|
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: 1387.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 419 QVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 499 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFS 578
Cdd:cd14917 401 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 579 LIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL 658
Cdd:cd14917 481 LIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 659 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 738
Cdd:cd14917 561 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 1034587182 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: 1352.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAVIAAIGDrSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSK-KKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 419 QVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 499 EEYKKEGIEWTFIDFGMDLQACIDLIEKP-MGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRniKGKPEAHF 577
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 578 SLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADApieKGKGKAKKGSSFQTVSALHRENLNK 657
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGG---GGGKKKKKGGSFRTVSQLHKEQLNK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 658 LMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFiD 737
Cdd:cd01377 555 LMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD-D 633
|
650 660
....*....|....*....|....*....
gi 1034587182 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: 1310.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14913 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 419 QVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 499 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFS 578
Cdd:cd14913 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 579 LIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL 658
Cdd:cd14913 481 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 659 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 738
Cdd:cd14913 561 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 1034587182 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: 1244.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQS-PGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPnANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFD 337
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 338 VLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 417
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 418 QQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 497
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 498 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHF 577
Cdd:cd14916 401 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 578 SLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIE-KGKGKAKKGSSFQTVSALHRENLN 656
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSgKGKGGKKKGSSFQTVSALHRENLN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 657 KLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 736
Cdd:cd14916 561 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 640
|
650 660 670
....*....|....*....|....*....|
gi 1034587182 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: 1228.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVIQYFAVIAAIGDR-SKKDQSPGK---GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 255
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDGpGKKAQFLATktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 256 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNA 335
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 336 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 415
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 416 NVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 496 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPR-NIKGKPE 574
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRpDKKRKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 575 AHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADA---PIEKGKGKAKKGSSFQTVSALH 651
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDStedPKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 652 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 731
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 1034587182 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: 1154.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAVIAAIGDRsKKDQSPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDK-KKEQQPGKmqGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd14923 240 DILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 417 VQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 497 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAH 576
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 577 FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIE--KGKGKAKKGSSFQTVSALHREN 654
Cdd:cd14923 480 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSggSKKGGKKKGSSFQTVSAVFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 655 LNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQ 734
Cdd:cd14923 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 1034587182 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: 1151.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14918 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14918 241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 419 QVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 499 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFS 578
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 579 LIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL 658
Cdd:cd14918 481 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 659 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 738
Cdd:cd14918 561 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 1034587182 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 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 417 VQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 497 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAH 576
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 577 FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGAD---APIEKGKGKAKKGSSFQTVSALHRE 653
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEgasAGGGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 654 NLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEG 733
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 1034587182 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: 1127.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 417 VQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 497 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAH 576
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 577 FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPI-EKGKGKAKKGSSFQTVSALHRENL 655
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEgGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 656 NKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 735
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 1034587182 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: 1126.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 417 VQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 497 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAH 576
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 577 FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAP-IEKGKGKAKKGSSFQTVSALHRENL 655
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEgGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 656 NKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 735
Cdd:cd14915 561 NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 1034587182 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: 1081.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 87 IEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 167 TDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKkdqspgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGK 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN------VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 247 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITnNPYDYAFISQ-GETTVASIDD 325
Cdd:pfam00063 155 YIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQsGCYTIDGIDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 326 AEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVK 405
Cdd:pfam00063 234 SEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 406 VGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEK 484
Cdd:pfam00063 314 TGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 485 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSANF 563
Cdd:pfam00063 394 LQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 564 QKPRNIKgkpEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAK---- 639
Cdd:pfam00063 472 QKPRLQG---ETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTpkrt 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 640 KGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 719
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1034587182 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: 1076.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKdqspgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-----LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKpELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14929 156 SSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14929 235 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 419 QVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd14929 315 QVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 499 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFS 578
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHFE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 579 LIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL 658
Cdd:cd14929 475 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQFGEKKRKKGASFQTVASLHKENLNKL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 659 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 738
Cdd:cd14929 555 MTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSS 634
|
650 660
....*....|....*....|....*...
gi 1034587182 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: 1029.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 80 NPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISD 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 160 NAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAigdrskkdQSPGKGTLEDQIIQANPALEAFGNAKTVRND 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG--------SNTEVGSVEDQILESNPILEAFGNAKTLRNN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 240 NSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNnPYDYAFISQGET- 318
Cdd:smart00242 153 NSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGGCl 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 319 TVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQA-EPDGTEEADKSAYLMGLNSADLLK 397
Cdd:smart00242 232 TVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 398 GLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLC 477
Cdd:smart00242 312 ALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 478 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLfDNH 556
Cdd:smart00242 392 INYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKL-NQH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 557 LGKSANFQKPRNikgKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGadapiekgkg 636
Cdd:smart00242 470 HKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVS---------- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 637 KAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 716
Cdd:smart00242 537 NAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFD 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034587182 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: 1016.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAVIAAigDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGA--SKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14909 159 AGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 419 QVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd14909 319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 499 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIK-GKPEAHF 577
Cdd:cd14909 399 EEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAAHF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 578 SLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADA-PIEKGKGKAKKGSSFQTVSALHRENLN 656
Cdd:cd14909 479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGgGEQAKGGRGKKGGGFATVSSAYKEQLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 657 KLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQfi 736
Cdd:cd14909 559 SLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE-- 636
|
650 660 670
....*....|....*....|....*....|
gi 1034587182 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: 1011.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVIQYFAVIAAIGdrskKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTG----KQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVL 339
Cdd:cd14934 158 GADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 340 GFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQ 419
Cdd:cd14934 238 GFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 420 VIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 499
Cdd:cd14934 318 CNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 500 EYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGK-PEAHFS 578
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAHFE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 579 LIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADApiekgKGKAKKGSSFQTVSALHRENLNKL 658
Cdd:cd14934 478 LVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG-----SKKQKRGSSFMTVSNFYREQLNKL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 659 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDS 738
Cdd:cd14934 553 MTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVDN 631
|
650 660
....*....|....*....|....*...
gi 1034587182 739 RKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14934 632 KKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
37-1432 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 855.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 37 VFVPDDKQEFVKAKIVSRE--GGKVTAE--TEYGKTVTVKEDQVMQ--QNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYG 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAfnKGKVTEEgkKEDGESVSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 111 SWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKR 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 191 VIQYFAVIAAIgdrskkdQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEK 270
Cdd:COG5022 172 IMQYLASVTSS-------STVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 271 SRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNnPYDYAFISQGE-TTVASIDDAEELMATDNAFDVLGFTSEEKNSM 349
Cdd:COG5022 245 SRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQN-PKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEEQDQI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 350 YKLTGAIMHFGNMKFKlKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAK 429
Cdd:COG5022 324 FKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 430 AVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWT 509
Cdd:COG5022 403 ALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWS 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 510 FIDFgMDLQACIDLIEK--PMGIMSILEEECMFPKATDMTFKAKLFDN-HLGKSANFQKPRNIKGKpeahFSLIHYAGIV 586
Cdd:COG5022 483 FIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVKHYAGDV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 587 DYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADapiekgkgkakKGSSFQTVSALHRENLNKLMTNLRSTH 666
Cdd:COG5022 558 EYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-----------SKGRFPTLGSRFKESLNSLMSTLNSTQ 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 667 PHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI---DSRKGAE 743
Cdd:COG5022 627 PHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDTKNAVK 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 744 KLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQSRGVLARMEYKKLLERRDSLLVIQWNIRAFMG 823
Cdd:COG5022 707 SILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRL 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 824 VKNWPWMKLYFKIKPLLKSAEREKEMASMKEEFTRLKEALEK----SEARRKELEEKMVSLLQE---------------K 884
Cdd:COG5022 787 VDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKRekklRETEEVEFSLKAEVLIQKfgrslkakkrfsllkK 866
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 885 NDLQLQVQAEQDNL--------ADAEER----------------------CDQLIKNKIQLE--AKVKEMNE--RLEDEE 930
Cdd:COG5022 867 ETIYLQSAQRVELAerqlqelkIDVKSIsslklvnleleseiielkkslsSDLIENLEFKTEliARLKKLLNniDLEEGP 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 931 EMNAELTAKKRKLEDECSELKRDIDDLELTLakveKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQ----- 1005
Cdd:COG5022 947 SIEYVKLPELNKLHEVESKLKETSEEYEDLL----KKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQlkelp 1022
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1006 -ALDDLQAEEDKVNTLTKAKvKLEQQVDDLEGSLEQEKK------VRMDLERAKRKLEGDLKLTQESIMDLEN-----DK 1073
Cdd:COG5022 1023 vEVAELQSASKIISSESTEL-SILKPLQKLKGLLLLENNqlqaryKALKLRRENSLLDDKQLYQLESTENLLKtinvkDL 1101
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1074 QQLDERLKKKDFELNAL------NARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEIS 1147
Cdd:COG5022 1102 EVTNRNLVKPANVLQFIvaqmikLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKR 1181
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1148 ER----LEEAGGATSVQIEMNK-KREAEFQKMRRDLEEatlqheataaalrkkhADSVAELGEQIDNLQRVKQKLEKEKS 1222
Cdd:COG5022 1182 LYqsalYDEKSKLSSSEVNDLKnELIALFSKIFSGWPR----------------GDKLKKLISEGWVPTEYSTSLKGFNN 1245
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1223 EFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQ--RAKLQTENGELSRQLDEKEALISQ 1300
Cdd:COG5022 1246 LNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFNalRTKASSLRWKSATEVNYNSEELDD 1325
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1301 LTRgkltyTQQLEDLKRQLE---EEVKAKNALAHALQSARHDCDLLREQYEEETEA-KAELQRVLSKANSEvAQWRTKYE 1376
Cdd:COG5022 1326 WCR-----EFEISDVDEELEeliQAVKVLQLLKDDLNKLDELLDACYSLNPAEIQNlKSRYDPADKENNLP-KEILKKIE 1399
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587182 1377 TDAIQRTEELE-EAKKKLAQRLQE-AEEAVEAVNAKCSSLEKTKhRLQNEIEDLMVDV 1432
Cdd:COG5022 1400 ALLIKQELQLSlEGKDETEVHLSEiFSEEKSLISLDRNSIYKEE-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 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKR-SEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 178 GESGAGKTVNTKRVIQYFAVIAAigdRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSG---SGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLIT---NNPYDYAFISQGE-TTVASIDDAEELMATD 333
Cdd:cd00124 158 LVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLElllSYYYLNDYLNSSGcDRIDGVDDAEEFQELL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 334 NAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREE--QAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 411
Cdd:cd00124 238 DALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 412 TKGQNVQQVIYATGALAKAVYERMFNWMVTRINATL--ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 489
Cdd:cd00124 318 TKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 490 NHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRn 568
Cdd:cd00124 398 NQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 569 ikgKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSlkllstlfanyagadapiekgkgkakkgssfqtvs 648
Cdd:cd00124 476 ---KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS----------------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 649 aLHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 728
Cdd:cd00124 518 -QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPG 596
|
650 660 670
....*....|....*....|....*....|....*...
