRK00409 580 KEAKKEADEIIKELRQLQKGGYASVKA----HELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
885-1097 |
3.86e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.07 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 885 NDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKemnerleDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKV 964
Cdd:PRK11637 43 SDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLK-------KQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 965 EKEKHATEnkvKNLTEEM---------AGLDEIIAKLTKEKKALQEAHQQALDdlQAEEDKVNTLTKAKVKLEQQVDDLE 1035
Cdd:PRK11637 116 EQQQAAQE---RLLAAQLdaafrqgehTGLQLILSGEESQRGERILAYFGYLN--QARQETIAELKQTREELAAQKAELE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119586555 1036 GSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLEN----DKQQLDErLKKKDFELNALNARIEDE 1097
Cdd:PRK11637 191 EKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESslqkDQQQLSE-LRANESRLRDSIARAERE 255
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
898-1013 |
3.93e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 898 LADAEERCDQLIKN----------KIQLEAKVKEMNERLEDEEE---MNAELTAKKRKLEDECSELKRDIDDLELTLAKV 964
Cdd:PRK12704 33 IKEAEEEAKRILEEakkeaeaikkEALLEAKEEIHKLRNEFEKElreRRNELQKLEKRLLQKEENLDRKLELLEKREEEL 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 119586555 965 EKEKHATENKVKNLTEEMAGLDEIIAK----------LTKEkkalqEAHQQALDDLQAE 1013
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEqlqelerisgLTAE-----EAKEILLEKVEEE 166
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
834-998 |
4.06e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 834 FKIKPLLKSAEREKEMAS------MKEEFTRLKEALEK-SEARRKELEEKMVSLLQEKNDLqlqvqaeqdnladaEERCD 906
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKkealleAKEEIHKLRNEFEKeLRERRNELQKLEKRLLQKEENL--------------DRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 907 QLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDE---CSELKRDiDDLELTLAKVEKE-KHATENKVKNLTEEm 982
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerISGLTAE-EAKEILLEKVEEEaRHEAAVLIKEIEEE- 181
|
170
....*....|....*.
gi 119586555 983 agldeiiAKLTKEKKA 998
Cdd:PRK12704 182 -------AKEEADKKA 190
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1688-1872 |
4.39e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1688 ELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKK---AITDAA 1764
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1765 MMAEELKKE--------------QDTSAHLERMKKNMEQtIKDLQHRLDEAE--QIALKGGKKQLQKLEARVRELENELE 1828
Cdd:PHA02562 269 SKIEQFQKVikmyekggvcptctQQISEGPDRITKIKDK-LKELQHSLEKLDtaIDELEEIMDEFNEQSKKLLELKNKIS 347
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 119586555 1829 AEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKL 1872
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1141-1411 |
4.55e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.32 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1141 RELEEISERLEEAggatsvqiemnKKR-EAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELgeqidnLQRVKQKLEK 1219
Cdd:PRK05035 439 RAIEQEKKKAEEA-----------KARfEARQARLEREKAAREARHKKAAEARAAKDKDAVAAA------LARVKAKKAA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1220 EKSEFKLELDDVTSNMEQIIKAKAANLEKmcrtledqmnehRSKAEETQRSVNDltsqraklqtengelsrqlDEKEALI 1299
Cdd:PRK05035 502 ATQPIVIKAGARPDNSAVIAAREARKAQA------------RARQAEKQAAAAA-------------------DPKKAAV 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1300 SQ-LTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALqsARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYET 1378
Cdd:PRK05035 551 AAaIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAI--ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKK 628
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 119586555 1379 DAIQRTEELEE---------------AKKKLAQRLQEAEEAVEAVNAK 1411
Cdd:PRK05035 629 AEQQANAEPEEpvdprkaavaaaiarAKARKAAQQQANAEPEEAEDPK 676
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
960-1191 |
4.73e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 960 TLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLE 1039
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1040 qekkvrmdlERAKRKLEG-------DLKLTQESIMDL-----------ENDKQQLDERLKKKDfELNALNARIEDEQAlg 1101
Cdd:COG3883 90 ---------ERARALYRSggsvsylDVLLGSESFSDFldrlsalskiaDADADLLEELKADKA-ELEAKKAELEAKLA-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1102 sQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEA 1181
Cdd:COG3883 158 -ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250
....*....|
gi 119586555 1182 TLQHEATAAA 1191
Cdd:COG3883 237 AAAAAAAASA 246
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1629-1834 |
5.29e-04 |
|
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: 43.86 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1629 QLSHANRMAAEAQKQVKSLQSLLKDTQIQLDdavRANDDLKENiaiverrnnllQAELEELRAVVEQTERSRKLAEQELI 1708
Cdd:pfam00261 23 KLEEAEKRAEKAEAEVAALNRRIQLLEEELE---RTEERLAEA-----------LEKLEEAEKAADESERGRKVLENRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1709 ETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLE------- 1781
Cdd:pfam00261 89 KDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEaseekas 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 119586555 1782 RMKKNMEQTIKDLQHRLDEAEQIALKGgKKQLQKLEARVRELENELEAEQKRN 1834
Cdd:pfam00261 169 EREDKYEEQIRFLTEKLKEAETRAEFA-ERSVQKLEKEVDRLEDELEAEKEKY 220
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
850-1173 |
5.77e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 850 ASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDE 929
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 930 EEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAH-QQALD 1008
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1009 DLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELN 1088
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1089 ALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKRE 1168
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
....*
gi 119586555 1169 AEFQK 1173
Cdd:COG4372 347 LVGLL 351
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
873-1151 |
6.02e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 873 LEEKMVSLLQEKNDLQLQVQAEQDN--------LADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLE 944
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAEPSRlyslyekeIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 945 DECSELKRDIDdlELTLAKVEkekhaTENKVKNLTEEMAGLDEIiakLTKEKKALQEAHQQalDDLQAEEDKVNT--LTK 1022
Cdd:pfam00038 103 NDLVGLRKDLD--EATLARVD-----LEAKIESLKEELAFLKKN---HEEEVRELQAQVSD--TQVNVEMDAARKldLTS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1023 AKVKLEQQVDdlegslEQEKKVRMDLERA-KRKLEgdlKLTQESIMDLEnDKQQLDERLKKKDFELNALNARIEDEQALG 1101
Cdd:pfam00038 171 ALAEIRAQYE------EIAAKNREEAEEWyQSKLE---ELQQAAARNGD-ALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 119586555 1102 SQLQKKLKELQARIEEleeeleaertARAKVEKLRSDLSRELEEISERLE 1151
Cdd:pfam00038 241 ASLERQLAETEERYEL----------QLADYQELISELEAELQETRQEMA 280
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
830-1322 |
6.10e-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: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 830 MKLYFKIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEkndLQLQVQ----------------- 892
Cdd:pfam05557 125 LELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFE---IQSQEQdseivknskselaripe 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 893 --AEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTA---KKRKLEDECSELKRDIDDLELTLAKVEke 967
Cdd:pfam05557 202 leKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPE-- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 968 khATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQalddlqaeedkvntltkakvkLEQQVDDLEGSLEQEKKVRMD 1047
Cdd:pfam05557 280 --DLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRE---------------------LEQELAQYLKKIEDLNKKLKR 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1048 LERAKRKLegdlkltQESIMDLENDKQQLDERLKKKDFELNALNAriedeqalGSQLQKKLKELqarieeleeeleaert 1127
Cdd:pfam05557 337 HKALVRRL-------QRRVLLLTKERDGYRAILESYDKELTMSNY--------SPQLLERIEEA---------------- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1128 arakvEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDleeatlqheaTAAALRKKHADSVAELGEQI 1207
Cdd:pfam05557 386 -----EDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQ----------ESLADPSYSKEEVDSLRRKL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1208 DNLQRVKQKLEKEKSEFKLELddVTSNMEQIIKAKAanlekmCRTLEDQMNehrSKAEETQRSVNDLTsqraKLQTENGE 1287
Cdd:pfam05557 451 ETLELERQRLREQKNELEMEL--ERRCLQGDYDPKK------TKVLHLSMN---PAAEAYQQRKNQLE----KLQAEIER 515
|
490 500 510
....*....|....*....|....*....|....*....
gi 119586555 1288 LSRQL----DEKEALISQLTRGKLTYTQQLEDLKRQLEE 1322
Cdd:pfam05557 516 LKRLLkkleDDLEQVLRLPETTSTMNFKEVLDLRKELES 554
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1573-1927 |
7.51e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.51 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1573 IERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEAlrvkkKMEGDLNEMEIQLSHANRMAAEAQK---QVKSLQS 1649
Cdd:PLN02939 61 SNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRA-----SMQRDEAIAAIDNEQQTNSKDGEQLsdfQLEDLVG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1650 LLKDTQ---IQLDDA-VRANDDLKEniaiVERRNNLLQAELEELRAVVEQTERSRKLAEQELIetseRVQLLHSQntsLI 1725
Cdd:PLN02939 136 MIQNAEkniLLLNQArLQALEDLEK----ILTEKEALQGKINILEMRLSETDARIKLAAQEKI----HVEILEEQ---LE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1726 NQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTS---AHLERMKKNMEQTIKDLQHRLDEAE 1802
Cdd:PLN02939 205 KLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1803 QIALKGGKKQLQKLEARVRELENELEAEQKRNAESV---KGMRKSERRIKELTYQTEEDRKNLLRLQdLVDKLQLKVKAY 1879
Cdd:PLN02939 285 EDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAAlvlDQNQDLRDKVDKLEASLKEANVSKFSSY-KVELLQQKLKLL 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 119586555 1880 KRQAEEAEEQANTnlskfrKVQHELDEAEERADIAESQVNKLRAKSRD 1927
Cdd:PLN02939 364 EERLQASDHEIHS------YIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1476-1911 |
7.64e-04 |
|
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: 44.57 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1476 RSLSTELFKLKNAYEESLEHLEtfkrenKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHE 1555
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLT------LRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1556 EGKiLRAQLEFNQIKAEIERKLA-EKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEiQLSHAN 1634
Cdd:TIGR00618 253 EEQ-LKKQQLLKQLRARIEELRAqEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRA-KLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1635 RMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQ----------AELEELRAVVEQTERSRKLAE 1704
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhihtlqqqktTLTQKLQSLCKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1705 QELIETSE----RVQLLHSQNTSLINQKKKMD-----ADLSQLQTEVEEAVQECRNA-EEKAKKAITDAAMMAEELKKEQ 1774
Cdd:TIGR00618 411 TIDTRTSAfrdlQGQLAHAKKQQELQQRYAELcaaaiTCTAQCEKLEKIHLQESAQSlKEREQQLQTKEQIHLQETRKKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1775 DTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGG-----------KKQLQKLEARVRELENELEAEQKRNAESVKGMRK 1843
Cdd:TIGR00618 491 VVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPltrrmqrgeqtYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ 570
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119586555 1844 SERRIKELTYQTEEDRKNLL----RLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERA 1911
Cdd:TIGR00618 571 SFSILTQCDNRSKEDIPNLQnitvRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA 642
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
800-1064 |
7.90e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 800 EYKKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAEREKEMASMKeeftrlKEALEKSEARRKELEEKMVS 879
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK------AEELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 880 LLQEKNDLQLQVQAEQDNLADAEErcdqlIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRdiddlel 959
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAE-----EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK------- 1709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 960 tlaKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQalddlQAEEDKVNTLTKAKVKLEQQVDDL----- 1034
Cdd:PTZ00121 1710 ---KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-----EEEKKKIAHLKKEEEKKAEEIRKEkeavi 1781
|
250 260 270
....*....|....*....|....*....|.
gi 119586555 1035 -EGSLEQEKKVRMDLERAKRKLEGDLKLTQE 1064
Cdd:PTZ00121 1782 eEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
853-1407 |
8.10e-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: 44.66 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 853 KEEFTRLKEALEKSEARRKELEEKM---VSLLQE-KNDLQLQVQAEQDNLADAEERCDQLIKNK--IQLEAKVKEMNERL 926
Cdd:TIGR01612 1103 KEENIKYADEINKIKDDIKNLDQKIdhhIKALEEiKKKSENYIDEIKAQINDLEDVADKAISNDdpEEIEKKIENIVTKI 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 927 EDEEEMNAELtakkRKLEDECSELKRDIDDLE---------------LTLAKVEKEKHATENKVKNLTEEMAGLDEIiak 991
Cdd:TIGR01612 1183 DKKKNIYDEI----KKLLNEIAEIEKDKTSLEevkginlsygknlgkLFLEKIDEEKKKSEHMIKAMEAYIEDLDEI--- 1255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 992 ltKEKKALQEAHQQALDDLQAEEDKVNT--------LTKAKVKLEQQVDDLEGSLE--QEKKVRMDLERAKRKLEGDLKL 1061
Cdd:TIGR01612 1256 --KEKSPEIENEMGIEMDIKAEMETFNIshdddkdhHIISKKHDENISDIREKSLKiiEDFSEESDINDIKKELQKNLLD 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1062 TQE----------------SIMDLENDKQQLDErLKKKDFELNALNARIEDEQALGSQLQKK------LKELQARIEELE 1119
Cdd:TIGR01612 1334 AQKhnsdinlylneianiyNILKLNKIKKIIDE-VKEYTKEIEENNKNIKDELDKSEKLIKKikddinLEECKSKIESTL 1412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1120 EELEAERTARaKVEKLRSDLSRELEEISERLEEAGGATS------VQIEMNKKREAEFQKMRRDleEATLQHEATAAALr 1193
Cdd:TIGR01612 1413 DDKDIDECIK-KIKELKNHILSEESNIDTYFKNADENNEnvlllfKNIEMADNKSQHILKIKKD--NATNDHDFNINEL- 1488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1194 KKHADSVAELGEQIDnlqRVKQKLEKEKSEFKLELDDVT-------------------SNMEQIIK-------------- 1240
Cdd:TIGR01612 1489 KEHIDKSKGCKDEAD---KNAKAIEKNKELFEQYKKDVTellnkysalaiknkfaktkKDSEIIIKeikdahkkfileae 1565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1241 ---AKAANLEKMCRTLEDQM--NEHRSKAE-ETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTrgkltyTQQLE 1314
Cdd:TIGR01612 1566 kseQKIKEIKKEKFRIEDDAakNDKSNKAAiDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKIS------SFSID 1639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1315 DLKRQLEEEVKAKNALAHALQSarhdcdlLREQYEEETEAKAELQRVLSKANS---EVAQWRTKYETDAIQRTEELEEAK 1391
Cdd:TIGR01612 1640 SQDTELKENGDNLNSLQEFLES-------LKDQKKNIEDKKKELDELDSEIEKieiDVDQHKKNYEIGIIEKIKEIAIAN 1712
|
650
....*....|....*.
gi 119586555 1392 KklaQRLQEAEEAVEA 1407
Cdd:TIGR01612 1713 K---EEIESIKELIEP 1725
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1623-1764 |
9.25e-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: 42.99 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1623 LNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQA---------ELEELRAVV 1693
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119586555 1694 EQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAA 1764
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1579-1923 |
1.04e-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: 43.73 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1579 EKDEEMEQAKRNHLRVVDS---LQTSLDAETRSRNEALR----VKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLL 1651
Cdd:pfam07888 10 EEESHGEEGGTDMLLVVPRaelLQNRLEECLQERAELLQaqeaANRQREKEKERYKRDREQWERQRRELESRVAELKEEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1652 KDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKM 1731
Cdd:pfam07888 90 RQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1732 DADLSQLQTEVEEAVQECRNaeekakkaitdaamMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQ--IALKGG 1809
Cdd:pfam07888 170 EAERKQLQAKLQQTEEELRS--------------LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeAENEAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1810 KKQLQKLEARVRELENELEAeQKRNAESVKGMRksERRIKELTYQTEEDRKNLLRLQDLvdKLQLKVKAYKRQAEEAEEQ 1889
Cdd:pfam07888 236 LEELRSLQERLNASERKVEG-LGEELSSMAAQR--DRTQAELHQARLQAAQLTLQLADA--SLALREGRARWAQERETLQ 310
|
330 340 350
....*....|....*....|....*....|....*.
gi 119586555 1890 ANTNLSKFR--KVQHELDEAEERADIAESQVNKLRA 1923
Cdd:pfam07888 311 QSAEADKDRieKLSAELQRLEERLQEERMEREKLEV 346
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1767-1918 |
1.05e-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: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1767 AEELKKEQDTSAHLERMKKNMEQTIKDLQhrldeaeqialkggkKQLQKLEARVRELENELEAEQKRNAES---VKGMRK 1843
Cdd:COG2433 391 PEEEPEAEREKEHEERELTEEEEEIRRLE---------------EQVERLEAEVEELEAELEEKDERIERLereLSEARS 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1844 SERR-------IKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRqAEEAEEQANT----NLSKFRKvqHELDEAEERAD 1912
Cdd:COG2433 456 EERReirkdreISRLDREIERLERELEEERERIEELKRKLERLKE-LWKLEHSGELvpvkVVEKFTK--EAIRRLEEEYG 532
|
....*.
gi 119586555 1913 IAESQV 1918
Cdd:COG2433 533 LKEGDV 538
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1274-1910 |
1.17e-03 |
|
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: 44.04 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1274 LTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTY--------------------------------TQQLEDLKRQLE 1321
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKTFwspelkkeralrkeeaarisvlkeqyrvtqeeNQHLQLTIQALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1322 EEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSevaqwRTKYETDAIQRT-EELE------------ 1388
Cdd:pfam10174 81 DELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHE-----RQAKELFLLRKTlEEMElrietqkqtlga 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1389 --EAKKKLAQRLQ------EAEEAVEAVNAKCSSLEKTKHRL-----QNEIEDLMVDVE-RSNAAAAALDKKQRNFDKIL 1454
Cdd:pfam10174 156 rdESIKKLLEMLQskglpkKSGEEDWERTRRIAEAEMQLGHLevlldQKEKENIHLREElHRRNQLQPDPAKTKALQTVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1455 AEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQL 1534
Cdd:pfam10174 236 EMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1535 EAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKlaekdEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALR 1614
Cdd:pfam10174 316 TNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEK-----ESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1615 VKKK----MEGDLNEMEIQLSHANRMAAEAQKQVKSLQ-------SLLKDTQIQLDDAVRANDDLKENIaivERRNNLLQ 1683
Cdd:pfam10174 391 VKERkinvLQKKIENLQEQLRDKDKQLAGLKERVKSLQtdssntdTALTTLEEALSEKERIIERLKEQR---EREDRERL 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1684 AELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAitda 1763
Cdd:pfam10174 468 EELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKA---- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1764 ammaeelkkeqDTSAHLERMKKNMEQTIKDLQHrldEAEQIALKGGKKQ--LQKLEARVRELENELEAEQKRNAE----- 1836
Cdd:pfam10174 544 -----------HNAEEAVRTNPEINDRIRLLEQ---EVARYKEESGKAQaeVERLLGILREVENEKNDKDKKIAEleslt 609
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119586555 1837 --SVKGMRKSERRIKELtyQTEEDRKNLLRLQD-LVDKLQLKVKAYKRQAEEAeeqantnLSKFRKVQHELDEAEER 1910
Cdd:pfam10174 610 lrQMKEQNKKVANIKHG--QQEMKKKGAQLLEEaRRREDNLADNSQQLQLEEL-------MGALEKTRQELDATKAR 677
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
852-1106 |
1.18e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.07 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 852 MKEEFTRLKEALEKSEARRK----ELEEKMVSLLQEKN------------DLQLQVQAEQDNLADAEERCDQLIKNKIQL 915
Cdd:PLN03229 484 LQERLENLREEFSKANSQDQlmhpVLMEKIEKLKDEFNkrlsrapnylslKYKLDMLNEFSRAKALSEKKSKAEKLKAEI 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 916 EAKVKEMNERLEDEEEMNAeltakkRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMaGLDEIIAKltke 995
Cdd:PLN03229 564 NKKFKEVMDRPEIKEKMEA------LKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSM-GLEVIGVT---- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 996 KKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKkvrmdLERAKRKLEGDLKlTQESIMDLEND-KQ 1074
Cdd:PLN03229 633 KKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSKIELLK-----LEVAKASKTPDVT-EKEKIEALEQQiKQ 706
|
250 260 270
....*....|....*....|....*....|....*...
gi 119586555 1075 QLDE-----RLKKKDFELNA-LNARIEDEQALGSQLQK 1106
Cdd:PLN03229 707 KIAEalnssELKEKFEELEAeLAAARETAAESNGSLKN 744
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1076-1238 |
1.25e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1076 LDERLKKKDFELNALNARIED-------EQALGSQLQKKLKELQARIEELEEEleaertaRAKVEKLRSDLSRELEEISE 1148
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAEladllslERQGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1149 RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAAL---RKKHADS---VAELGEQIDN--LQRVKQkLEKE 1220
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALdasEKRDRESqakIADLGRRLNValAQRVQE-LNRY 195
|
170
....*....|....*...