gi 1034587182 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: 806.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVIQYFAVIAAigDRSKKDQSPGK---------GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 250
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAA--SKPKGSGAVPHpavnpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 251 HFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGETTVASIDDAEELM 330
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAEFQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 331 ATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTEeADKSAYLMGLNSADLLKGLCHPRVKVGNE 409
Cdd:cd14911 239 ATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNTV-AQKIAHLLGLSVTDMTRAFLTPRIKVGRD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 410 YVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 488
Cdd:cd14911 318 FVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 489 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLgksanfQKPRN 568
Cdd:cd14911 398 FNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 569 IKG--KPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANY----AGADAPIEKGKGKAKKGS 642
Cdd:cd14911 472 MKTdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAeivgMAQQALTDTQFGARTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 643 SFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 722
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1034587182 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 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGE--LERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 417
Cdd:cd14920 238 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 418 QQVIYATGALAKAVYERMFNWMVTRINATLETKQpRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd14920 317 EQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 496 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFdNHLGKSANFQKPRNIKGk 572
Cdd:cd14920 396 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKD- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 573 pEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFAN---YAGAD----APIEKGKGKAKKGSS-F 644
Cdd:cd14920 474 -KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrIVGLDqvtgMTETAFGSAYKTKKGmF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 645 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 724
Cdd:cd14920 553 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1034587182 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 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQSP---GKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVAS-SFKTKKDQSSialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYS-KYRFLSNGNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 415
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 416 NVQQVIYATGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 494
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 495 VLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFdNHLGKSANFQKPRNIKG 571
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPKKLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 572 kpEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANY---AGADA----PIEKGKGKAKKGSSF 644
Cdd:cd14932 478 --DADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdriVGLDKvagmGESLHGAFKTRKGMF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 645 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 724
Cdd:cd14932 556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1034587182 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: 698.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYG-SWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 178 GESGAGKTVNTKRVIQYFAVIAaiGDRSKKDQspgkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVG--GSSSGETQ------VEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNK-KPELLDMLLITNNpyDYAFISQGE-TTVASIDDAEELMATDNA 335
Cdd:cd01380 153 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHLGSAE--DFFYTNQGGsPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 336 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 415
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 416 NVQQVIYATGALAKAVYERMFNWMVTRINATLETKQP--RQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 493
Cdd:cd01380 311 TLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 494 FVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGK-SANFQKPRNIKGK 572
Cdd:cd01380 391 FKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 573 peahFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLlstlfanyagadapiekgkgkakkgssfQTVSALHR 652
Cdd:cd01380 470 ----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK----------------------------KTVGSQFR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 653 ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAipE 732
Cdd:cd01380 518 DSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK--E 595
|
650 660 670
....*....|....*....|....*....|....
gi 1034587182 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: 697.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQSPgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVAS-SHKGKKDTSI-TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVASIDDAEELMATDNAFDVL 339
Cdd:cd14921 160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN-NYTFLSNGFVPIPAAQDDEMFQETLEAMSIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 340 GFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14921 239 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 419 QVIYATGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 497
Cdd:cd14921 318 QADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 498 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRNIKGKPE 574
Cdd:cd14921 398 QEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 575 ahFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANY---AGADAPIEKGKGKAKKGSS-----FQT 646
Cdd:cd14921 477 --FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdriVGLDQMAKMTESSLPSASKtkkgmFRT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 647 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 726
Cdd:cd14921 555 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1034587182 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: 685.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQspgkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVAS-SHKSKKDQ----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItnNPYD-YAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14919 157 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 417
Cdd:cd14919 235 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 418 QQVIYATGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14919 314 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 497 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRNIKGKp 573
Cdd:cd14919 394 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 574 eAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANY---AGAD-----APIEKGKGKAKKGSSFQ 645
Cdd:cd14919 472 -ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriIGLDqvagmSETALPGAFKTRKGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 646 TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 725
Cdd:cd14919 551 TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1034587182 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: 680.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQSP---GKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVAS-SHKTKKDQNSlalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYN-NYRFLSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 417 VQQVIYATGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd15896 320 QEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 496 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRNIKGk 572
Cdd:cd15896 400 LEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPKKLKD- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 573 pEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANY---AGADAPI---EKGKGKAKKGSSFQT 646
Cdd:cd15896 478 -EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVdriVGLDKVSgmsEMPGAFKTRKGMFRT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 647 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 726
Cdd:cd15896 557 VGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 636
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1034587182 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: 673.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE--LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYdYAFISQGETTVASiDDAEELMATDNAFDVL 339
Cdd:cd14930 160 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 340 GFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 419 QVIYATGALAKAVYERMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14930 317 QADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 497 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRNIKGkp 573
Cdd:cd14930 396 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLRD-- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 574 EAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAG----------ADAPiekgKGKAKKGSS 643
Cdd:cd14930 473 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqvsslGDGP----PGGRPRRGM 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 644 FQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 723
Cdd:cd14930 549 FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1034587182 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: 663.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVIQYFAVIAaigdrskKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVS-------GGSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVL 339
Cdd:cd01378 155 GGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 340 GFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDgTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEY---VTKGQN 416
Cdd:cd01378 235 GFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 417 VQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQ-YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHhmFV 495
Cdd:cd01378 314 VEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--LT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 496 L--EQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFP-KATDMTFKAKLfDNHLGKSANFQKPRNIKG 571
Cdd:cd01378 392 LkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 572 KPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADA---PIekgkgkakkgssfqTVS 648
Cdd:cd01378 470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSkkrPP--------------TAG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 649 ALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 728
Cdd:cd01378 536 TKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPK 615
|
650 660 670
....*....|....*....|....*....|....*...
gi 1034587182 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 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRgkKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYfavIAAIGDrskkdqspGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd01383 79 ESGAGKTETAKIAMQY---LAALGG--------GSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNnPYDYAFISQGET-TVASIDDAEELMATDNAFD 337
Cdd:cd01383 148 CGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNClTIDGVDDAKKFHELKEALD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 338 VLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 417
Cdd:cd01383 227 TVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 418 QQVIYATGALAKAVYERMFNWMVTRINATLET-KQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd01383 307 QQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 497 EQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLfDNHLGKSANFqkprniKGKPEA 575
Cdd:cd01383 387 EQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGERGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 576 HFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENL 655
Cdd:cd01383 459 AFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQKQSVATKFKGQL 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 656 NKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 735
Cdd:cd01383 539 FKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQD 618
|
650 660 670
....*....|....*....|....*....|.
gi 1034587182 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: 639.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVIQYFAVIaaigdrskkdqSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd01381 82 SGAGKTESTKLILQYLAAI-----------SGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITnNPYDYAFISQGETTVAS-IDDAEELMATDNAFDV 338
Cdd:cd01381 151 GAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-DASDYYYLTQGNCLTCEgRDDAAEFADIRSAMKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQRE--EQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd01381 230 LMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 417 VQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYF---IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 493
Cdd:cd01381 310 AEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 494 FVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRNikgK 572
Cdd:cd01381 390 FKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKPKS---D 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 573 PEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADApiekgkgkaKKGSSFQTVSALHR 652
Cdd:cd01381 465 LNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGS---------ETRKKSPTLSSQFR 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 653 ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPaAIPE 732
Cdd:cd01381 536 KSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP-GIPP 614
|
650 660 670
....*....|....*....|....*....|....
gi 1034587182 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: 619.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVIQYfavIAAIGDRSKKdqspgkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14883 82 SGAGKTETTKLILQY---LCAVTNNHSW--------VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKK--PELLDmLLITNNPYDYAFISQ-GETTVASIDDAEELMATDNAF 336
Cdd:cd14883 151 GAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKE-KLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRLAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 415
Cdd:cd14883 230 NVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 416 NVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd14883 310 KVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 496 LEQEEYKKEGIEWTFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRNIKGKPE 574
Cdd:cd14883 390 LEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPDRRRWKTE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 575 ahFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLF-----ANYAGADAPIEKGKGKAKKGSSFQTVSA 649
Cdd:cd14883 468 --FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtypdlLALTGLSISLGGDTTSRGTSKGKPTVGD 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 650 LHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAA 729
Cdd:cd14883 546 TFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRA 625
|
650 660 670
....*....|....*....|....*....|....*...
gi 1034587182 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 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 178 GESGAGKTVNTKRVIQYFAviaaigDRSKKDQSPGKgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLA------YMGGRAVTEGR-SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGET-TVASIDDAEELMATDNAF 336
Cdd:cd01384 154 ISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKL-KDPKQFHYLNQSKCfELDGVDDAEEYRATRRAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKlKQREEQAEPDGTEEADKS----AYLMGLNSADLLKGLCHPRVKVGNEYVT 412
Cdd:cd01384 233 DVVGISEEEQDAIFRVVAAILHLGNIEFS-KGEEDDSSVPKDEKSEFHlkaaAELLMCDEKALEDALCKRVIVTPDGIIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 413 KGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 492
Cdd:cd01384 312 KPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 493 MFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNhLGKSANFQKPRnikg 571
Cdd:cd01384 392 VFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPK---- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 572 KPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFAnyagadapiEKGKGKAKKGSSFQTVSALH 651
Cdd:cd01384 466 LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFP---------PLPREGTSSSSKFSSIGSRF 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 652 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIp 731
Cdd:cd01384 537 KQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVL- 615
|
650 660 670
....*....|....*....|....*....|....*
gi 1034587182 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 |
1.75e-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: 1.75e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAVIAAigdrskkdqspGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAG-----------STNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLlitNNPYDYAFISQGET-TVASIDDAEELMATDNAFD 337
Cdd:cd14872 150 CGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW---GSSAAYGYLSLSGCiEVEGVDDVADFEEVVLAME 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 338 VLGFTSEEKNSMYKLTGAIMHFGNMKF------KLKQREEQAEPDGTEEAdksAYLMGLNSADLLKGLCHPRVKVgneyv 411
Cdd:cd14872 227 QLGFDDADINNVMSLIAAILKLGNIEFasgggkSLVSGSTVANRDVLKEV---ATLLGVDAATLEEALTSRLMEI----- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 412 tKGQNV-------QQVIYATGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 483
Cdd:cd14872 299 -KGCDPtripltpAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 484 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSan 562
Cdd:cd14872 378 KLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS-- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 563 FQKPRNIKGKPEaHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFanyagadAPIEkgkgkAKKGS 642
Cdd:cd14872 455 TFVYAEVRTSRT-EFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF-------PPSE-----GDQKT 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 643 SFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 722
Cdd:cd14872 522 SKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRY 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1034587182 723 RILnPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14872 602 RFL-VKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
845-1923 |
3.34e-173 |
|
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: 557.10 E-value: 3.34e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 845 REKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNE 924
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 925 RLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQ 1004
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1005 QALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKD 1084
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1085 FELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMN 1164
Cdd:pfam01576 243 EELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1165 KKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKAN 1244
Cdd:pfam01576 323 SKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1245 LEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVK 1324
Cdd:pfam01576 403 SEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1325 AKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQEAEEAV 1404
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1405 EAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKL 1484
Cdd:pfam01576 562 EEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSL 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1485 KNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLE 1564
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVN 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1565 FNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVK 1644
Cdd:pfam01576 722 MQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLK 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1645 SLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLI 1724
Cdd:pfam01576 802 KLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQ 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1725 NQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIA 1804
Cdd:pfam01576 882 DEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTV 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1805 LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEE 1884
Cdd:pfam01576 962 KSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEE 1041
|
1050 1060 1070
....*....|....*....|....*....|....*....
gi 1034587182 1885 AEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1923
Cdd:pfam01576 1042 AEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-766 |
2.91e-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: 539.75 E-value: 2.91e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 178 GESGAGKTVNTKRVIQYFAVIAaigdrskkdqspgkGTLED----QIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 253
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA--------------GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 254 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDmLLITNNPYDYafisQGETTVASID---DAEELM 330
Cdd:cd14903 147 KNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERL-FLDSANECAY----TGANKTIKIEgmsDRKHFA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 331 ATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE--PDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGN 408
Cdd:cd14903 222 RTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 409 EYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 488
Cdd:cd14903 302 DVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 489 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRN 568
Cdd:cd14903 382 FTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRT 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 569 IKgkpeAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGS-----S 643
Cdd:cd14903 461 SR----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRrggalT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 644 FQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 723
Cdd:cd14903 537 TTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFW 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1034587182 724 ILNPAAipEGQFIDSRKGAEKLLSSLDIDH-NQYKFGHTKVFFK 766
Cdd:cd14903 617 LFLPEG--RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
102-766 |
8.43e-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: 8.43e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 102 LYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 181 GAGKTVNTKRVIQYFAVIAAIGDrskkdqspgkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 260
Cdd:cd01382 84 GAGKTESTKYILRYLTESWGSGA----------GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 261 ADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLitnnpydyafisqgetTVASIDDAEELMATDNAFDVLG 340
Cdd:cd01382 154 GFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 341 FTSEEKNSMYKLTGAIMHFGNMKFklkqrEEQAEPDG-----TEEADKS----AYLMGLNSADLLKGLCHpRVKVGNEYV 411
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSGggcnvKPKSEQSleyaAELLGLDQDELRVSLTT-RVMQTTRGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 412 TKGQ------NVQQVIYATGALAKAVYERMFNWMVTRINATLETKQpRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 485
Cdd:cd01382 292 AKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 486 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNHLgKSANFQ 564
Cdd:cd01382 371 QQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-NHFRLS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 565 KPRniKGKPEAH--------FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADApiekGKG 636
Cdd:cd01382 449 IPR--KSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK----DSK 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 637 KAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 716
Cdd:cd01382 523 QKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFH 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1034587182 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 |
3.52e-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: 3.52e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVIQYFAVIAaigdrskkdQSPGKGTLEdQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGKLA 259
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVN---------QRRNNLVTE-QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDM--LLitnNPYDYAFISQGETT-VASIDDAEELMATDNAF 336
Cdd:cd01387 151 GAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKygLQ---EAEKYFYLNQGGNCeIAGKSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQRE---EQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 413
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 414 GQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 493
Cdd:cd01387 308 PLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 494 FVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRniKGK 572
Cdd:cd01387 388 FKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR--MPL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 573 PEahFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYagadAPIEKGKGKAKKGSSF-------Q 645
Cdd:cd01387 464 PE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH----RAQTDKAPPRLGKGRFvtmkprtP 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 646 TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 725
Cdd:cd01387 538 TVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1034587182 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 |
5.08e-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: 525.50 E-value: 5.08e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYML----TDRENQSI 174
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIqsgvLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 175 LITGESGAGKTVNTKRVIQY-------FAVIAAIGDRSKKDQSPGK-GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGK 246
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYlaritsgFAQGASGEGEAASEAIEQTlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 247 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNnPYDYAFISQGETTVASIDDA 326
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 327 EELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEA-DKSAYLMGLNSADLLKGLCHPRVK 405
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTLQSlKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 406 VGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 485
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 486 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILE--EEC--MFPKATDMTFKAKLFDNHLGKS 560
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgKVNGKPGIFItlDDCwrFKGEEANKKFVSQLHASFGRKS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 561 ANFQKPRNIKGKP---------EAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTlfanyagadapi 631
Cdd:cd14890 480 GSGGTRRGSSQHPhfvhpkfdaDKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIREV------------ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 632 ekgkgkakkgssfqTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPN 711
Cdd:cd14890 548 --------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFAL 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587182 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 |
1.24e-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: 1.24e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAVIAAIGDRskkdqspgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVLGKANNR----------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQIL----SNKKpeLLDMLLITNNPYDY-AFISQGETTVASID-DAEELMAT 332
Cdd:cd01379 151 TGARISEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKPPRYlQNDGLTVQDIVNNSgNREKFEEI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 333 DNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQ----AEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGN 408
Cdd:cd01379 229 EQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 409 EYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATL---ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 485
Cdd:cd01379 309 ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpdRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 486 QQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHlgKSANFQ 564
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYW 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 565 KPRnikgKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLStlfanyagadapiekgkgkakkgssf 644
Cdd:cd01379 466 RPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR-------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 645 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 724
Cdd:cd01379 516 QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1034587182 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 |
7.20e-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: 7.20e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRgKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 178 GESGAGKTVNTKRVIQYFAViAAIGDRSKKDqspgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF----- 252
Cdd:cd14888 80 GESGAGKTESTKYVMKFLAC-AGSEDIKKRS------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklks 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 253 ----GATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILS-----------------------NKKPELLDMLLI-T 304
Cdd:cd14888 153 krmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSFeP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 305 NNPYDYAFISqGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQA---EPDGTEEA 381
Cdd:cd14888 233 HLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 382 DKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVL 460
Cdd:cd14888 312 EKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 461 DIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLI-EKPMGIMSILEEECM 539
Cdd:cd14888 392 DIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECF 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 540 FPKATDMTFKAKLFDNHLGKSaNFQKprnIKGKPEAhFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLST 619
Cdd:cd14888 471 VPGGKDQGLCNKLCQKHKGHK-RFDV---VKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISN 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 620 LFANYagadapIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVL 699
Cdd:cd14888 546 LFSAY------LRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVL 619
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587182 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 |
6.79e-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: 6.79e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAY------RGKKRSEAPPHIFSISDNAYQYMLTDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 171 --NQSILITGESGAGKTVNTKRVIQYfavIAAIGDRSKKDQSPG-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 247
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNY---LASVSSATTHGQNATeRENVRDRVLESNPILEAFGNARTNRNNNSSRFGKF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 248 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVA--SIDD 325
Cdd:cd14901 158 IRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVE-EYKYLNSSQCYDRrdGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 326 AEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAY-LMGLNSADLLKGLCHPRV 404
Cdd:cd14901 237 SVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 405 KVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQP--RQYFIGVLDIAGFEIFDFNSFEQLCINFTN 482
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 483 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNhLGKSA 561
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 562 NFQKPRNIKGKpeAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTlfanyagadapiekgkgkakkg 641
Cdd:cd14901 475 SFSVSKLQQGK--RQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS---------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 642 ssfqTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 721
Cdd:cd14901 531 ----TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHT 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1034587182 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 |
2.16e-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: 503.06 E-value: 2.16e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 102 LYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESG 181
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 182 AGKTVNTKRVIQYFAVIaaigdrSKKDQSPGkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASA 261
Cdd:cd01385 84 SGKTESTNFLLHHLTAL------SQKGYGSG---VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 262 DIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNnPYDYAFISQGET-TVASIDDAEELMATDNAFDVLG 340
Cdd:cd01385 155 VVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDCyTLEGEDEKYEFERLKQAMEMVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 341 FTSEEKNSMYKLTGAIMHFGNMKFKLK--QREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd01385 234 FLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 419 QVIYATGALAKAVYERMFNWMVTRINATLETKQ----PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 494
Cdd:cd01385 314 EAIATRDAMAKCLYSALFDWIVLRINHALLNKKdleeAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 495 VLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKlFDNHLGKSANFQKPRnikgKP 573
Cdd:cd01385 394 KLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ----VM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 574 EAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLF------------------ANYAGADA------ 629
Cdd:cd01385 468 EPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIgidpvavfrwavlraffrAMAAFREAgrrraq 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 630 -----------PIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGV 698
Cdd:cd01385 548 rtaghsltlhdRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGM 627
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587182 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 |
3.00e-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: 485.03 E-value: 3.00e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 105 LKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRG--KKRSEAPPHIFSISDNAYQYMLTDR----ENQSILIT 177
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTPQSIVVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 178 GESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKG--TLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 255
Cdd:cd14892 87 GESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 256 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKpELLDMLLITNNPYDYAFISQGE-TTVASIDDAEELMATDN 334
Cdd:cd14892 167 GRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGNcVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 335 AFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKL--KQREEQAEPDGTEEADKSAYLMGLNSADLLKGLChPRVKVGneyvT 412
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV-TQTTST----A 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 413 KGQNVQ------QVIYATGALAKAVYERMFNWMVTRINAtlETKQ------------PRQYFIGVLDIAGFEIFDFNSFE 474
Cdd:cd14892 321 RGSVLEikltarEAKNALDALCKYLYGELFDWLISRINA--CHKQqtsgvtggaaspTFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 475 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEK-PMGIMSILEEECMFP-KATDMTFKAKL 552
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTIY 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 553 FDNHLGKSANFQKPRNikgkPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSslkllstlfanyagadapie 632
Cdd:cd14892 478 HQTHLDKHPHYAKPRF----ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS-------------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 633 kgkgkakkgSSFqtvsalhRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNR 712
Cdd:cd14892 534 ---------SKF-------RTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIR 597
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 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 |
3.51e-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: 481.99 E-value: 3.51e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAVIA--AIGDRSKKDQSpgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISqqSLELSLKEKTS----CVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITnNPYDYAFISQ-GETTVASIDDAEELMATDNA 335
Cdd:cd14873 158 NIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLNQsGCVEDKTISDQESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 336 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFklkqreeqAEPDGTEEADK-----SAYLMGLNSADLLKGLCHPRVKVGNEY 410
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLRGEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 411 VTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQyFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 490
Cdd:cd14873 309 ILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 491 HHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRnik 570
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPR--- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 571 gKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADApieKGKGKAKKGSSFQTVSAL 650
Cdd:cd14873 463 -VAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNN---QDTLKCGSKHRRPTVSSQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 651 HRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP-AA 729
Cdd:cd14873 539 FKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRnLA 618
|
650 660 670
....*....|....*....|....*....|....*..