gi 119586555 1221 KSEFKLELDDVTSNMEQI 1238
Cdd:PRK09039 196 RSEFFGRLREILGDREGI 213
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1650-1924 |
1.26e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 44.16 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1650 LLKDTQIQLDDAVRANDDLKEniaiverrnnlLQAELEELRAVVEQTERSRKLAE-QELietseRVQLLHSQNTSLINQK 1728
Cdd:PLN03188 951 LLKEKYENHPEVLRTKIELKR-----------VQDELEHYRNFYDMGEREVLLEEiQDL-----RSQLQYYIDSSLPSAR 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1729 KK---------MDADLSQLQTEVEEAVQECrnAEEKAKK-------AITDAAMMAEELKKEQDTSAHLERMKKNMEQTIK 1792
Cdd:PLN03188 1015 KRnsllkltysCEPSQAPPLNTIPESTDES--PEKKLEQerlrwteAESKWISLAEELRTELDASRALAEKQKHELDTEK 1092
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1793 DLQHRLDEAEQIALKGGKKQLQK----------LEARVRELENELEAEQKrnAESVKGMRKSERR--------IKELTYQ 1854
Cdd:PLN03188 1093 RCAEELKEAMQMAMEGHARMLEQyadleekhiqLLARHRRIQEGIDDVKK--AAARAGVRGAESKfinalaaeISALKVE 1170
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119586555 1855 TEEDRKnllRLQDLVDKLQLKVkaykRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAE-------SQVNKLRAK 1924
Cdd:PLN03188 1171 REKERR---YLRDENKSLQAQL----RDTAEAVQAAGELLVRLKEAEEALTVAQKRAMDAEqeaaeayKQIDKLKRK 1240
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
914-1115 |
1.27e-03 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 43.80 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 914 QLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 993
Cdd:PRK15374 103 QLESRLAVWQAMIESQKEMGIQVSKEFQTALGEAQEATDLYEASIKKTDTAKSVYDAAEKKLTQAQNKLQSLDPADPGYA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 994 KEKKALQEAHQQALDDLQAEEDK----VNTLTKAKVKLEQQvDDLEGSLEQEKKVRMDLERAK---RKLEGDLKLTQESI 1066
Cdd:PRK15374 183 QAEAAVEQAGKEATEAKEALDKAtdatVKAGTDAKAKAEKA-DNILTKFQGTANAASQNQVSQgeqDNLSNVARLTMLMA 261
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 119586555 1067 MDLENDKQQLDERLKKkdfELNALNARIEDEQAlgsQLQKKLKELQARI 1115
Cdd:PRK15374 262 MFIEIVGKNTEESLQN---DLALFNALQEGRQA---EMEKKSAEFQEET 304
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1210-1335 |
1.40e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 41.46 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1210 LQRVKQkLEKEKSEFKLELDDVTSNMEQIIKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELS 1289
Cdd:pfam08614 13 LDRTAL-LEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 119586555 1290 RQLDEKEALISQLTRGKltytQQLEDLKRQLEEEVKAKNALAHALQ 1335
Cdd:pfam08614 92 KKLREDERRLAALEAER----AQLEEKLKDREEELREKRKLNQDLQ 133
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1128-1362 |
1.42e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.99 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1128 ARAKVEKLRSDLSRELEEISERLEEaggatsvqiEMNKKR--EAEFQKMRRDLEEATLQH---EATA-------AALRKK 1195
Cdd:pfam00038 69 ERARLQLELDNLRLAAEDFRQKYED---------ELNLRTsaENDLVGLRKDLDEATLARvdlEAKIeslkeelAFLKKN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1196 HADSVAELGEQIDNLQRVkqklekeksefkLELDDVTS-NMEQIIKAKAANLEKMC-RTLEDQMNEHRSKAEETQRSVND 1273
Cdd:pfam00038 140 HEEEVRELQAQVSDTQVN------------VEMDAARKlDLTSALAEIRAQYEEIAaKNREEAEEWYQSKLEELQQAAAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1274 LTSQRAKLQTENGELSRQLDEKEALISQLTRgkltytqQLEDLKRQLEEevkAKNALAHALQSARhdcDLLREQYEEETE 1353
Cdd:pfam00038 208 NGDALRSAKEEITELRRTIQSLEIELQSLKK-------QKASLERQLAE---TEERYELQLADYQ---ELISELEAELQE 274
|
....*....
gi 119586555 1354 AKAELQRVL 1362
Cdd:pfam00038 275 TRQEMARQL 283
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
846-1115 |
1.49e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.59 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 846 EKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDN--LADAEERCDQLIKNKIQLEAKVKEmN 923
Cdd:pfam09731 160 KAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPplLDAAPETPPKLPEHLDNVEEKVEK-A 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 924 ERLEDEEEMNAELTAKKRklEDECSELKRDIDDLELTLAKVEKEKHATENKVknLTEEMAGLDEIIAKLTKEKKALQEAH 1003
Cdd:pfam09731 239 QSLAKLVDQYKELVASER--IVFQQELVSIFPDIIPVLKEDNLLSNDDLNSL--IAHAHREIDQLSKKLAELKKREEKHI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1004 QQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMD-----LENDKQQLDE 1078
Cdd:pfam09731 315 ERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEhlkdvLVEQEIELQR 394
|
250 260 270
....*....|....*....|....*....|....*..
gi 119586555 1079 RLKKKdfelnaLNARIEDEQALgsqLQKKLKELQARI 1115
Cdd:pfam09731 395 EFLQD------IKEKVEEERAG---RLLKLNELLANL 422
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1389-1620 |
1.51e-03 |
|
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: 43.21 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1389 EAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSEL 1468
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1469 ESSQKEARSLSTELFKLKNAYEESL----EHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSA 1544
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119586555 1545 LEEAEASleheegkilraqlefnqiKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKME 1620
Cdd:COG4942 180 LAELEEE------------------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1188-1304 |
1.54e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1188 TAAALRKKHADSVAElgeQIDNLQRVKQKLEKEKSEFKLELDDVTsnmeqiiKAKAANLEKMCRTLEDQMNEHRSKAEET 1267
Cdd:COG0542 397 EAAARVRMEIDSKPE---ELDELERRLEQLEIEKEALKKEQDEAS-------FERLAELRDELAELEEELEALKARWEAE 466
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 119586555 1268 QRSVNDLTSQRAKLQTENG---ELSRQLDEKEALISQLTR 1304
Cdd:COG0542 467 KELIEEIQELKEELEQRYGkipELEKELAELEEELAELAP 506
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1071-1851 |
1.61e-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: 43.79 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1071 NDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAE-------RTARAKVEKLRSdLSREL 1143
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnlvQTALRQQEKIER-YQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1144 EEISERLEEAGGAtsvqiemnkkreaefqkmrrdLEEATLQHEATAAALRKKHaDSVAELGEQIDNLQRV---------- 1213
Cdd:COG3096 357 EELTERLEEQEEV---------------------VEEAAEQLAEAEARLEAAE-EEVDSLKSQLADYQQAldvqqtraiq 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1214 -KQKLE-KEKSEFKLELDDVT----SNMEQIIKAKAANLEKMCRTLEDQMN---EHRS---KAEETQRSVNDLTSQRAKL 1281
Cdd:COG3096 415 yQQAVQaLEKARALCGLPDLTpenaEDYLAAFRAKEQQATEEVLELEQKLSvadAARRqfeKAYELVCKIAGEVERSQAW 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1282 QTENgELSRQLDEKEALISQLTrgklTYTQQLEDLKRQLEEEVKAK---NALAHALQSARHDCDLLREQYEEETEAKAEL 1358
Cdd:COG3096 495 QTAR-ELLRRYRSQQALAQRLQ----QLRAQLAELEQRLRQQQNAErllEEFCQRIGQQLDAAEELEELLAELEAQLEEL 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1359 QRVLSKANSEVAQWRtkyetdaiQRTEELEEAKKKLAQR---LQEAEEAVEAVNAKC-----SSLEKTKHR---LQNEIE 1427
Cdd:COG3096 570 EEQAAEAVEQRSELR--------QQLEQLRARIKELAARapaWLAAQDALERLREQSgealaDSQEVTAAMqqlLERERE 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1428 dlmVDVERSNAAAA--ALDKKQRN-------FDKILAEWKQKYeesqselessqkeARSLSTELFK---LKNA-YEESL- 1493
Cdd:COG3096 642 ---ATVERDELAARkqALESQIERlsqpggaEDPRLLALAERL-------------GGVLLSEIYDdvtLEDApYFSALy 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1494 ---------EHLETFKRENKNLQEEISDL-----TEQLGS-SGKTIHELEK---VR-----------------------K 1532
Cdd:COG3096 706 gparhaivvPDLSAVKEQLAGLEDCPEDLyliegDPDSFDdSVFDAEELEDavvVKlsdrqwrysrfpevplfgraareK 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1533 QLEAEKMELQsALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEME-QAKRNHLRVVDSLQTSLDAETRSRNE 1611
Cdd:COG3096 786 RLEELRAERD-ELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAElAALRQRRSELERELAQHRAQEQQLRQ 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1612 ALRVKKKMEGDLNEMeiqLSHANRMAAEaqkqvkSLQSLLKDTQIQLDDAVRANDDLKEN---IAIVERRNNLLQ---AE 1685
Cdd:COG3096 865 QLDQLKEQLQLLNKL---LPQANLLADE------TLADRLEELREELDAAQEAQAFIQQHgkaLAQLEPLVAVLQsdpEQ 935
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1686 LEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLS-QLQTEVEEAVQECRNAEEKAKKA---IT 1761
Cdd:COG3096 936 FEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSDLNeKLRARLEQAEEARREAREQLRQAqaqYS 1015
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1762 DAAMMAEELKKEQDTSAhleRMKKNMEQTIKDLQHRLD-EAEQIAlkggkkqlqklEARVRELENELEAEQKRNAESVKG 1840
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQ---QTLQELEQELEELGVQADaEAEERA-----------RIRRDELHEELSQNRSRRSQLEKQ 1081
|
890
....*....|.