gi 1034587182 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 |
2.68e-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: 473.41 E-value: 2.68e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKK-RSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVIQYFAVIaaigdrSKKDQSpgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKL------SPSDDS----DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGETTVASIDDAEELMATDNAFDVL 339
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELEYYRQMFHDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 340 -------GFTSEEKNSMYKLTGAIMHFGNMKFklkqrEEQAEPDGTEEADK-----SAYLMGLNSADLLKGLCHPRVKVG 407
Cdd:cd14897 232 tnimkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTIR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 408 NEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYF-----IGVLDIAGFEIFDFNSFEQLCINFTN 482
Cdd:cd14897 307 GERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLSN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 483 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLfDNHLGKSA 561
Cdd:cd14897 387 ERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 562 NFQKPrnIKGKPEahFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYagadapiekgkgkakkg 641
Cdd:cd14897 465 RYVAS--PGNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY----------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 642 ssfqtvsalHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 721
Cdd:cd14897 524 ---------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKR 594
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1034587182 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 |
1.10e-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: 1.10e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 178 GESGAGKTVNTKRVIQYFAVIAAigdrSKKDQSPGKgtledqIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG----GRKDKTIAK------VIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSN-KKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14904 151 LIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 337 DVLGFTSEEKNSMYKLTGAIMHFGNMKFkLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd14904 231 SLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 417 VQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQY-FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd14904 310 PVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 496 LEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNH--LGKSANFQKPRNIKgkp 573
Cdd:cd14904 390 TVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 574 eAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANyagADAPIEKGKGKA-KKGSSFQTVSALHR 652
Cdd:cd14904 466 -TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGS---SEAPSETKEGKSgKGTKAPKSLGSQFK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 653 ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE 732
Cdd:cd14904 542 TSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHS 621
|
650 660 670
....*....|....*....|....*....|....*
gi 1034587182 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 |
1.63e-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: 1.63e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAY-----------RGKKRSEAPPHIFSISDNAYQYM--- 165
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 166 -LTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRF 244
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 245 GKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLdmllitnnpydyafisqgettvaSID 324
Cdd:cd14900 163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAAR-----------------------KRD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 325 DAEELMAtdnAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFK-------LKQREEQAEPDGTEEADKSAYLMGLNSADLLK 397
Cdd:cd14900 220 MYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEhdensdrLGQLKSDLAPSSIWSRDAAATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 398 GLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATL-----ETKQPRQYFIGVLDIAGFEIFDFNS 472
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 473 FEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAK 551
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLASK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 552 LFdNHLGKSANFQKPRNIKGKpeAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQksslkllstlfanYAGAdapi 631
Cdd:cd14900 456 LY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV-------------YGLQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 632 ekgkgkakkgssfqtvsalHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPN 711
Cdd:cd14900 516 -------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPI 576
|
650 660
....*....|....*....|
gi 1034587182 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 |
1.65e-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: 452.82 E-value: 1.65e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYML----TDRENQSILI 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 177 TGESGAGKTVNTKRVIqyfaviaaigdRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATG 256
Cdd:cd14889 83 SGESGAGKTESTKLLL-----------RQIMELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQI---LSNKKPELLDMLlitnNPYDYAFISQG---ETTVASIDDA-EEL 329
Cdd:cd14889 151 HVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNGagcKREVQYWKKKyDEV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 330 MatdNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREE-QAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGN 408
Cdd:cd14889 227 C---NAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 409 EYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQY---FIGVLDIAGFEIFDFNSFEQLCINFTNEKL 485
Cdd:cd14889 304 EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVelrEIGILDIFGFENFAVNRFEQACINLANEQL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 486 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDL-IEKPMGIMSILEEECMFPKATDMTFKAKLfDNHLGKSANFQ 564
Cdd:cd14889 384 QYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 565 KPRNIKGKpeahFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSF 644
Cdd:cd14889 462 KSRSKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSDN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 645 ------QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 718
Cdd:cd14889 538 fnstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEF 617
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1034587182 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 |
1.18e-138 |
|
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: 447.94 E-value: 1.18e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGK--------KRSEAPPHIFSISDNAYQYMLTDREN 171
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 172 QSILITGESGAGKTVNTKRVIQYFAVIAA--------IGDRSKKDQ-SPGKGTLEDQIIQANPALEAFGNAKTVRNDNSS 242
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevLTLTSSIRAtSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 243 RFGKFIRIHFG-ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNP--YDYAFISQGET- 318
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLsgDRYDYLKKSNCy 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 319 TVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQ--REEQAEPDGTEEADKSAYLMGLNSADLL 396
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 397 KGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATL--------ETKQPRQYFIGVLDIAGFEIF 468
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 469 DFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF--IDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATD 545
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 546 MTFKAKLFDNHlGKSANFQKPRNIKGKpeaHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFanYA 625
Cdd:cd14907 482 EKLLNKIKKQH-KNNSKLIFPNKINKD---TFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF--SG 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 626 GADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRIC 705
Cdd:cd14907 556 EDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVR 635
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 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 |
3.49e-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: 434.47 E-value: 3.49e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGS--WMIYTYSGLFCVTVNPYKWLPvyTPEVvAAYRGKKRSEAPPHIFSISDNAYQYMLTDRE---NQS 173
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 174 ILITGESGAGKTVNTKRVIQY--------FAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFG 245
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFlttravggKKASGQDIEQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 246 KFIRIHFGATG-KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITnNPYDYAFISQ-GETTVASI 323
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLL-SPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 324 DDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKlKQREEQAEPDGTEEADK-----SAYLMGLNSADLLKG 398
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFD-EEDTSEGEAEIASESDKealatAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 399 LCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFD-FNSFEQLC 477
Cdd:cd14891 316 ITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 478 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNH 556
Cdd:cd14891 396 INYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 557 lGKSANFQKPRNiKGKPEAhFSLIHYAGIVDYNIIGWLQKNKDPLNETvvglyqksslklLSTLFANyagadapiekgkg 636
Cdd:cd14891 475 -KRHPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPED------------FEDLLAS------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 637 kakkgssfqtvSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 716
Cdd:cd14891 527 -----------SAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYA 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587182 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 |
3.56e-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: 437.02 E-value: 3.56e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYR--------GKKRSEAPPHIFSISDNAYQYML-TD 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 169 RENQSILITGESGAGKTVNTKRVIQYFAviaAIGDRSKKDQSPGKGTLE--DQIIQANPALEAFGNAKTVRNDNSSRFGK 246
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLT---SVGRDQSSTEQEGSDAVEigKRILQTNPILESFGNAQTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 247 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNpYDYAFISQGETTVA----- 321
Cdd:cd14902 158 FIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKG-GKYELLNSYGPSFArkrav 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 322 SIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEA---DKSAYLMGLNSADLLKG 398
Cdd:cd14902 237 ADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 399 LCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRIN-------ATLETKQPRQYF--IGVLDIAGFEIFD 469
Cdd:cd14902 317 LSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSdeinyfdSAVSISDEDEELatIGILDIFGFESLN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 470 FNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLqACIDLIE-KPMGIMSILEEECMFPKATDMTF 548
Cdd:cd14902 397 RNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNA-ACLALFDdKSNGLFSLLDQECLMPKGSNQAL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 549 KAKLFDNHLgksanfqkprnikgkPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGAD 628
Cdd:cd14902 476 STKFYRYHG---------------GLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 629 APIEKGKGKAKKGSSFQT--VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICR 706
Cdd:cd14902 541 PGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIAR 620
|
650 660
....*....|....*....|.
gi 1034587182 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 |
6.92e-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: 429.33 E-value: 6.92e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYR--GKKRS---EAP----PHIFSISDNAYQYMLTD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 169 RENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKD-QSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 247
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEgEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 248 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQIL------SNKKPELLDMLLITNN-PYDYAFISQGET-T 319
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDGITGGLQlPNEFHYTGQGGApD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 320 VASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAY---LMGLNSADLL 396
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 397 KGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATL--ETKQPRQYFIGVLDIAGFEIFDFNSFE 474
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 475 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFP-KATDMTFKAKL 552
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 553 FDNHL-------GKSANFQKPRNIKGKpeAHFSLIHYAGIVDYNI-IGWLQKNKDPLNETVVGLYQKsslkllSTLFany 624
Cdd:cd14908 480 YETYLpeknqthSENTRFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFES------GQQF--- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 625 agadapiekgkgkakkgssfqtvsalhRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRI 704
Cdd:cd14908 549 ---------------------------KAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRV 601
|
650 660
....*....|....*....|...
gi 1034587182 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 |
4.11e-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: 4.11e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYfavIAAIGDRSKKDQspgkgtlEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGKL 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQF---LSSLYQDQTEDR-------LRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGET-TVASIDDAEELMATDNAFD 337
Cdd:cd14896 150 VGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 338 VLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQRE--EQAEPDGTEEADKSAYLMGLnSADLLKGLCHPRVKVGN-EYVTKG 414
Cdd:cd14896 229 GLGLCAEELTAIWAVLAAILQLGNICFSSSEREsqEVAAVSSWAEIHTAARLLQV-PPERLEGAVTHRVTETPyGRVSRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 415 QNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYF--IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 492
Cdd:cd14896 308 LPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 493 MFVLEQEEYKKEGIEWTFIDfGMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSANFQKPRNikg 571
Cdd:cd14896 388 LLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL--- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 572 kPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANyagADAPIEKGKGKAKKGSSFQtvsalh 651
Cdd:cd14896 463 -PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE---AEPQYGLGQGKPTLASRFQ------ 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 652 rENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILnpAAIP 731
Cdd:cd14896 533 -QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL--GSER 609
|
650 660 670
....*....|....*....|....*....|....*
gi 1034587182 732 EGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14896 610 QEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
62-819 |
1.56e-128 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 424.83 E-value: 1.56e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 62 ETEYGKTVTVKEDQVMQQNPP-KFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVA 140
Cdd:PTZ00014 72 DPPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 141 AYR-GKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAViAAIGDRSKKDQspgkgtleDQ 219
Cdd:PTZ00014 152 RYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS-SKSGNMDLKIQ--------NA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 220 IIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLD 299
Cdd:PTZ00014 223 IMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 300 MLLITNNPyDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFklKQREEQAEPDGTE 379
Cdd:PTZ00014 303 KYKLKSLE-EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEI--EGKEEGGLTDAAA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 380 EADKS-------AYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQP 452
Cdd:PTZ00014 380 ISDESlevfneaCELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGG 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 453 RQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGI-----EWTfidfgmDLQACIDLI-EK 526
Cdd:PTZ00014 460 FKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGIsteelEYT------SNESVIDLLcGK 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 527 PMGIMSILEEECMFPKATDMTFKAKLFdNHLGKSANFQKPRNIKGKpeaHFSLIHYAGIVDYNIIGWLQKNKDPLNETVV 606
Cdd:PTZ00014 534 GKSVLSILEDQCLAPGGTDEKFVSSCN-TNLKNNPKYKPAKVDSNK---NFVIKHTIGDIQYCASGFLFKNKDVLRPELV 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 607 GLYQKSSLKLLSTLFanyagADAPIEKGKGKAKKGSSFQTVsalhrENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDN 686
Cdd:PTZ00014 610 EVVKASPNPLVRDLF-----EGVEVEKGKLAKGQLIGSQFL-----NQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNS 679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 687 PLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNpAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 766
Cdd:PTZ00014 680 SKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLK 758
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587182 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 |
2.29e-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: 397.79 E-value: 2.29e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTpevVAAYRGK--KRSEAPPHIFSISDNAYQYMLT-------D 168
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 169 RENQSILITGESGAGKTVNTKRVIQYFAVIA----AIGDRSKKDQSPGkgtleDQIIQANPALEAFGNAKTVRNDNSSRF 244
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSkhttATSSSKRRRAISG-----SELLSANPILESFGNARTLRNDNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 245 GKFIRIHFG-----ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDML-LITNNPYDYAFISQGET 318
Cdd:cd14895 153 GKFVRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELqLELLSAQEFQYISGGQC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 319 TVAS--IDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGT------------------ 378
Cdd:cd14895 233 YQRNdgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAasapcrlasaspssltvq 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 379 EEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQY--- 455
Cdd:cd14895 313 QHLDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnk 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 456 --------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-K 526
Cdd:cd14895 393 aankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 527 PMGIMSILEEECMFPKATDMTFKAKLFdNHLGKSANFQKPRniKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVV 606
Cdd:cd14895 472 PSGIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 607 GLYQKSSLKLLSTLFANY-AGADAPIEKGKGKAKKGSSFQT---VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPG 682
Cdd:cd14895 549 SVLGKTSDAHLRELFEFFkASESAELSLGQPKLRRRSSVLSsvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASD 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 683 VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPegqfidSRKGAEKLLSSLDIDHNQykFGHTK 762
Cdd:cd14895 629 QFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNA------SDATASALIETLKVDHAE--LGKTR 700
|
....