gi 119586555 1841 MRKSERRIKEL 1851
Cdd:COG3096 1082 LTRCEAEMDSL 1092
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
852-998 |
1.73e-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: 42.83 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 852 MKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAeercdQLIKNKI-QLEAKVKEMNERLEdee 930
Cdd:pfam10186 17 ARNRLYELRVDLARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKL-----RLLKSEVaISNERLNEIKDKLD--- 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119586555 931 EMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 998
Cdd:pfam10186 89 QLRREIAEKKKKIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRS 156
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1563-1837 |
1.81e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.50 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1563 QLEFNQIKAEIERklAEKDEEMEQAKrnhlrVVDSLQTSLDAetrsrnealrvkkkmegdLNEMEIqlshANRMAAEAQK 1642
Cdd:PRK10929 22 APDEKQITQELEQ--AKAAKTPAQAE-----IVEALQSALNW------------------LEERKG----SLERAKQYQQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1643 QVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAE---LEELRAVVEQTERSRKLAE-------------QE 1706
Cdd:PRK10929 73 VIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSsqlLEKSRQAQQEQDRAREISDslsqlpqqqtearRQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1707 LIETSERVQLLHSQNTSLiNQkkkmdADLSQLQteveeavqecrnAEEKAKKAITDaammaeELKkeqdtsahLERMKKN 1786
Cdd:PRK10929 153 LNEIERRLQTLGTPNTPL-AQ-----AQLTALQ------------AESAALKALVD------ELE--------LAQLSAN 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 119586555 1787 MEQTIKDLQHRLdeaeqialkgGKKQLQKLEARVRELENELEAEQKRNAES 1837
Cdd:PRK10929 201 NRQELARLRSEL----------AKKRSQQLDAYLQALRNQLNSQRQREAER 241
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
948-1256 |
1.92e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 948 SELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKL 1027
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1028 EQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIE--DEQALGSQLQ 1105
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1106 KKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEA----GGATSVQIEMNKKREAEFQKMRRDLEEA 1181
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAlsalLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119586555 1182 TLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKAANLEKMCRTLEDQ 1256
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
846-1036 |
1.94e-03 |
|
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: 43.29 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 846 EKEMASMKEEFTR-LKEALEKSEARRKELEE----KMVSLLQEKNDLQLQVQAEQDNLAdaEERCDQLIK------NKIQ 914
Cdd:pfam12128 695 DKKHQAWLEEQKEqKREARTEKQAYWQVVEGaldaQLALLKAAIAARRSGAKAELKALE--TWYKRDLASlgvdpdVIAK 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 915 LEAKVKEMNERLEDEEEMNAE------------------LTAKKRKLEDECSELK----RDIDDLELTLAKVEKEKHATE 972
Cdd:pfam12128 773 LKREIRTLERKIERIAVRRQEvlryfdwyqetwlqrrprLATQLSNIERAISELQqqlaRLIADTKLRRAKLEMERKASE 852
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119586555 973 NKVKNLTEEMAGLDEIIAKLT--KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEG 1036
Cdd:pfam12128 853 KQQVRLSENLRGLRCEMSKLAtlKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKN 918
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
841-1082 |
2.22e-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: 42.96 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVK 920
Cdd:pfam07888 144 RVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 921 EMNERLEDEEEMNAELTAKKRKLE--DECSE-LKRDIDDLELTLAKVEKEKHATENKVKNLTEEMA----GLDEIIAKLT 993
Cdd:pfam07888 224 TAHRKEAENEALLEELRSLQERLNasERKVEgLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLAdaslALREGRARWA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 994 KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKV-RMDLERAKRKLE---GDLKLTQESIMDL 1069
Cdd:pfam07888 304 QERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCnRVQLSESRRELQelkASLRVAQKEKEQL 383
|
250
....*....|...
gi 119586555 1070 ENDKQQLDERLKK 1082
Cdd:pfam07888 384 QAEKQELLEYIRQ 396
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1586-1860 |
2.24e-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: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1586 QAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSllkdtqiQLDDAVRAN 1665
Cdd:pfam15905 66 QKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEK-------QLLELTRVN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1666 DDLKENIAI--VERRNNLLQAELEELRAVVEQTERSrKLAEQELIEtserVQLLHSQNTslINQKKKMDADLSQLQTEVE 1743
Cdd:pfam15905 139 ELLKAKFSEdgTQKKMSSLSMELMKLRNKLEAKMKE-VMAKQEGME----GKLQVTQKN--LEHSKGKVAQLEEKLVSTE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1744 EAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlkggKKQLQKLEARVREL 1823
Cdd:pfam15905 212 KEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL----SKQIKDLNEKCKLL 287
|
250 260 270
....*....|....*....|....*....|....*...
gi 119586555 1824 ENELEAEQKRNAESVKGMRKSERRIKE-LTYQTEEDRK 1860
Cdd:pfam15905 288 ESEKEELLREYEEKEQTLNAELEELKEkLTLEEQEHQK 325
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
847-1043 |
2.31e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 847 KEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM---- 922
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESergr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 923 ----NERLEDEEEMN---AELTAKKRKLED---ECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKL 992
Cdd:pfam00261 81 kvleNRALKDEEKMEileAQLKEAKEIAEEadrKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 119586555 993 -TKEKKALQ------EAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKK 1043
Cdd:pfam00261 161 eASEEKASEredkyeEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1024-1428 |
2.35e-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: 42.81 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1024 KVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDfelNALNARIEDEQALGSQ 1103
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAE---EALREQAELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1104 LQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSvQIEMNKKREAEFQKMRRDLEEAtl 1183
Cdd:pfam05557 85 LEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQE-RLDLLKAKASEAEQLRQNLEKQ-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1184 QHEATAAALRKK--------HADSVAELG------EQIDNLQRVKQKLEKE----------KSEFKLELDDVTSNMEQI- 1238
Cdd:pfam05557 162 QSSLAEAEQRIKelefeiqsQEQDSEIVKnskselARIPELEKELERLREHnkhlnenienKLLLKEEVEDLKRKLEREe 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1239 -IKAKAANLEKMCRTLEDQMNEHRSKAEETQ---RSVNDLTSQRAKLQT-------ENGELSRQLDEKEALISQLTRGKL 1307
Cdd:pfam05557 242 kYREEAATLELEKEKLEQELQSWVKLAQDTGlnlRSPEDLSRRIEQLQQreivlkeENSSLTSSARQLEKARRELEQELA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1308 TYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLR---EQYEEETeakaelqrvlskANSEVAQWRTKYETDAIQRT 1384
Cdd:pfam05557 322 QYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRailESYDKEL------------TMSNYSPQLLERIEEAEDMT 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 119586555 1385 EELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEK--TKHRLQNEIED 1428
Cdd:pfam05557 390 QKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERelQALRQQESLAD 435
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1165-1321 |
2.38e-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: 43.13 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1165 KKREAEFQKMRRDLEEATLQheATAAALRKKHADS-VAELGEQIDNLqrvkqkleKEKSEFKLEldDVtsnmeqiIKAKA 1243
Cdd:pfam05911 20 EKAEAEALALKQQLESVTLQ--KLTAEERAAHLDGaLKECMQQLRNV--------KEEQEQKIH--DV-------VLKKT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119586555 1244 ANLEKMCRTLEDQMNEhrskaeetqrsvndlTSQR-AKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLE 1321
Cdd:pfam05911 81 KEWEKIKAELEAKLVE---------------TEQElLRAAAENDALSRSLQERENLLMKLSEEKSQAEAEIEALKSRLE 144
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1641-1887 |
2.55e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1641 QKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHsQ 1720
Cdd:pfam02029 69 AKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWS-T 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1721 NTSLINQKKKMDADLSQLQTEVE------EAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDL 1794
Cdd:pfam02029 148 EVRQAEEEGEEEEDKSEEAEEVPtenfakEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1795 ----QHRLDEAEQIALKGGKKQLQKLEARVRELENElEAEQKRNA--------ESVKGMRKSERRIKELTYQTEEDRKNL 1862
Cdd:pfam02029 228 gglsQSQEREEEAEVFLEAEQKLEELRRRRQEKESE-EFEKLRQKqqeaelelEELKKKREERRKLLEEEEQRRKQEEAE 306
|
250 260
....*....|....*....|....*
gi 119586555 1863 LRLQDLVDKLQLKVKAYKRQAEEAE 1887
Cdd:pfam02029 307 RKLREEEEKRRMKEEIERRRAEAAE 331
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
839-1112 |
2.55e-03 |
|
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: 42.85 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 839 LLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEekmvsllQEKNDLqlqvqaeQDNLADAEERCDQLIKNKIQLEAK 918
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQ-------QERDEL-------ADEIASGASGKSALQDEKRRLEAR 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 919 VKEMNERLEdEEEMNAELTAKK-RKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEmagldeiiakltkekk 997
Cdd:pfam01576 891 IAQLEEELE-EEQSNTELLNDRlRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAK---------------- 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 998 alqeahqqalddLQAEEDKVNTLTKAKVK-LEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQL 1076
Cdd:pfam01576 954 ------------LQEMEGTVKSKFKSSIAaLEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQY 1021
|
250 260 270
....*....|....*....|....*....|....*.
gi 119586555 1077 DERLKKKDFELNALNARIEDEQALGSQLQKKLKELQ 1112
Cdd:pfam01576 1022 KDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQ 1057
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
923-1320 |
2.64e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 923 NERLEDEEEMNAEL-TAKKRKLEDEcsELKRDIDDLELTL---AKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 998
Cdd:PRK11281 32 NGDLPTEADVQAQLdALNKQKLLEA--EDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 999 LQEAHQQALDDLQAEEdkvntltkakvkLEQQVDDLEGSLEQekkVRMDL--------------ERAKRKLEGDLKLTQE 1064
Cdd:PRK11281 110 NDEETRETLSTLSLRQ------------LESRLAQTLDQLQN---AQNDLaeynsqlvslqtqpERAQAALYANSQRLQQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1065 ----SIMDLENDKQQLDERLKKKDFELNALNARIEDEQAL---GSQLQ----KKLKELQARIEELEEELEAERTArakVE 1133
Cdd:PRK11281 175 irnlLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSlegNTQLQdllqKQRDYLTARIQRLEHQLQLLQEA---IN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1134 KLRSDLSRELEEISERLEEAGgatsvQIEMNK--KREAEF-QKMRRDLEEATLQ-HEATAAALRKKHA-DSVAE----LG 1204
Cdd:PRK11281 252 SKRLTLSEKTVQEAQSQDEAA-----RIQANPlvAQELEInLQLSQRLLKATEKlNTLTQQNLRVKNWlDRLTQsernIK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1205 EQIDNLQ------RV--KQKLekeksefKLELDDVTSNM-EQIikakaANLekmcRTLEDQMNEHRSKAEETQRSVNDLt 1275
Cdd:PRK11281 327 EQISVLKgslllsRIlyQQQQ-------ALPSADLIEGLaDRI-----ADL----RLEQFEINQQRDALFQPDAYIDKL- 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 119586555 1276 sqrakLQTENGELSRQldEKEALISQL-TRGKLtytqqLEDLKRQL 1320
Cdd:PRK11281 390 -----EAGHKSEVTDE--VRDALLQLLdERREL-----LDQLNKQL 423
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
852-1577 |
2.69e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.90 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 852 MKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMN-------- 923
Cdd:PTZ00440 726 YTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISndinilke 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 924 ----------------ERLEDEEEMNAE-------------LTAKKRKLEDECSELKRDID----DLEL------TLAKV 964
Cdd:PTZ00440 806 nkknnqdllnsyniliQKLEAHTEKNDEelkqllqkfptedENLNLKELEKEFNENNQIVDniikDIENmnkninIIKTL 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 965 EKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQ-------EAHQQALDDLQAEEDKVNT------LTKAKVKLEQQV 1031
Cdd:PTZ00440 886 NIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINtdniiqkNEKLNLLNNLNKEKEKIEKqlsdtkINNLKMQIEKTL 965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1032 D-----------DLEGSLEQEKKVRMDLERAKRKLEG---DLKLTQESIMDLENDKQQ-----LDERLKKKDfelNALNA 1092
Cdd:PTZ00440 966 EyydkskeningNDGTHLEKLDKEKDEWEHFKSEIDKlnvNYNILNKKIDDLIKKQHDdiielIDKLIKEKG---KEIEE 1042
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1093 RIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEE-----AGGATSVQIEMNKKR 1167
Cdd:PTZ00440 1043 KVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEiknksHEHVVNADKEKNKQT 1122
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1168 EAeFQKMRRDLEEATLQHEATAAALRKKH-----ADSVAELGEQIDNL--QRVKQKLEKEKSEFKLELDDVTSNMEQIIK 1240
Cdd:PTZ00440 1123 EH-YNKKKKSLEKIYKQMEKTLKELENMNleditLNEVNEIEIEYERIliDHIVEQINNEAKKSKTIMEEIESYKKDIDQ 1201
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1241 AKAANL-EKMCRTLEDQMNEHRSKAEETQRSVNDLTsQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQ 1319
Cdd:PTZ00440 1202 VKKNMSkERNDHLTTFEYNAYYDKATASYENIEELT-TEAKGLKGEANRSTNVDELKEIKLQVFSYLQQVIKENNKMENA 1280
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1320 LeEEVKAKNALAHALQSARHDCDLLREQYEEET---EAKAELQ---RVLSKANSEVAQWRT-KYETDAIQRTEELEEAKK 1392
Cdd:PTZ00440 1281 L-HEIKNMYEFLISIDSEKILKEILNSTKKAEEfsnDAKKELEktdNLIKQVEAKIEQAKEhKNKIYGSLEDKQIDDEIK 1359
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1393 KLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEdlmvDVERSNAAAAALDKKQRNFDKILAEWK-QKYEESQSELESS 1471
Cdd:PTZ00440 1360 KIEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVR----NASRGKDKIDFLNKHEAIEPSNSKEVNiIKITDNINKCKQY 1435
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1472 QKEARSLSTELFKLKNA---YEESLEH-------------LETFKRENKNLQEEI----SDLTEQLGSSGKTIHELEKVR 1531
Cdd:PTZ00440 1436 SNEAMETENKADENNDSiikYEKEITNilnnssilgkktkLEKKKKEATNIMDDIngehSIIKTKLTKSSEKLNQLNEQP 1515
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 119586555 1532 KQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKL 1577
Cdd:PTZ00440 1516 NIKREGDVLNNDKSTIAYETIQYNLGRVKHNLLNILNIKDEIETIL 1561
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
902-1043 |
2.84e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 902 EERCDQLIKNKIQLEAKVKEMNErleDEEEMNAELTakkrkledECSELKRDIDDLELTL-AKVEKEKHATENKVKNLTE 980
Cdd:smart00787 136 EWRMKLLEGLKEGLDENLEGLKE---DYKLLMKELE--------LLNSIKPKLRDRKDALeEELRQLKQLEDELEDCDPT 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119586555 981 EMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKK 1043
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1750-1915 |
2.90e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1750 RNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQTIKDLQHRLdeaeqialkggkkqLQKLEARVRELENELEA 1829
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKE------AEAIKKEALLEAKEEIHKL--------------RNEFEKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1830 EQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQAnTNLSKFRKVQHELDEAEE 1909
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI-SGLTAEEAKEILLEKVEE 165
|
....*...