gi 1034587182 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 |
3.13e-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: 392.43 E-value: 3.13e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRG-KKRSEAPPHIFSIS----DNAYQYmltdRENQS 173
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTArralENLHGV----NKSQT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 174 ILITGESGAGKTVNTKRVIQYFAViaaigdrSKKDQSPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 253
Cdd:cd14876 77 IIVSGESGAGKTEATKQIMRYFAS-------AKSGNMDLR--IQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 254 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLD--MLLITNnpyDYAFISQGETTVASIDDAEELMA 331
Cdd:cd14876 148 SEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSkyHLLGLK---EYKFLNPKCLDVPGIDDVADFEE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 332 TDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQ-----AEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKV 406
Cdd:cd14876 225 VLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 407 GNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQ 486
Cdd:cd14876 305 GGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 487 QFFNHHMFVLEQEEYKKEGI-----EWTfidfgmDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLFDNhLGKS 560
Cdd:cd14876 385 KNFIDIVFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 561 ANFQKprnIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANyagadAPIEKGKGKAKK 640
Cdd:cd14876 458 GKFKP---AKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG-----VVVEKGKIAKGS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 641 GSSFQTVSalhreNLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ 720
Cdd:cd14876 530 LIGSQFLK-----QLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLY 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1034587182 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 |
6.76e-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: 6.76e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEA-PPHIFSISDNAYQYMLTDRE--NQSILI 176
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 177 TGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAER--IEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILsnkKPELLDMLLITNNP--YDYAFISQGETTVASiDDAEelmATDN 334
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQIC---KGASADERLQWHLPegAAFSWLPNPERNLEE-DCFE---VTRE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 335 AFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQA---EPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 411
Cdd:cd14880 234 AMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 412 TKGQNVQQVIYAT--GALAKAVYERMFNWMVTRINATLETKQPR-QYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 488
Cdd:cd14880 314 VFKKPCSRAECDTrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 489 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDmtfkAKLFDNHLGKS-ANFQKP 566
Cdd:cd14880 394 FVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSS----AAQLQTRIESAlAGNPCL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 567 RNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEkgkGKAKKGSSFQT 646
Cdd:cd14880 469 GHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEE---PSGQSRAPVLT 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 647 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL- 725
Cdd:cd14880 546 VVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLr 625
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1034587182 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 |
5.14e-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: 359.79 E-value: 5.14e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYR-------GKKRSEA---PPHIFSISDNAYQYMLTD 168
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 169 RENQSILITGESGAGKTVNTKRVIQYFAV-------IAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNS 241
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAVhcgtgnnNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 242 SRFGKFIRIHF-GATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNK----KPELLDMLLITNNPYDYAFISQG 316
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 317 ETTVA--SIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKL--KQREEQAEPDGTEEA----------D 382
Cdd:cd14899 242 LCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 383 KSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQY------- 455
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 456 --------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlQACIDLIE-K 526
Cdd:cd14899 402 ddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 527 PMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVV 606
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 607 GLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSAL--------HRENLNKLMTNLRSTHPHFVRCIIPNET 678
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIaavsvgtqFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1034587182 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 |
2.83e-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: 2.83e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 101 VLYNLKDRYGSWMI-YTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEA-PPHIFSISDNAY-QYMLTDRENQSILIT 177
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 178 GESGAGKTVNTKRVIQYFAVIAAIgdRSKkdqSPGKGTLEDQIIQ----ANPALEAFGNAKTVRNDNSSRFGKFIRIHF- 252
Cdd:cd14875 83 GESGSGKTENAKMLIAYLGQLSYM--HSS---NTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 253 GATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTV------ASIDDA 326
Cdd:cd14875 158 PTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 327 EELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEAdKSAYLMGLNSADLLKGLChprVKV 406
Cdd:cd14875 238 HEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL---VKS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 407 GNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLetkQPRQ-----YFIGVLDIAGFEIFDFNSFEQLCINFT 481
Cdd:cd14875 314 KTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASI---TPQGdcsgcKYIGLLDIFGFENFTRNSFEQLCINYA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 482 NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKS 560
Cdd:cd14875 391 NESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 561 ANFQKPrniKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADapiekgkgkakk 640
Cdd:cd14875 470 PYFVLP---KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLA------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 641 gSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF-R 719
Cdd:cd14875 535 -RRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFcR 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 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 |
9.23e-106 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 356.21 E-value: 9.23e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKR-SEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT-GK 257
Cdd:cd14906 83 ESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 258 LASADIETYLLEKSRVIFQL-KAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASI------------- 323
Cdd:cd14906 163 IDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsnhnn 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 324 --DDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQ---REEQAEPDGTEEADKSAYLMGLNSADLLKG 398
Cdd:cd14906 243 ktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFKQA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 399 LCHPRVKVGNE--YVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINAT-LETKQPRQ----------YFIGVLDIAGF 465
Cdd:cd14906 323 LLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKfNQNTQSNDlaggsnkknnLFIGVLDIFGF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 466 EIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKAT 544
Cdd:cd14906 403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPKGS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 545 DMTFKAKLfdNHLGKSANFQKPRNI-KGKpeahFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFan 623
Cdd:cd14906 482 EQSLLEKY--NKQYHNTNQYYQRTLaKGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLF-- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 624 yagaDAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIR 703
Cdd:cd14906 554 ----QQQITSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIK 629
|
650 660
....*....|....*....|...
gi 1034587182 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 |
1.92e-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: 348.53 E-value: 1.92e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 181 GAGKTVNTKRVIQYFAVIAAIgdrSKKDQSPGKgtledqiIQA-NPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAGS---VGGVLSVEK-------LNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFisqGETTVASIDD----AEELMATDNA 335
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF---GIVPLQKPEDkqkaAAAFSKLQAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 336 FDVLGFTSEEKNSMYKLTGAIMHFGN---MKFKLKQREEQAEPdgtEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVT 412
Cdd:cd01386 230 MKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQST 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 413 ---------------KGQNVQQviyATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------ 471
Cdd:cd01386 307 tssgqesparsssggPKLTGVE---ALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrga 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 472 SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEK---------------PMGIMSILEE 536
Cdd:cd01386 384 TFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLDE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 537 ECMFPKATDMTFKAKLFdNHLGKSANFQKPRNIKGKPEA-HFSLIHYAGI--VDYNIIGWLQKNK-DPLNETVVGLYQKS 612
Cdd:cd01386 464 EALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQES 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 613 SlKLLSTLFANYAGADApiekgkgkakkgsSFQtvsalhrenLNKLMTNLRSTHPHFVRCIIPN------------ETKS 680
Cdd:cd01386 543 Q-KETAAVKRKSPCLQI-------------KFQ---------VDALIDTLRRTGLHFVHCLLPQhnagkderstssPAAG 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 681 PGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA----AIPEGQFIDSRKGAEKLLSSLDIDHNQY 756
Cdd:cd01386 600 DELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkkLGLNSEVADERKAVEELLEELDLEKSSY 679
|
730
....*....|
gi 1034587182 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 |
5.45e-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: 345.72 E-value: 5.45e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 105 LKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRS-----EAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAViaaigdrskkDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAY----------GHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQI---LSNKKPELLDMLLITNnpydYAFISQGET-TVASIDDAEELMATDN 334
Cdd:cd14886 157 KGGKITSYMLELSRIEFQSTNERNYHIFYQCikgLSPEEKKSLGFKSLES----YNFLNASKCyDAPGIDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 335 AFDVLgFTSEEKNSMYKLTGAIMHFGNMKFKLKQR---EEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 411
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 412 TKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 491
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFIN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 492 HMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKP-MGIMSILEEECMFPKATDMTFKAKLfDNHLgKSANFqkprnIK 570
Cdd:cd14886 392 QVFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF-----IP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 571 GKPEA-HFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLstlfaNYAGADAPIEKGKGKAkkgssfQTVSA 649
Cdd:cd14886 464 GKGSQcNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIV-----NKAFSDIPNEDGNMKG------KFLGS 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 650 LHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL---N 726
Cdd:cd14886 533 TFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishN 612
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1034587182 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 |
5.43e-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: 323.00 E-value: 5.43e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKwlPVYTPEVVAAYRgKKRSEAPPHIFSISDNAYQYMLTdRENQSILITGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVIQYFAviaaigdrskkDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgaTGKLA 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLV-----------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKIT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKpelldmLLITNNPYDYAFISQGETTVasIDDAEELMATDNAFDVL 339
Cdd:cd14898 145 GAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSAMKSL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 340 GFTSEEknSMYKLTGAIMHFGNMKFklkQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQ 419
Cdd:cd14898 217 GIANFK--SIEDCLLGILYLGSIQF---VNDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 420 VIYATGALAKAVYERMFNWMVTRINATLETKQPRQyfIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 499
Cdd:cd14898 292 ARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 500 EYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKAT--DMTFKAKLFDNHlgksanfqkprNIKGKPEAHF 577
Cdd:cd14898 370 MYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNG-----------FINTKARDKI 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 578 SLIHYAGIVDYNIIGWLQKNKdplnetvvglyQKSSLKLLSTLFANYAGadapiekgkgkakkgsSFQTVSALHRENLNK 657
Cdd:cd14898 438 KVSHYAGDVEYDLRDFLDKNR-----------EKGQLLIFKNLLINDEG----------------SKEDLVKYFKDSMNK 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 658 LMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIpegQFID 737
Cdd:cd14898 491 LLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLF---EVVD 567
|
....
gi 1034587182 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 |
2.78e-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: 2.78e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYR---GKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 176
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 177 TGESGAGKTVNTKRVIQYFAViaaigdRSkkdqSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTC------RA----SSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 257 K-LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGE----TTVASIDDAEELMA 331
Cdd:cd14878 152 KhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHL-NNLCAHRYLNQTMredvSTAERSLNREKLAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 332 TDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 411
Cdd:cd14878 231 LKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 412 TKGQNVQQVIYATGALAKAVYERMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQ 487
Cdd:cd14878 311 IRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 488 FFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLfdNHLGKSANFQ-- 564
Cdd:cd14878 391 YINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDFFfQKPSGFLSLLDEESQMIWSVEPNLPKKL--QSLLESSNTNav 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 565 ----KPRNIKGKPEAH---FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFanyagadapiekgkgk 637
Cdd:cd14878 469 yspmKDGNGNVALKDQgtaFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF---------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 638 akkGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGD 717
Cdd:cd14878 533 ---QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSD 609
|
....*...
gi 1034587182 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 |
8.16e-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: 8.16e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGS--------WMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 171 NQSILITGESGAGKTVNTKRVIQYfavIAAIGDRSKKDQSPGkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTY---LAAVSDRRHGADSQG---LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 251 HFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKK-PELLDMLLITNNPYDYafisqgettvasiddaeEL 329
Cdd:cd14887 155 HFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVaAATQKSSAGEGDPEST-----------------DL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 330 MATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPD-------GTEE--ADKS--AYLMGLNS------ 392
Cdd:cd14887 218 RRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRkltsvsvGCEEtaADRShsSEVKCLSSglkvte 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 393 ------ADLLKGLCHPRVKVGNEYV------------TKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQ 454
Cdd:cd14887 298 asrkhlKTVARLLGLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 455 Y--------------FIGVLDIAGFEIF---DFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEG--IEWTFIDFGM 515
Cdd:cd14887 378 EsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCSAFPF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 516 DLQACIDLIEKP------------------------MGIMSILEEE-CMFPKATDMTFKAKLFDNHLGKSA-NFQKPRNI 569
Cdd:cd14887 458 SFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKNIiNSAKYKNI 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 570 K---GKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYqksslkllstLFANYAGADAPIEKGKGKAKKGSSFQT 646
Cdd:cd14887 538 TpalSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF----------LACSTYTRLVGSKKNSGVRAISSRRST 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 647 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 726
Cdd:cd14887 608 LSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKL 687
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1034587182 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 |
2.26e-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: 294.23 E-value: 2.26e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEvvaaYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 181 GAGKTVNTKRVIQYFavIAAIgdrsKKDQSPGKgTLEDqiiqANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 260
Cdd:cd14937 79 GSGKTEASKLVIKYY--LSGV----KEDNEISN-TLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 261 ADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVASIDDAEELMATDNAFDVLG 340
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 341 FTSEEKNSMYKLTGAIMhFGNMKFKL-----KQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 415
Cdd:cd14937 227 MHDMKDDLFLTLSGLLL-LGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 416 NVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd14937 306 SVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 496 LEQEEYKKEGIEWTFIDFGMDlQACIDLIEKPMGIMSILEEECMFPKATDMTFkAKLFDNHLGKSANFQKPRNIKGKpea 575
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYASTKKDINK--- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 576 HFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADApiekgkgkakkGSSFQTVSALHRENL 655
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSES-----------LGRKNLITFKYLKNL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 656 NKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRIcRKGFPNRILYGDFRQRYRILNPAAIPEGQF 735
Cdd:cd14937 530 NNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSL 608
|
650 660 670
....*....|....*....|....*....|.
gi 1034587182 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 |
7.00e-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: 287.14 E-value: 7.00e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 105 LKDRYGSWMIYTY---SGLfcVTVNPYKWLPVYTPEVVAAYR-------GKKRSEAPPHIFSISDNAYQYMLTDRENQSI 174
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 175 LITGESGAGKTVNTKRVIQyfaviaAIGDRSKkdqSPGKGT-LEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 253
Cdd:cd14879 88 VFLGETGSGKSESRRLLLR------QLLRLSS---HSKKGTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 254 ATGKLASADIETYLLEKSRVIfQLKA-ERDYHIFYQILSNKKPELLDMLLItNNPYDYAFI--SQGETTVAS--IDDAEE 328
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGL-DDPSDYALLasYGCHPLPLGpgSDDAEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 329 LMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFklkqreeQAEPDGTEEA---------DKSAYLMGLNSADLLKGL 399
Cdd:cd14879 237 FQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEF-------TYDHEGGEESavvkntdvlDIVAAFLGVSPEDLETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 400 CHPRVKVGNEYVTkgqnvqqvIY--ATGA------LAKAVYERMFNWMVTRINATL-ETKQPRQYFIGVLDIAGFEIFD- 469
Cdd:cd14879 310 TYKTKLVRKELCT--------VFldPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSs 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 470 --FNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEEC-MFPKATD 545
Cdd:cd14879 382 tgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 546 MTFKAKLfDNHLGKSANFQKPRNIKGKPEAH-FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLyqksslkLLSTLFANY 624
Cdd:cd14879 461 EQMLEAL-RKRFGNHSSFIAVGNFATRSGSAsFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNL-------LRGATQLNA 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 625 AgadapiekgkgkakkgssfqtvsalhrenLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRI 704
Cdd:cd14879 533 A-----------------------------LSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAAR 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 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 |
1.58e-74 |
|
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: 263.69 E-value: 1.58e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYRGKKRSEA-------PPHIFSISDNAYQYMLTDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 171 NQSILITGESGAGKTVNTKRVIQYFAVIAaiGDRSKKDqspgkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQ--TDSQMTE-------RIDKLIYINNILESMSNATTIKNNNSSRCGRINLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 251 HF---------GATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGE---- 317
Cdd:cd14884 152 IFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEshqk 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 318 --------TTVASIDDAEELMATD--------NAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLkqreeqaepdgteea 381
Cdd:cd14884 232 rsvkgtlrLGSDSLDPSEEEKAKDeknfvallHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA--------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 382 dkSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINAT----------LETKQ 451
Cdd:cd14884 297 --AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNvlkckekdesDNEDI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 452 PR--QYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF--GMDLQACIDLIEKP 527
Cdd:cd14884 375 YSinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVApsYSDTLIFIAKIFRR 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 528 MGIMSILEEECMfpKATDMTFKAKLFDN----HLGK--SANFQKPRNIKGKPEAH------FSLIHYAGIVDYNIIGWLQ 595
Cdd:cd14884 455 LDDITKLKNQGQ--KKTDDHFFRYLLNNerqqQLEGkvSYGFVLNHDADGTAKKQnikkniFFIRHYAGLVTYRINNWID 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 596 KNKDPLNETVVGLYQKSSLKLLStlfanyagadapiekGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIP 675
Cdd:cd14884 533 KNSDKIETSIETLISCSSNRFLR---------------EANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLP 597
|
650 660 670
....*....|....*....|....*....|....*....
gi 1034587182 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 |
1.91e-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: 1.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYrgkkrseappHIFSISDNAYQYMLTDREN-QSILITG 178
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 179 ESGAGKTVNTKRVIQYFAviaaigdrskkdQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14874 72 ESGSGKSYNAFQVFKYLT------------SQPKSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNpYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14874 140 GLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL-QKFFYINQGNSTENIQSDVNHFKHLEDALHV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 339 LGFTSEEKNSMYKLTGAIMHFGNMKFKLKQ----REEQAEPDGTEEADKSAYLMGLNSADLLKGLChPRVKVGNEYvtkg 414
Cdd:cd14874 219 LGFSDDHCISIYKIISTILHIGNIYFRTKRnpnvEQDVVEIGNMSEVKWVAFLLEVDFDQLVNFLL-PKSEDGTTI---- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 415 qNVQQVIYATGALAKAVYERMFNWMVTRINatLETKQPRQY-FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 493
Cdd:cd14874 294 -DLNAALDNRDSFAMLIYEELFKWVLNRIG--LHLKCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 494 FVLEQEEYKKEGIEwtfIDFGMdlQACID-------LIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSAnFQKP 566
Cdd:cd14874 371 FHDQLVDYAKDGIS---VDYKV--PNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGKA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 567 RNikgKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQT 646
Cdd:cd14874 445 RN---KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMIVSQAQFILRGAQEI 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 647 VsalhrENLNKlmtnlrsTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 726
Cdd:cd14874 522 A-----DKING-------SHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLL 589
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1034587182 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 |
7.22e-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: 7.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 100 AVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPvyTPEVVAAYRGKKRSeapPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 180 SGAGKTVNTKRVI-QYFAVIaaigdrskkdqspGKGTLED---QIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgAT 255
Cdd:cd14881 77 SGSGKTYASMLLLrQLFDVA-------------GGGPETDafkHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 256 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITN-NPYDYAFISQGETTVASIDDAEELMATDN 334
Cdd:cd14881 143 GALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGySPANLRYLSHGDTRQNEAEDAARFQAWKA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 335 AFDVLG--FTSeeknsMYKLTGAIMHFGNMKFkLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGL---CHprvkvgne 409
Cdd:cd14881 223 CLGILGipFLD-----VVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRGLttrTH-------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 410 yVTKGQNVQQVIYAT------GALAKAVYERMFNWMVTRIN------ATLETKQpRQYFIGVLDIAGFEIFDFNSFEQLC 477
Cdd:cd14881 289 -NARGQLVKSVCDANmsnmtrDALAKALYCRTVATIVRRANslkrlgSTLGTHA-TDGFIGILDMFGFEDPKPSQLEHLC 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 478 INFTNEKLQQFFNHHMFVLEQEEYKKEGIewtfidfGMDLQA-------CIDLIEK-PMGIMSILEEECMfPKATDMTFK 549
Cdd:cd14881 367 INLCAETMQHFYNTHIFKSSIESCRDEGI-------QCEVEVdyvdnvpCIDLISSlRTGLLSMLDVECS-PRGTAESYV 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 550 AKLfdnhlgKSANFQKPRNIKGKPEA--HFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLkllSTLFANYAga 627
Cdd:cd14881 439 AKI------KVQHRQNPRLFEAKPQDdrMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNC---NFGFATHT-- 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 628 dapiekgkgkakkgSSFQTvsalhreNLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRK 707
Cdd:cd14881 508 --------------QDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAG 566
|
650 660 670
....*....|....*....|....*....|....*....
gi 1034587182 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 |
1.40e-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: 1.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 105 LKDRYGSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVAAYrgKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAG 183
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 184 KTVNTKRVIQYfaVIAAIGDRSKkdqspgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADI 263
Cdd:cd14905 85 KSENTKIIIQY--LLTTDLSRSK--------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 264 ETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITN-NPYDYafISQGET-TVASIDDAEELMATDNAFDVLGF 341
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDiNSYHY--LNQGGSiSVESIDDNRVFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 342 TSEEKNSMYKLTGAIMHFGNMKFKLKQREeqaepdgTEEADKSaylmglnsadLLKGLCH----PRVKVGNEYVT-KGQN 416
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRT----------LIESLSHnitfDSTKLENILISdRSMP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 417 VQQVIYATGALAKAVYERMFNWMVTRINATLetkQPRQY--FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 494
Cdd:cd14905 296 VNEAVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 495 VLEQEEYKKEGIEW-TFIDFgMDLQACIDLIEKpmgIMSILEEECMFPKATDMTFKAKLfdnhlgksANFQKPRNIKGKP 573
Cdd:cd14905 373 KQEQREYQTERIPWmTPISF-KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 574 EAHFSLIHYAGIVDYNIIGWLQKNKDP-------------------------LNETVVGLYQ---------KSSLKLLST 619
Cdd:cd14905 441 PNKFGIEHYFGQFYYDVRGFIIKNRDEilqrtnvlhknsitkylfsrdgvfnINATVAELNQmfdakntakKSPLSIVKV 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 620 LFA--------------NYAGADAPIEKGKGKAKKGSSFQTVSAlhrenLNKLMTNlRSTHPHFVRCIIPNETKSPGVMD 685
Cdd:cd14905 521 LLScgsnnpnnvnnpnnNSGGGGGGGNSGGGSGSGGSTYTTYSS-----TNKAINN-SNCDFHFIRCIKPNSKKTHLTFD 594
|
650 660 670
....*....|....*....|....*....|....*..