gi 119586555 1910 --RADIAE 1915
Cdd:PRK12704 166 eaRHEAAV 173
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1735-1921 |
3.05e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1735 LSQLQTEVEEAVQECRNAEEK---AKKAITDAAMMAEELKKE-QDTSAHLERMKKNMEQTikdlQHRLDEAEQIA----- 1805
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKleeAEKRAEKAEAEVAALNRRiQLLEEELERTEERLAEA----LEKLEEAEKAAdeser 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1806 -LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTE--EDRKNLL--RLQDLVDKLQL---KVK 1877
Cdd:pfam00261 79 gRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraEERAELAesKIVELEEELKVvgnNLK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 119586555 1878 AYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKL 1921
Cdd:pfam00261 159 SLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL 202
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
840-1017 |
3.23e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 42.31 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 840 LKSAEREKEmaSMKEEFTRLK-----------EALEKSEARRKELEEKMVSLlQEKNDLQ-------LQVQAEQDNLADA 901
Cdd:NF033838 206 IKQAKAKVE--SKKAEATRLEkiktdrekaeeEAKRRADAKLKEAVEKNVAT-SEQDKPKrrakrgvLGEPATPDKKEND 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 902 EERCDQLI-------------KNKIQLEAKVKEMNERLED--EEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEK 966
Cdd:NF033838 283 AKSSDSSVgeetlpspslkpeKKVAEAEKKVEEAKKKAKDqkEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEA 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 119586555 967 EKHATENKVKNLTEEMAGLDEIIAKLTK----EKKALQEAHQQAlddlqAEEDKV 1017
Cdd:NF033838 363 KEPRNEEKIKQAKAKVESKKAEATRLEKiktdRKKAEEEAKRKA-----AEEDKV 412
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
841-1098 |
3.45e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVK 920
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 921 EMNERLedeEEMNAELTAKKRKLeDECSELKRDIDDLELTLAKVEKEKhatENKVKNLTEEMAGLDEiIAKLTKEKKALQ 1000
Cdd:COG1340 82 ELNEKL---NELREELDELRKEL-AELNKAGGSIDKLRKEIERLEWRQ---QTEVLSPEEEKELVEK-IKELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1001 EAHQQ------ALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQ 1074
Cdd:COG1340 154 KALEKneklkeLRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEII 233
|
250 260
....*....|....*....|....
gi 119586555 1075 QLDERLKKKDFELNALNARIEDEQ 1098
Cdd:COG1340 234 ELQKELRELRKELKKLRKKQRALK 257
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1276-1796 |
3.47e-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: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1276 SQRAKLQTENGELSRQLDEKEALI--SQLTRGKLTYTQQLEDLKRQLEEEvkAKNALAHALQSARHDCDLLREQyeeETE 1353
Cdd:COG3096 215 SLRDYLLPENSGVRKAFQDMEAALreNRMTLEAIRVTQSDRDLFKHLITE--ATNYVAADYMRHANERRELSER---ALE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1354 AKAELQRVLSKANSEvaQWRTKYETDAIqrtEELEEAKKKLAQRLQEAEEAVEAVnakcssleKTKHRLQNEIEDLMVDV 1433
Cdd:COG3096 290 LRRELFGARRQLAEE--QYRLVEMAREL---EELSARESDLEQDYQAASDHLNLV--------QTALRQQEKIERYQEDL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1434 ErsnAAAAALDKKQrnfdKILAEWKQKYEESQSELESSQKEARSLSTELFKlknaYEESLEHLETfkrenKNLQEEisdl 1513
Cdd:COG3096 357 E---ELTERLEEQE----EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD----YQQALDVQQT-----RAIQYQ---- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1514 teqlgssgKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEgkilraqlEFNQIKAEIERKLAEKDEemeqAKRNHLR 1593
Cdd:COG3096 417 --------QAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQ--------QATEEVLELEQKLSVADA----ARRQFEK 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1594 VVDSLQTSLDAETRSR-----NEALRV---KKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAvran 1665
Cdd:COG3096 477 AYELVCKIAGEVERSQawqtaRELLRRyrsQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA---- 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1666 DDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHsqntslinqkkKMDADLSQLQTEVEEA 1745
Cdd:COG3096 553 EELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL-----------AAQDALERLREQSGEA 621
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 119586555 1746 VQECRnaeekakkAITDAamMAEELKKEQDTSA---HLERMKKNMEQTIKDLQH 1796
Cdd:COG3096 622 LADSQ--------EVTAA--MQQLLEREREATVerdELAARKQALESQIERLSQ 665
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
843-1097 |
3.49e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 843 AEREKEMASMKE---EFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIknkiqlEAKV 919
Cdd:COG4913 671 AELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE------DLAR 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 920 KEMNERLED--EEEMNAELTAKKRK-LEDECSELKRDIDDLELTLAKVEKE-KHATENKVKNLTEEMAGLDEIIAKLT-- 993
Cdd:COG4913 745 LELRALLEErfAAALGDAVERELREnLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLDrl 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 994 ----------KEKKALQEAHQQALDDLQAEedkvntLTKAKVKLEQQVDDLEGSLEQ-----EKKVRMDLERAKRKlegD 1058
Cdd:COG4913 825 eedglpeyeeRFKELLNENSIEFVADLLSK------LRRAIREIKERIDPLNDSLKRipfgpGRYLRLEARPRPDP---E 895
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 119586555 1059 LKLTQESIMDLENDKQQLDERLKKKDFE-LNALNARIEDE 1097
Cdd:COG4913 896 VREFRQELRAVTSGASLFDEELSEARFAaLKRLIERLRSE 935
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
1646-1755 |
3.53e-03 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 40.72 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1646 SLQSLLKDT-QIQLDDAVRANDDLKENIAIVE-----------RRNNLL---------QAELEELRAVVEQTERSRKLAE 1704
Cdd:pfam05266 50 SFAGLLEKVkKLQVDDSRSVFESLMESFAELEkhgfdvkapqsRINKLLslkdrqtklLEELKKLEKKIAEEESEKRKLE 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 119586555 1705 QELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEK 1755
Cdd:pfam05266 130 EEIDELEKKILELERQLALAKEKKEAADKEIARLKSEAEKLEQEIQDVELE 180
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
840-1811 |
3.67e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 840 LKSAE--REKEMASMKEEFTRL-KEALEKSEARRKELEEKMVSLLQEKNDLQLQVqAEQDNLADAEERCDQLIK------ 910
Cdd:NF041483 296 LASAEsaNEQRTRTAKEEIARLvGEATKEAEALKAEAEQALADARAEAEKLVAEA-AEKARTVAAEDTAAQLAKaartae 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 911 ---NKIQLEAK-----VKEMNERLEDEEEMNAE-LTAKKRKLEDECS-ELKRDIDDLELTLAKVEKEKHATENKVKNLTE 980
Cdd:NF041483 375 evlTKASEDAKattraAAEEAERIRREAEAEADrLRGEAADQAEQLKgAAKDDTKEYRAKTVELQEEARRLRGEAEQLRA 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 981 EMAGLDEIIakltkEKKALQEAHQQALDDLQAEEDkvnTLTKAKVkleqQVDDLEGSLEQE-KKVRMD-LERA---KRKL 1055
Cdd:NF041483 455 EAVAEGERI-----RGEARREAVQQIEEAARTAEE---LLTKAKA----DADELRSTATAEsERVRTEaIERAttlRRQA 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1056 EGDLKLTQESIMDLENDKQQLDERLKKkDFELNALNARIEDEQALGSQLQKKLKELqARIEELEEE-----LEAERTARA 1130
Cdd:NF041483 523 EETLERTRAEAERLRAEAEEQAEEVRA-AAERAARELREETERAIAARQAEAAEEL-TRLHTEAEErltaaEEALADARA 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1131 KVEKLRSDLSRELEEIseRLEEAGGATSVQiemnKKREAEFQKMRR----DLEEATLQHEATAAALRKKHADSVAEL-GE 1205
Cdd:NF041483 601 EAERIRREAAEETERL--RTEAAERIRTLQ----AQAEQEAERLRTeaaaDASAARAEGENVAVRLRSEAAAEAERLkSE 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1206 QIDNLQRVKqklekekSEFKLELDDVTSNMEQIIKAKAANLEKMCRTLEDQMNEHRSKAEETQRSVND-----LTSQRAK 1280
Cdd:NF041483 675 AQESADRVR-------AEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREqseelLASARKR 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1281 LQTENGELSRQLDEKEALISQLTRGKLTYTQQLED----LKRQLEEEVKA-KNALAHALQSARhdcdllreqyeeeTEAK 1355
Cdd:NF041483 748 VEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDsvagLQEQAEEEIAGlRSAAEHAAERTR-------------TEAQ 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1356 AELQRVLSKANSEvaqwRTKYETDAI---QRTEELEEAKKKLAQR-LQEAEEAVEAVNAKCSSLEKtkhRLQNEIEDLMV 1431
Cdd:NF041483 815 EEADRVRSDAYAE----RERASEDANrlrREAQEETEAAKALAERtVSEAIAEAERLRSDASEYAQ---RVRTEASDTLA 887
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1432 DVERSNAAAAALDKKQRNfdKILAEwkqkyeeSQSELESSQKEARSLSTELFKLKNAYEESLehLETFKRENKNLQEEIS 1511
Cdd:NF041483 888 SAEQDAARTRADAREDAN--RIRSD-------AAAQADRLIGEATSEAERLTAEARAEAERL--RDEARAEAERVRADAA 956
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1512 DLTEQLGSsgKTIHELEKVRK---------QLEAEKMELQSALEEAEASLEHEEgkiLRAQlefnqIKAEIERKLAEKDE 1582
Cdd:NF041483 957 AQAEQLIA--EATGEAERLRAeaaetvgsaQQHAERIRTEAERVKAEAAAEAER---LRTE-----AREEADRTLDEARK 1026
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1583 EMEQAKRNHLRVVDSLQTSLDAE-----TRSRNEALRVKKKMEGDLNEM-EIQLSHANRMAAEAQKQVKSLQSLLKDTQI 1656
Cdd:NF041483 1027 DANKRRSEAAEQADTLITEAAAEadqltAKAQEEALRTTTEAEAQADTMvGAARKEAERIVAEATVEGNSLVEKARTDAD 1106
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1657 QLDDAVRanddlKENIAIVERRNNL---LQAELEEL--RAVVEQTERSR----------KLAEQELIETSERVQLLHSQN 1721
Cdd:NF041483 1107 ELLVGAR-----RDATAIRERAEELrdrITGEIEELheRARRESAEQMKsagercdalvKAAEEQLAEAEAKAKELVSDA 1181
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1722 TS-----LINQKKKMDADLSQLQTEVEEAVQEcrnAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQH 1796
Cdd:NF041483 1182 NSeaskvRIAAVKKAEGLLKEAEQKKAELVRE---AEKIKAEAEAEAKRTVEEGKRELDV---LVRRREDINAEISRVQD 1255
|
1050
....*....|....*
gi 119586555 1797 RLDEAEQIALKGGKK 1811
Cdd:NF041483 1256 VLEALESFEAPSGGG 1270
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1772-1924 |
4.02e-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: 42.04 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1772 KEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGK------KQLQKLEARVRELENELEAEQKRNAESVKGMRKSE 1845