gi 1034587182 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 |
1.59e-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: 1.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 102 LYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKR----------SEAPPHIFSISDNAYQYMLTDREN 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 172 QSILITGESGAGKTVNTKRVIQYfavIAAIGDRS--KKDQSPGKGTLE---DQIIQANPALEAFGNAKTVRNDNSSRFGK 246
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQY---LCEIGDETepRPDSEGASGVLHpigQQILHAFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 247 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKK--PELLDMLLITNNPYDYAFISQG--ETTVAS 322
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 323 ID--DAEELMATdnaFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLN-------SA 393
Cdd:cd14893 241 LDarDYRDLMSS---FSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQSCALKdpaqillAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 394 DLLKglCHPRV------------KVGNEYVT--KGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPR------ 453
Cdd:cd14893 318 KLLE--VEPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 454 ---QYFIGVLDIAGFEIFD--FNSFEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEG--IEWTFIDFGMDLQACI 521
Cdd:cd14893 396 vinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 522 DLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNH-----LGKSANFQKPRNIKGKPEAHFSLI----HYAGIVDYNII 591
Cdd:cd14893 476 QLFEdKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNeavggLSRPNMGADTTNEYLAPSKDWRLLfivqHHCGKVTYNGK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 592 GWLQKNKDPLNETVVGLYQKSSLKLLSTLFANY---AGADAPIEKGKGKAKKGSSFQTVSALHRENLN------------ 656
Cdd:cd14893 556 GLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQmaaASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynq 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 657 --KLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRilnpaaipegQ 734
Cdd:cd14893 636 adALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK----------N 705
|
730 740 750
....*....|....*....|....*....|....*
gi 1034587182 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 |
4.02e-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: 4.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 121 FCVTVNPYKWLPVYTPEVV-AAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587182 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 |
2.08e-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: 2.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 101 VLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 181 GAGKTVNTKRVIQYFAViaaIGDrskkdqspGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 260
Cdd:cd14882 83 YSGKTTNARLLIKHLCY---LGD--------GNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 261 ADIETYLLEKSRVIFQLKAERDYHIFYQILS--NKKPELLDMLLITNNPYDYAFISQG-------------ETTVASIDD 325
Cdd:cd14882 152 AIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 326 AEELmatdnaFDVLGFTSEEKNSMYKLTGAIMHFGNMKFklKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVK 405
Cdd:cd14882 232 FEEI------LKDLDFNEEQLETVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 406 VGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETkqPR-----QYFIGVLDIAGFEIFDFNSFEQLCINF 480
Cdd:cd14882 304 KGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVNT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 481 TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEecmfpKATDMTFKAKLFDNHLGKS 560
Cdd:cd14882 382 LNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 561 ANFQKPRNikgkpeAH-FSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANyagadapiekgkgkaK 639
Cdd:cd14882 457 SQFVKKHS------AHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN---------------S 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 640 KGSSFQTVSALHR----ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILY 715
Cdd:cd14882 516 QVRNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPF 595
|
650
....*....|
gi 1034587182 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 |
2.17e-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: 173.87 E-value: 2.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 99 PAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSE-APPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 178 GESGAGKTVNTKRVIQYFAViAAIGDRSKKDQS--------------PGKGTLEDQIIQANPALEAFGNAKTVRNDNSSR 243
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAY-QVKGSRRLPTNLndqeednihneentDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 244 FGKFIRIHFgATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYdYAFISQGETTVASI 323
Cdd:cd14938 160 FSKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIEN-YSMLNNEKGFEKFS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 324 DDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGN-------------MKFKLKQRE----------EQAEPDGTEE 380
Cdd:cd14938 238 DYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 381 ADKSAYL----MGLNSADLLKGLCHPRVkVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYF 456
Cdd:cd14938 318 NVKNLLLacklLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 457 ---IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM--GIM 531
Cdd:cd14938 397 tnyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 532 SILEEECMfPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAhFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQK 611
Cdd:cd14938 477 SLLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 612 SSLKLLSTL--FANYAGADAPIEKGKG----------KAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETK 679
Cdd:cd14938 555 SENEYMRQFcmFYNYDNSGNIVEEKRRysiqsalklfKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 680 SP-GVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPaaipegqfiDSRKGAEKLLSSLDIDHNQYKF 758
Cdd:cd14938 635 RElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMI 705
|
....*.
gi 1034587182 759 GHTKVF 764
Cdd:cd14938 706 GNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1173-1930 |
9.63e-33 |
|
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: 139.42 E-value: 9.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1173 KMRRdlEEATLQHEATAAALrKKHADSVAELGEQIDNLQRVKQK----LEKEKSEFKLELDDVTSNMEQIIKAKANLEKM 1248
Cdd:TIGR02168 171 KERR--KETERKLERTRENL-DRLEDILNELERQLKSLERQAEKaeryKELKAELRELELALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1249 CRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEevkAKNA 1328
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE---LEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1329 LAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRtkyetDAIQRTEELEEAKKKLAQRLQEAEEAVEAVN 1408
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE-----ELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1409 AKCSSLEKTKHRLQNEIEDLMVDVE--RSNAAAAALDKKQRNF---DKILAEWKQKYEESQSELESSQKEARSLSTELFK 1483
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEelLKKLEEAELKELQAELeelEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1484 LKN----------AYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEA---EKME------LQSAL 1544
Cdd:TIGR02168 480 AERelaqlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAalgGRLQavvvenLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1545 EEAEASLEHEEGK--------ILRAQLEFN--QIKAEIERKLAEKDEEMEQAKR---------NHLRVVDSLQTSLDAET 1605
Cdd:TIGR02168 560 KAIAFLKQNELGRvtflpldsIKGTEIQGNdrEILKNIEGFLGVAKDLVKFDPKlrkalsyllGGVLVVDDLDNALELAK 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1606 RSRNEALRVKKkmEGDL-----------NEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIV 1674
Cdd:TIGR02168 640 KLRPGYRIVTL--DGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1675 -------ERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQE 1747
Cdd:TIGR02168 718 rkeleelSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1748 CRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKgGKKQLQKLEARVRELENELE 1827
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1828 AEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFR-KVQHELDEA 1906
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEA 956
|
810 820
....*....|....*....|....
gi 1034587182 1907 EERADIAESQVNKLRAKSRDIGTK 1930
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
840-1672 |
4.50e-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: 130.56 E-value: 4.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 840 LKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKV 919
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 920 KEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKAL 999
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1000 QEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLEraKRKLEGDLKLTQESIMDLENDKQQLDER 1079
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1080 LKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERT---ARAKVEKLRSDLSRELEEISER------- 1149
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfseGVKALLKNQSGLSGILGVLSELisvdegy 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1150 ---LEEAGGATSVQIEMNKKREAefqkmrRDLEEATLQHEATAAAL----RKKHADSVAELGEQIDNLQRVKQ---KLEK 1219
Cdd:TIGR02168 536 eaaIEAALGGRLQAVVVENLNAA------KKAIAFLKQNELGRVTFlpldSIKGTEIQGNDREILKNIEGFLGvakDLVK 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1220 EKSEFKLEL----------DDVTSNMEQIIKAKANLekMCRTLEDQM-----------NEHRSKAEETQRSVNDLTSQRA 1278
Cdd:TIGR02168 610 FDPKLRKALsyllggvlvvDDLDNALELAKKLRPGY--RIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIE 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1279 KLQTENGELSRQLDEKEALISQLtrgkltyTQQLEDLKRQLEEEVKAKNALAHALQSArhdcdllreqyEEETEAKAELQ 1358
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEEL-------EEELEQLRKELEELSRQISALRKDLARL-----------EAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1359 RVLSKANSEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLmvdversNAA 1438
Cdd:TIGR02168 750 AQLSKELTELEAEIEELE----ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-------NEE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1439 AAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGS 1518
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1519 SGKTIHELEKVRKQLEAEKMELQSALEEAEASLEheegkilRAQLEFNQIKAeierKLAEKDE-EMEQAKRNHLRVVDSL 1597
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLE-------GLEVRIDNLQE----RLSEEYSlTLEEAEALENKIEDDE 967
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034587182 1598 QtsldaETRSRNEALRVKKKMEGDLNEMEIQlshanrmaaEAQKQVKSLQSLLKdtqiQLDDAVRANDDLKENIA 1672
Cdd:TIGR02168 968 E-----EARRRLKRLENKIKELGPVNLAAIE---------EYEELKERYDFLTA----QKEDLTEAKETLEEAIE 1024
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
942-1871 |
1.29e-28 |
|
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: 125.94 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 942 KLEDECSELKRDIDDLELTLAKVEkekhatenKVKNLTEEMAGLDeiIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLT 1021
Cdd:TIGR02168 190 RLEDILNELERQLKSLERQAEKAE--------RYKELKAELRELE--LALLVLRLEELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1022 KAKVKLEQQVDDLEGSLEQekkvrmdLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEdeqalg 1101
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSE-------LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE------ 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1102 sQLQKKLKELQARIeeleeeleaertarAKVEKLRSDLSRELEEISERLEEAGGatsvQIEMNKKREAEFQKMRRDLEEA 1181
Cdd:TIGR02168 327 -ELESKLDELAEEL--------------AELEEKLEELKEELESLEAELEELEA----ELEELESRLEELEEQLETLRSK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1182 TLQHEATAAALRKKhadsVAELGEQIDNLQRVKQKLEKEKSEFKLELDdvtsnmeqiikakanlekmcrtlEDQMNEHRS 1261
Cdd:TIGR02168 388 VAQLELQIASLNNE----IERLEARLERLEDRRERLQQEIEELLKKLE-----------------------EAELKELQA 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1262 KAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVK----AKNALAHALQSAR 1337
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegVKALLKNQSGLSG 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1338 HDcDLLREQYEEETEAKAELQRVLSKANSEVAqwrTKYETDAIQRTEELEEAKK--------------KLAQRLQEAEEA 1403
Cdd:TIGR02168 521 IL-GVLSELISVDEGYEAAIEAALGGRLQAVV---VENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKN 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1404 VEAVNAKCSSLEKTKHRLQNEIEDL-----MVD-VERSNAAAAALDKKQRNF----DKILAEWkqkyeesqseleSSQKE 1473
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRKALSYLlggvlVVDdLDNALELAKKLRPGYRIVtldgDLVRPGG------------VITGG 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1474 ARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLgssgktiHELEKVRKQLEAEKMELQSALEEAEASLEH 1553
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL-------EELEEELEQLRKELEELSRQISALRKDLAR 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1554 EEGKILRAQLEFNQIKAEIERKLAEKDEEMEQakrnhlrvvdslqtsLDAETRSRNEALRVKKKMEGDLNEMEIQLSHAN 1633
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEER---------------LEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1634 RMAAEAQKQvkslqslLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIEtserv 1713
Cdd:TIGR02168 803 EALDELRAE-------LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE----- 870
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1714 qlLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNMEQTIKDL 1793
Cdd:TIGR02168 871 --LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE---LRLEGLEVRIDNLQERL 945
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1794 --QHRLDEAEQIALK-GGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDK 1870
Cdd:TIGR02168 946 seEYSLTLEEAEALEnKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
.