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRqldresDRNQELQKRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119586555 1846 RRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1924
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQ 161
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1789-1928 |
4.03e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1789 QTIKDLQHRLDEAEQIA--LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQ 1866
Cdd:COG1579 7 RALLDLQELDSELDRLEhrLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119586555 1867 DL--VDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1928
Cdd:COG1579 87 NNkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1255-1448 |
4.14e-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: 42.51 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1255 DQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEkealISQlTRGKLTYTQQledlkrqleeevkakNALAHAL 1334
Cdd:NF012221 1545 DAVSKHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAA----ISG-SQSQLESTDQ---------------NALETNG 1604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1335 QSARhdcDLLREQYEEETEAKAELQRVLSKANSEVA-------QWRTKYET---DAIQR---------TEELEEAKKKLA 1395
Cdd:NF012221 1605 QAQR---DAILEESRAVTKELTTLAQGLDALDSQATyagesgdQWRNPFAGgllDRVQEqlddakkisGKQLADAKQRHV 1681
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 119586555 1396 QRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNaaAAALDKKQR 1448
Cdd:NF012221 1682 DNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRK--DDALAKQNE 1732
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
950-1111 |
4.35e-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: 40.66 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 950 LKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKAlQEAHQQALDDLQAeedKVNTLTKAKVKLEQ 1029
Cdd:pfam13851 31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN-YEKDKQSLKNLKA---RLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1030 QVDDLEgslEQEKKVRMDLERAKRKLEGDLKLTQESI----MDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQ 1105
Cdd:pfam13851 107 EHEVLE---QRFEKVERERDELYDKFEAAIQDVQQKTglknLLLEKKLQALGETLEKKEAQLNEVLAAANLDPDALQAVT 183
|
....*.
gi 119586555 1106 KKLKEL 1111
Cdd:pfam13851 184 EKLEDV 189
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
843-1151 |
4.42e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 843 AEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM 922
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 923 NERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKE------K 996
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaeqalD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 997 KALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQL 1076
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119586555 1077 DERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLE 1151
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1792-1932 |
4.43e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1792 KDLQHRLDEAEQIALKggkKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDK 1871
Cdd:COG1196 216 RELKEELKELEAELLL---LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119586555 1872 LQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKR 1932
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1526-1797 |
4.45e-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: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1526 ELEKVRkqLEAEKMELQSALEEaEASLEHEEGKIL-RAQLEFNQ----IKAEIERKLAEKDEEMEQAKRNHLRVVDSLQT 1600
Cdd:pfam17380 349 ELERIR--QEERKRELERIRQE-EIAMEISRMRELeRLQMERQQknerVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1601 SLDAETRSRNEALRVKKKMEgdlNEMEiqlshanRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNN 1680
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERA---REME-------RVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1681 LLQAELEELRAVVEQTERSRKLAEQELIEtservqllhSQNTSLINQKKKMDADLSQLQTEVEEavqecrnaeekaKKAI 1760
Cdd:pfam17380 496 ILEKELEERKQAMIEEERKRKLLEKEMEE---------RQKAIYEEERRREAEEERRKQQEMEE------------RRRI 554
|
250 260 270
....*....|....*....|....*....|....*..
gi 119586555 1761 TDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHR 1797
Cdd:pfam17380 555 QEQMRKATEERSRLEA---MEREREMMRQIVESEKAR 588
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1484-1663 |
4.58e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1484 KLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQ----------------SALEE 1547
Cdd:PHA02562 217 RKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkvikmyekggvcptctQQISE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1548 AEASLEHEEGKILRAQLEFNQIKAEIErKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEgdlnemE 1627
Cdd:PHA02562 297 GPDRITKIKDKLKELQHSLEKLDTAID-ELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIE------E 369
|
170 180 190
....*....|....*....|....*....|....*.
gi 119586555 1628 IQLSHANRmaaeaQKQVKSLQSLLKDTQIQLDDAVR 1663
Cdd:PHA02562 370 LQAEFVDN-----AEELAKLQDELDKIVKTKSELVK 400
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1433-1706 |
4.69e-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: 41.87 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1433 VERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARslstelFKLKNAYEESLEHLETfkrENKNLQEEISD 1512
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAA------AEAEQELEESKRETET---GIQNLTAEIEQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1513 LTEQLGSSGKTIHElekvrkqlEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHL 1592
Cdd:COG5185 348 GQESLTENLEAIKE--------EIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1593 RVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEiQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENI 1672
Cdd:COG5185 420 RQIEELQRQIEQATSSNEEVSKLLNELISELNKVM-READEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLK 498
|
250 260 270
....*....|....*....|....*....|....
gi 119586555 1673 AIVERRNNLLQAELEELRAVVEQTERSRKLAEQE 1706
Cdd:COG5185 499 ATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
841-1105 |
4.96e-03 |
|
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: 42.13 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKND--LQLQVQAEQDNLADAEERCDQLIKNKIQLEAK 918
Cdd:pfam12128 662 KQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEqkREARTEKQAYWQVVEGALDAQLALLKAAIAAR 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 919 VKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHA-------------------------TEN 973
Cdd:pfam12128 742 RSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEvlryfdwyqetwlqrrprlatqlsnIER 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 974 KVKNLTEEMAGLDE----IIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLtkAKVKLEQQVDDLEGSLEQEKKVRMDLE 1049
Cdd:pfam12128 822 AISELQQQLARLIAdtklRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL--ATLKEDANSEQAQGSIGERLAQLEDLK 899
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119586555 1050 RAKRKLEGDLKLTQESIMDLENDKQQLD-----ERLKKKDFELNALNARIEDEQALGSQLQ 1105
Cdd:pfam12128 900 LKRDYLSESVKKYVEHFKNVIADHSGSGlaetwESLREEDHYQNDKGIRLLDYRKLVPYLE 960
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1397-1590 |
5.05e-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: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1397 RLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKyeesqselessqkeAR 1476
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR--------------IK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1477 SLSTELFKLKNAYE-ESLEH-LETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEh 1554
Cdd:COG1579 77 KYEEQLGNVRNNKEyEALQKeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE- 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 119586555 1555 EEGKILRAQLEfnQIKAEIERKLAEKDEEMEQAKRN 1590
Cdd:COG1579 156 AELEELEAERE--ELAAKIPPELLALYERIRKRKNG 189
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
896-1166 |
5.13e-03 |
|
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.
Pssm-ID: 463118 [Multi-domain] Cd Length: 360 Bit Score: 41.48 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 896 DNLADAEercdqLIKNKIQLEAKVKEMNERLEDEEEMnaeltakkrkledecselkrDIDDLELTLAKVEKEKHATENKV 975
Cdd:pfam10498 107 DDLADEA-----LKRKNFKWKKPKYPPEEEFEEEDVV--------------------EEDDAELTLEKVEEEMLIEGDDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 976 KNLTEEmaglDEIIAKLTKEKKALQEAHQQALD------DLQAEEDKVntLTKAKVKLEQQVDDLEGSLEQ----EKKVR 1045
Cdd:pfam10498 162 KEDDED----EDLYNESTKGEEAESSKPREIIEsnvdaaEWKLELERV--LPQLKVTIKADAKDWRAHLEQmkqhKKSIE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1046 MDLERAK---RKLEGDLKLTQESIMDLE---NdkQQLDERLKkkdfELNALNARIedeqalgSQLQKKLKELQARIeele 1119
Cdd:pfam10498 236 ESLPDTKsqlDKLHTDISKTLEKIESREkyiN--SQLEPLIQ----EYREAQDEL-------SEVQEKYKQLSEGV---- 298
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 119586555 1120 eeleaertarakveklrSDLSRELEEISERLEeaggatSVQIEMNKK 1166
Cdd:pfam10498 299 -----------------TERTRELAEITEELE------KVKQEMEER 322
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1759-1932 |
5.56e-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: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1759 AITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKRNAESV 1838
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1839 KGMRKSERRIKELT-----YQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADI 1913
Cdd:COG3883 93 RALYRSGGSVSYLDvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170
....*....|....*....
gi 119586555 1914 AESQVNKLRAKSRDIGTKR 1932
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEE 191
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
846-989 |
5.62e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 846 EKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQleaKVKEMNER 925
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVK---KLEELEEE 233
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119586555 926 LEDEEEMNAELTAKKRKLEDECSELKR-----------DIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEII 989
Cdd:smart00787 234 LQELESKIEDLTNKKSELNTEIAEAEKkleqcrgftfkEIEKLKEQLKLLQSLTGWKITKLSGNTLSMTYDREIN 308
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
924-1152 |
5.80e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 924 ERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL----DEIIAKLTKEKKAL 999
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELrekrDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1000 QEAHQQA------LDDLQAEEDKVNTLTKAKVKLEQQVDDLEG-------SLEQEKKVRMDLERAKRKLEgdlklTQESI 1066
Cdd:COG1340 81 DELNEKLnelreeLDELRKELAELNKAGGSIDKLRKEIERLEWrqqtevlSPEEEKELVEKIKELEKELE-----KAKKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1067 MDLENDKQQLDERLKKKDFELNALNARIedeQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEI 1146
Cdd:COG1340 156 LEKNEKLKELRAELKELRKEAEEIHKKI---KELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEI 232
|
....*.
gi 119586555 1147 SERLEE 1152
Cdd:COG1340 233 IELQKE 238
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
864-1001 |
6.10e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.82 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 864 EKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDqliKNKIQLEAKVKEMNERLEDEEEMN-----AELTA 938
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTE---KDQTALETLEKALKDLLTDEGGAIarkeiKDLQK 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119586555 939 KKRKLEDEC-SELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQE 1001
Cdd:cd22656 187 ELEKLNEEYaAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEK 250
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1369-1508 |
6.42e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1369 VAQWRTKYETDA------IQRTEELEeakKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERsnAAAAA 1442
Cdd:PRK00409 504 IEEAKKLIGEDKeklnelIASLEELE---RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK--EAQQA 578
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119586555 1443 LDKKQRNFDKILAEWKQKYEESQSELES-SQKEARSlstelfKLKNAYEESLEHLETFKRENKNLQE 1508
Cdd:PRK00409 579 IKEAKKEADEIIKELRQLQKGGYASVKAhELIEARK------RLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
839-1152 |
6.59e-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: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 839 LLKSAEREKEMASMKEEFTRLKEALEKSE----ARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDqlIKNKIQ 914
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDKLEKLVEQNTdlrlEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSID--IKKATE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 915 LEAKVKEmnerledEEEMNAELTAKKRKLEdecSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAgLDEIIAKLTK 994
Cdd:COG5185 313 SLEEQLA-------AAEAEQELEESKRETE---TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE-LSKSSEELDS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 995 EKKALQEAHQqalddlQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLE-NDK 1073
Cdd:COG5185 382 FKDTIESTKE------SLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNkVMR 455
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119586555 1074 QQLDERLKKKDFELNALNARIEDEQAlgsQLQKKLKELQARIeeleeeleaeRTARAKVEKLRSDLSRELEEISERLEE 1152
Cdd:COG5185 456 EADEESQSRLEEAYDEINRSVRSKKE---DLNEELTQIESRV----------STLKATLEKLRAKLERQLEGVRSKLDQ 521
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1100-1430 |
6.69e-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: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1100 LGSQLQKKLKEL-------QARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQ 1172
Cdd:pfam07888 32 LQNRLEECLQERaellqaqEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1173 KMRRDLEEATLQHEATAAALRKKHADSVAELGEQID---NLQRVKQKLEKEKSEFKLELDDVTSnmeqiIKAKAANLEKM 1249
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLEretELERMKERAKKAGAQRKEEEAERKQ-----LQAKLQQTEEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1250 CRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQL--TRGKLTYTQQ-LEDLKRQLEEEVKA 1326
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELrsLQERLNASERkVEGLGEELSSMAAQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1327 KNALAHALQSARHDCDLLREQYEE------ETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTE-------------EL 1387
Cdd:pfam07888 267 RDRTQAELHQARLQAAQLTLQLADaslalrEGRARWAQERETLQQSAEADKDRIEKLSAELQRLEerlqeermereklEV 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 119586555 1388 EEAKKKLAQRLQEAEEAVEAVNAKCS--SLEKTKHRLQNEIEDLM 1430
Cdd:pfam07888 347 ELGREKDCNRVQLSESRRELQELKASlrVAQKEKEQLQAEKQELL 391
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
844-1152 |
6.75e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 844 EREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMN 923
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 924 ERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLE-----LTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 998
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEqelqaLSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 999 LQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDE 1078
Cdd:COG4372 216 LAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALEL 295
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119586555 1079 RLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEE 1152
Cdd:COG4372 296 KLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
835-1112 |
6.76e-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: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 835 KIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNdlQLQVQAEQDNLADAEERCDQLIKNKIQ 914
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEE--QLAAAEAEQELEESKRETETGIQNLTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 915 --------LEAKVKEMNERLE--DEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENK-VKNLTEEMA 983
Cdd:COG5185 344 eieqgqesLTENLEAIKEEIEniVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDtLKAADRQIE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 984 GLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRmDLERAKRKLEGDLKLTQ 1063
Cdd:COG5185 424 ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNE-ELTQIESRVSTLKATLE 502
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 119586555 1064 ESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQ 1112
Cdd:COG5185 503 KLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELI 551
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
835-1083 |
6.78e-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: 40.95 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 835 KIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAeERCDQLIKNKIQ 914
Cdd:pfam15905 68 NLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLEL-TRVNELLKAKFS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 915 LEAKVKEMN----ERLEDEEEMNA---ELTAKKRKLEDECSELKRD-------IDDLELTLAKVEKEKHATENKVKNLTE 980
Cdd:pfam15905 147 EDGTQKKMSslsmELMKLRNKLEAkmkEVMAKQEGMEGKLQVTQKNlehskgkVAQLEEKLVSTEKEKIEEKSETEKLLE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 981 EMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLK 1060
Cdd:pfam15905 227 YITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLN 306
|
250 260
....*....|....*....|...
gi 119586555 1061 LTQESIMDLENDKQQLDERLKKK 1083
Cdd:pfam15905 307 AELEELKEKLTLEEQEHQKLQQK 329
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1104-1797 |
7.43e-03 |
|
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: 41.35 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1104 LQKKLKELQarieelEEELEAERTARAKVEKLRSDL-------SRELEEISERLEEAGGATSVQIEMNKKREAEFQKM-- 1174
Cdd:pfam10174 1 LQAQLRDLQ------RENELLRRELDIKESKLGSSMnsiktfwSPELKKERALRKEEAARISVLKEQYRVTQEENQHLql 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1175 -----------RRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNME---QIIK 1240
Cdd:pfam10174 75 tiqalqdelraQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIEtqkQTLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1241 AKAANLEKMCRTLedQMNEHRSKAEEtqrSVNDLTSQRAKLQTENGELSRQLDEKEALISQLtRGKLTYTQQLED---LK 1317
Cdd:pfam10174 155 ARDESIKKLLEML--QSKGLPKKSGE---EDWERTRRIAEAEMQLGHLEVLLDQKEKENIHL-REELHRRNQLQPdpaKT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1318 RQLEEEVKAKNA-----------LAHALQSARHDCDLLREQYEEETEAKA--------------ELQRVLSKANSEVAQW 1372
Cdd:pfam10174 229 KALQTVIEMKDTkisslernirdLEDEVQMLKTNGLLHTEDREEEIKQMEvykshskfmknkidQLKQELSKKESELLAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1373 RTKYETDAIQRTEEleeakkklaqrLQEAEEAVEAVNAKcsslEKTKHRLQNEIEDLMVDversnaaaaaLDKKQRNFDK 1452
Cdd:pfam10174 309 QTKLETLTNQNSDC-----------KQHIEVLKESLTAK----EQRAAILQTEVDALRLR----------LEEKESFLNK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1453 ilaewKQKYeesqseLESSQKEARSLSTELFKLKNAyeeslehLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRK 1532
Cdd:pfam10174 364 -----KTKQ------LQDLTEEKSTLAGEIRDLKDM-------LDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVK 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1533 QLEAEKMELQSALEEAEASLEHEEGKILRaqlefnqIKAEIERKLAEKDEEMEQAKR---NHLRVVDSLQTSLDAETRSR 1609
Cdd:pfam10174 426 SLQTDSSNTDTALTTLEEALSEKERIIER-------LKEQREREDRERLEELESLKKenkDLKEKVSALQPELTEKESSL 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1610 NEalrVKKKMEGDLNEMEIQLSHANRMAAEAQKQVK---SLQSLLKDTQiQLDDAVRANDDLKENIAIVERR-------N 1679
Cdd:pfam10174 499 ID---LKEHASSLASSGLKKDSKLKSLEIAVEQKKEecsKLENQLKKAH-NAEEAVRTNPEINDRIRLLEQEvarykeeS 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1680 NLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLH-SQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKK 1758
Cdd:pfam10174 575 GKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMkEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQ 654
|
730 740 750
....*....|....*....|....*....|....*....
gi 119586555 1759 AITDAAMMAEELKKEQdtsahLERMKKNMEQTIKDLQHR 1797
Cdd:pfam10174 655 LQLEELMGALEKTRQE-----LDATKARLSSTQQSLAEK 688
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1353-1857 |
7.71e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1353 EAKAELQRVLSKANSEVAQWRTKYETDAIQRTeelEEAKKKLAQRLQEAEEAVEAVNAKCsslEKTKHRLQNEIEDLMVD 1432
Cdd:NF041483 276 EARAEAEKVVAEAKEAAAKQLASAESANEQRT---RTAKEEIARLVGEATKEAEALKAEA---EQALADARAEAEKLVAE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1433 VE---RSNAA---AAALDKKQRNFDKILAEwkqkyeesqselesSQKEARSLStelfklKNAYEESLEHLETFKRENKNL 1506
Cdd:NF041483 350 AAekaRTVAAedtAAQLAKAARTAEEVLTK--------------ASEDAKATT------RAAAEEAERIRREAEAEADRL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1507 QEEISDLTEQLGSSGKtiheleKVRKQLEAEKMELQSaleeaEASLEHEEGKILRAQL--EFNQIKAEIERKLAEKDEEM 1584
Cdd:NF041483 410 RGEAADQAEQLKGAAK------DDTKEYRAKTVELQE-----EARRLRGEAEQLRAEAvaEGERIRGEARREAVQQIEEA 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1585 EQAKRNHLRV----VDSLQTSLDAET-RSRNEALRVKKKMEGDLNE-MEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQL 1658
Cdd:NF041483 479 ARTAEELLTKakadADELRSTATAESeRVRTEAIERATTLRRQAEEtLERTRAEAERLRAEAEEQAEEVRAAAERAAREL 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1659 -DDAVRANDDLKENIAIVERRnnlLQAELEELRAVVEQT--------ERSRKLAEQEL----IETSERVQLLHSQntsli 1725
Cdd:NF041483 559 rEETERAIAARQAEAAEELTR---LHTEAEERLTAAEEAladaraeaERIRREAAEETerlrTEAAERIRTLQAQ----- 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1726 nqkkkMDADLSQLQTE-VEEAVQECRNAEEKAKKAITDAAMMAEELKKE-QDTS--------AHLERMKKNMEQTIKDLQ 1795
Cdd:NF041483 631 -----AEQEAERLRTEaAADASAARAEGENVAVRLRSEAAAEAERLKSEaQESAdrvraeaaAAAERVGTEAAEALAAAQ 705
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119586555 1796 H----RLDEAEQIaLKGGKKQLQKLEARVRELENELEAEQKR-----NAESVKGMRKSERRIKELTYQTEE 1857
Cdd:NF041483 706 EeaarRRREAEET-LGSARAEADQERERAREQSEELLASARKrveeaQAEAQRLVEEADRRATELVSAAEQ 775
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
949-1863 |
7.73e-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: 41.48 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 949 ELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAgldeiiaKLTKEKKALQEAHQQALDDLQaeedKVNTLTKAKVKLE 1028
Cdd:COG3096 282 ELSERALELRRELFGARRQLAEEQYRLVEMARELE-------ELSARESDLEQDYQAASDHLN----LVQTALRQQEKIE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1029 QQVDDLEG---SLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLEN---DKQQ-LDERLKKKDFELNALNARIEDEQALG 1101
Cdd:COG3096 351 RYQEDLEElteRLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSqlaDYQQaLDVQQTRAIQYQQAVQALEKARALCG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1102 ------SQLQKKLKELQARieeLEEELEAERTARAKVEkLRSDLSRELEEISERLEEAGGATSvqiemnkkREAEFQKMR 1175
Cdd:COG3096 431 lpdltpENAEDYLAAFRAK---EQQATEEVLELEQKLS-VADAARRQFEKAYELVCKIAGEVE--------RSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1176 RDLEEA-TLQHEA-TAAALRKKHAdsvaELGEQIDNLQRVKQKLEKEKSEFKLELDDVTsnmeqiikakaanlekmcrTL 1253
Cdd:COG3096 499 ELLRRYrSQQALAqRLQQLRAQLA----ELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-------------------EL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1254 EDQMNEHRSKAEETQRSVNDLTSQRAklqtengELSRQLDEKEALISQLTRGK---LTYTQQLEDLKRQLEEEVKAKNAL 1330
Cdd:COG3096 556 EELLAELEAQLEELEEQAAEAVEQRS-------ELRQQLEQLRARIKELAARApawLAAQDALERLREQSGEALADSQEV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1331 AHALQsarhdcdllrEQYEEETEAKAELQRVLskansevaqwrtkyetdaiQRTEELEEAKKKLAQ-------RLQEAEE 1403
Cdd:COG3096 629 TAAMQ----------QLLEREREATVERDELA-------------------ARKQALESQIERLSQpggaedpRLLALAE 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1404 AVEAVnakcsslektkhrLQNEI-EDLMVD-----------------VERSNAAAAALDKK----------QRN---FDK 1452
Cdd:COG3096 680 RLGGV-------------LLSEIyDDVTLEdapyfsalygparhaivVPDLSAVKEQLAGLedcpedlyliEGDpdsFDD 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1453 ILAEWKQkyEESQSELESSQKEAR-SLSTELFKLKNAYEEslEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEK-V 1530
Cdd:COG3096 747 SVFDAEE--LEDAVVVKLSDRQWRySRFPEVPLFGRAARE--KRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfV 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1531 RKQL--------EAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIE--RKLAE-----KDEEMEQakrnhlRVV 1595
Cdd:COG3096 823 GGHLavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllNKLLPqanllADETLAD------RLE 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1596 DslqtsLDAETRSRNEALRVKKKMEGDLNEMEIQLShANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLkeniaiV 1675
Cdd:COG3096 897 E-----LREELDAAQEAQAFIQQHGKALAQLEPLVA-VLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEV------V 964
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1676 ERRNNLLQAE----LEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLiNQKkkmdadLSQLQTEVEEAVQECRN 1751
Cdd:COG3096 965 QRRPHFSYEDavglLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQY-NQV------LASLKSSRDAKQQTLQE 1037
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1752 AEEKAK----KAITDAAMMAEELKKEQDTSAHLERMKKNmeQTIKDLQHRldEAEQIALkggKKQLQKLEARVRELENEL 1827
Cdd:COG3096 1038 LEQELEelgvQADAEAEERARIRRDELHEELSQNRSRRS--QLEKQLTRC--EAEMDSL---QKRLRKAERDYKQEREQV 1110
|
970 980 990 1000
....*....|....*....|....*....|....*....|
gi 119586555 1828 EAEQKRNAESVKGMRKS--ERRI--KELTYQTEEDRKNLL 1863
Cdd:COG3096 1111 VQAKAGWCAVLRLARDNdvERRLhrRELAYLSADELRSMS 1150
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1529-1653 |
7.81e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1529 KVRKQLEAEKMELQSALEEAEASLE-HEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETR 1607
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEaIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 119586555 1608 SRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKD 1653
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1525-1794 |
7.83e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1525 HELEKVRKQLEaekmELQSALEEAEASLEheegkILRAQLEfnqikaEIErKLAEKDEEMEQ--AKRNHLRVVDSLQTSL 1602
Cdd:COG0497 165 RAWRALKKELE----ELRADEAERARELD-----LLRFQLE------ELE-AAALQPGEEEEleEERRRLSNAEKLREAL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1603 daetrsrNEALRVkkkmegdLNEMEI----QLSHANRM---AAEAQKQVKSLQSLLKDTQIQLDDAVRanddlkeniaiv 1675
Cdd:COG0497 229 -------QEALEA-------LSGGEGgaldLLGQALRAlerLAEYDPSLAELAERLESALIELEEAAS------------ 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1676 errnnllqaeleELRAVVEQTErsrkLAEQELIETSERVQLLHS-------QNTSLINQKKKMDADLSQLQtEVEEAVQE 1748
Cdd:COG0497 283 ------------ELRRYLDSLE----FDPERLEEVEERLALLRRlarkygvTVEELLAYAEELRAELAELE-NSDERLEE 345
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 119586555 1749 CRNAEEKAKKAITDAammAEEL-KKEQDTSAHLErmkKNMEQTIKDL 1794
Cdd:COG0497 346 LEAELAEAEAELLEA---AEKLsAARKKAAKKLE---KAVTAELADL 386
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
882-1058 |
8.27e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.01 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 882 QEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNA---ELTAKKRKLEDECSELKRDIDDLE 958
Cdd:PRK00106 42 QEAVNLRGKAERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSerqELKQIESRLTERATSLDRKDENLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 959 LTLAKVEKEKHATENKVKNLTEEmaglDEIIAKLTKEKkalqEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSL 1038
Cdd:PRK00106 122 SKEKTLESKEQSLTDKSKHIDER----EEQVEKLEEQK----KAELERVAALSQAEAREIILAETENKLTHEIATRIREA 193
|
170 180
....*....|....*....|....*.
gi 119586555 1039 EQEKKVRMD------LERAKRKLEGD 1058
Cdd:PRK00106 194 EREVKDRSDkmakdlLAQAMQRLAGE 219
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
953-1066 |
8.46e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 953 DIDDLELTLAKVEKEKHATENkvknltEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVD 1032
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100 110
....*....|....*....|....*....|....
gi 119586555 1033 DLEgSLEQEkkvrmdLERAKRKLEGDLKLTQESI 1066
Cdd:COG0542 486 KIP-ELEKE------LAELEEELAELAPLLREEV 512
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1526-1789 |
8.84e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1526 ELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQL------EFNQIKAEIERKLAEKDEEMEQAKRNhlRVVDSL- 1598
Cdd:PRK10929 31 ELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQyqqvidNFPKLSAELRQQLNNERDEPRSVPPN--MSTDALe 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1599 ----QTS--LDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSllkdtqiqlddavranddlkENI 1672
Cdd:PRK10929 109 qeilQVSsqLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGT--------------------PNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1673 AIVERRNNLLQAELEELRAVVEQTERSRKLA--EQELIETseRVQLLHSQNTSLINQKKKMDADL-SQLQTEVEEAVQec 1749
Cdd:PRK10929 169 PLAQAQLTALQAESAALKALVDELELAQLSAnnRQELARL--RSELAKKRSQQLDAYLQALRNQLnSQRQREAERALE-- 244
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 119586555 1750 rNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 1789
Cdd:PRK10929 245 -STELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDL 283
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
879-1041 |
9.06e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.74 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 879 SLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDE-EEMNAELTAKKRKLED---------ECS 948
Cdd:cd00176 37 ALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRwEELRELAEERRQRLEEaldlqqffrDAD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 949 ELKRDIDDLELTLAKVEKEKHATE-----NKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQalDDLQAEEDKVNTLTKA 1023
Cdd:cd00176 117 DLEQWLEEKEAALASEDLGKDLESveellKKHKELEEELEAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNER 194
|
170
....*....|....*...
gi 119586555 1024 KVKLEQQVDDLEGSLEQE 1041
Cdd:cd00176 195 WEELLELAEERQKKLEEA 212
|
|
| F-BAR_PSTPIP2 |
cd07672 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
1248-1425 |
9.16e-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: 39.93 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1248 KMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLE---EEV 1324
Cdd:cd07672 19 KNCKEFEDFLKERASIEEKYGKELLNLSKKKPCGQTEINTLKRSLDVFKQQIDNVGQSHIQLAQTLRDEAKKMEdfrERQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1325 KAKNALAHALQSARHDCDLLreQYEEETEAKAEL-QRVLSKANSEVAQWRTKYETDAIQRteelEEAKKKLAQRLQEAEE 1403
Cdd:cd07672 99 KLARKKIELIMDAIHKQRAM--QFKKTMESKKNYeQKCRDKDEAEQAVNRNANLVNVKQQ----EKLFAKLAQSKQNAED 172
|
170 180
....*....|....*....|..
gi 119586555 1404 AVEAVNAKCSSLEKTKHRLQNE 1425
Cdd:cd07672 173 ADRLYMQNISVLDKIREDWQKE 194
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
985-1163 |
9.56e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 985 LDEIIAKLTKEKkALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSlEQEKKVRMdLERAKRKLEGDLKLTQE 1064
Cdd:COG2433 365 RDEVKARVIRGL-SIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIR-RLEEQVER-LEAEVEELEAELEEKDE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119586555 1065 SIMDLEN---DKQQLDERLKKKDFELNALNARIEdeqalgsQLQKKLKELQARIEELEEELEAERTARAK---------- 1131
Cdd:COG2433 442 RIERLERelsEARSEERREIRKDREISRLDREIE-------RLERELEEERERIEELKRKLERLKELWKLehsgelvpvk 514
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 119586555 1132 -VEKLRSDLSRELEE---ISER----LEEAGGATSVQIEM 1163
Cdd:COG2433 515 vVEKFTKEAIRRLEEeygLKEGdvvyLRDASGAGRSTAEL 554
|
|
| |