gi 1034587182 1871 L 1871
Cdd:TIGR02168 1026 I 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
833-1452 |
1.94e-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: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 833 YFKIKPLLKSAERE---KEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLI 909
Cdd:COG1196 215 YRELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 910 KNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEII 989
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 990 AKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDL 1069
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1070 ENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAK---------VEKLRSDLS 1140
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLaglrglagaVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1141 RELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKE 1220
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1221 KSEFKLELDDVTSNMEQIIKAKAnlekmcrtledQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQ 1300
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALR-----------RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1301 LTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAqwrtKYETDAI 1380
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPEP 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1381 QRTEELEEAKKKLAQRLQE-------AEEAVEAVNAKCSSLEKTKHRLQNEIEDLM-----VDVERSNAAAAALDKKQRN 1448
Cdd:COG1196 760 PDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEeaieeIDRETRERFLETFDAVNEN 839
|
....
gi 1034587182 1449 FDKI 1452
Cdd:COG1196 840 FQEL 843
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
963-1851 |
3.65e-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: 114.77 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 963 KVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALD--DLQAEEDKVNtLTKAKVKLEQQVDDLEGSLEQ 1040
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykELKAELRELE-LALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1041 EKKvrmdLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDeqalgsqLQKKLKELQARIEELEE 1120
Cdd:TIGR02168 248 LKE----AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR-------LEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1121 ELEAERTARAKVEKLRSDLSRELEEISERLEEAggatSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsV 1200
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEEL----KEELESLEAELEELEAELEELESRLEELEEQLETLRSK----V 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1201 AELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKmcRTLEDQMNEHRSKAEETQRSVNDLTSQRAKL 1280
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEEL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1281 QTENGELSRQLDEKEALISQLtRGKLTYTQQLEDLKRQLEEEVKakNALAHALQSARHDcDLLREQYEEETEAKAELQRV 1360
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSEGVK--ALLKNQSGLSGIL-GVLSELISVDEGYEAAIEAA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1361 LSKANSEVAqwrTKYETDAIQRTEELEEAKK--------------KLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIE 1426
Cdd:TIGR02168 543 LGGRLQAVV---VENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1427 DL-----MVD-VERSNAAAAALDKKQRNF----DKILAEWkqkyeesqseleSSQKEARSLSTELFKLKNAYEESLEHLE 1496
Cdd:TIGR02168 620 YLlggvlVVDdLDNALELAKKLRPGYRIVtldgDLVRPGG------------VITGGSAKTNSSILERRREIEELEEKIE 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1497 TFKRENKNLQEEISDLTEQLgssgktiHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKL 1576
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKEL-------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1577 AEKDEEMEQakrnhlrvvdslqtsLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQvkslqslLKDTQIQ 1656
Cdd:TIGR02168 761 AEIEELEER---------------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE-------LTLLNEE 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1657 LDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIEtservqlLHSQNTSLINQKKKMDADLSQ 1736
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-------LESELEALLNERASLEEALAL 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1737 LQTEVEEAVQECRNAEEKakkaitdaammaeelkkeqdtsahlermkknmeqtIKDLQHRLDEAEQiALKGGKKQLQKLE 1816
Cdd:TIGR02168 892 LRSELEELSEELRELESK-----------------------------------RSELRRELEELRE-KLAQLELRLEGLE 935
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 1034587182 1817 ARVRELENELEAEQKRNAESVKGM--------RKSERRIKELT 1851
Cdd:TIGR02168 936 VRIDNLQERLSEEYSLTLEEAEALenkieddeEEARRRLKRLE 978
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
840-1700 |
7.50e-25 |
|
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: 113.62 E-value: 7.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 840 LKSAEREKEMAsmkEEFTRLKEalEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKV 919
Cdd:TIGR02169 200 LERLRREREKA---ERYQALLK--EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 920 KEMNERLEDE-EEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 998
Cdd:TIGR02169 275 EELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 999 LQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDkqqlde 1078
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA------ 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1079 rLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERL----EEAG 1154
Cdd:TIGR02169 429 -IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseERVR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1155 GATSVQIEMNKKREAEFQKMRrDLEEATLQHEA---TAAALRKKHA----DSVAElgEQIDNLQRVKQ------KLEKEK 1221
Cdd:TIGR02169 508 GGRAVEEVLKASIQGVHGTVA-QLGSVGERYATaieVAAGNRLNNVvvedDAVAK--EAIELLKRRKAgratflPLNKMR 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1222 SEfklELDDVTSNMEQIIKAKANLekmcRTLEDQMNEHRSKAEETQRSVNDLTSQRA-----KLQTENGELSrqldEKEA 1296
Cdd:TIGR02169 585 DE---RRDLSILSEDGVIGFAVDL----VEFDPKYEPAFKYVFGDTLVVEDIEAARRlmgkyRMVTLEGELF----EKSG 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1297 LIS----QLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRvLSKANSEVAQwr 1372
Cdd:TIGR02169 654 AMTggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE-IEKEIEQLEQ-- 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1373 tkYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNaaaaaLDKKQRNFDKI 1452
Cdd:TIGR02169 731 --EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR-----IPEIQAELSKL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1453 laewkqkyeesqselessQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQ 1532
Cdd:TIGR02169 804 ------------------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1533 LEAEKMELQSALEEAEASLEHEEGKILRAQLEfnqiKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEAL 1612
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELEAQ----LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1613 RVKKKMEGDLNEMEIQLshanrMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEniaiverRNNLLQAELEELRAVV 1692
Cdd:TIGR02169 942 EDEEIPEEELSLEDVQA-----ELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE-------KRAKLEEERKAILERI 1009
|
....*...
gi 1034587182 1693 EQTERSRK 1700
Cdd:TIGR02169 1010 EEYEKKKR 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1310-1928 |
4.86e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.80 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1310 QQLEDLKRQ-----------LEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVaqwrtkyetd 1378
Cdd:COG1196 200 RQLEPLERQaekaeryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL---------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1379 aiqrtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQ 1458
Cdd:COG1196 270 -----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1459 KYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKM 1538
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1539 ELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRsrneaLRVKKKM 1618
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-----LLLLLEA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1619 EGDlnemeiqlshanrmAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQaeleelRAVVEQTERS 1698
Cdd:COG1196 500 EAD--------------YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ------NIVVEDDEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1699 RKLAEQELIETSERVQLLHSqntSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAH 1778
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPL---DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1779 LERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVkgmRKSERRIKELTYQTEEDR 1858
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL---EEALLAEEEEERELAEAE 713
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1859 KNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSkfrKVQHELDEAEERADIAESQVNKLRAKSRDIG 1928
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLE---EEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1106-1909 |
3.28e-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: 108.23 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1106 KKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEaggatsVQIEMNKKReaEFQKMRRDLEEAtlqh 1185
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLER------LRREREKAE--RYQALLKEKREY---- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1186 EATAAALRKKHADsvaelgEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTL-EDQMNEHRSKAE 1264
Cdd:TIGR02169 224 EGYELLKEKEALE------RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1265 ETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRgkltytqQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLR 1344
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA-------EIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1345 EQYEEETEAKAELQRvlskansEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNE 1424
Cdd:TIGR02169 371 AELEEVDKEFAETRD-------ELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1425 IEDLMVDVErsnaaaaALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLknayEESLEHLETFKRENKN 1504
Cdd:TIGR02169 443 KEDKALEIK-------KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA----EAQARASEERVRGGRA 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1505 LQEEISDLTEqlGSSGkTIHELEKVRKQ------------LEAEKMELQSALEEAEASLEHEegKILRAQ-LEFNQIKAE 1571
Cdd:TIGR02169 512 VEEVLKASIQ--GVHG-TVAQLGSVGERyataievaagnrLNNVVVEDDAVAKEAIELLKRR--KAGRATfLPLNKMRDE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1572 --------------IERKLAEKDEEMEQAKRNHLR---VVDSLQT-----------SLDAE-----------TRSRNEAL 1612
Cdd:TIGR02169 587 rrdlsilsedgvigFAVDLVEFDPKYEPAFKYVFGdtlVVEDIEAarrlmgkyrmvTLEGElfeksgamtggSRAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1613 RVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVV 1692
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1693 EQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSqlQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKE 1772
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1773 QDTSAHLERMKKNMEQTIKDLQHRLDE-AEQIALKGGKK-----QLQKLEARVRELENELEAEQKRNAESVKGMRKSERR 1846
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSiEKEIENLNGKKeeleeELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034587182 1847 IKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSkFRKVQHELDEAEER 1909
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1074-1729 |
5.91e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.33 E-value: 5.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1074 QQLDERLKKKD-----FELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISE 1148
Cdd:COG1196 216 RELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1149 RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALrkkhadsvAELGEQIDNLQRVKQKLEKEKSEFKLEL 1228
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL--------EELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1229 DDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTrgklty 1308
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE------ 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1309 tQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEE 1388
Cdd:COG1196 442 -EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1389 AKKKLAQRLQEAEEAVEAVnakcsslektkhrLQNEIEDLMVDVERSNAAAAAldkKQRNFDKILAEWKQKYEESQSELE 1468
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAA-------------LEAALAAALQNIVVEDDEVAA---AAIEYLKAAKAGRATFLPLDKIRA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1469 SSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAE 1548
Cdd:COG1196 585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1549 ASLEHEEGKILRAQlefnqikAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQ 1628
Cdd:COG1196 665 GSRRELLAALLEAE-------AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1629 LShanrmaaeaqkqvkslqsLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEqtersrkLAEQELIE 1708
Cdd:COG1196 738 LE------------------ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNL-------LAIEEYEE 792
|
650 660
....*....|....*....|.
gi 1034587182 1709 TSERVQLLHSQNTSLINQKKK 1729
Cdd:COG1196 793 LEERYDFLSEQREDLEEARET 813
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1578 |
2.48e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 105.15 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 844 EREKEMAsmKEEFTRLKEALEKSEARRKELEEKMVSLLQEKND--------------------------------LQLQV 891
Cdd:TIGR02169 169 DRKKEKA--LEELEEVEENIERLDLIIDEKRQQLERLRREREKaeryqallkekreyegyellkekealerqkeaIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 892 QAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLED--EEEMNA------ELTAKKRKLEDECSELKRDIDDLELTLAK 963
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRvkekigELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 964 VEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKK 1043
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1044 VRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFE--------------LNALNARIEDEQALGSQLQKKLK 1109
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEikkqewkleqlaadLSKYEQELYDLKEEYDRVEKELS 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1110 ELQARIEELEEELEAERTA----RAKVEKLRSDLS------RELEEISER----LEEAGG----ATSVQIEMNKKREAEF 1171
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERvrggRAVEEVLKASIQgvhgtvAQLGSVGERyataIEVAAGnrlnNVVVEDDAVAKEAIEL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1172 QKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKeksEFKLELDDvTSNMEQIIKAKANLEKM-CR 1250
Cdd:TIGR02169 567 LKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEP---AFKYVFGD-TLVVEDIEAARRLMGKYrMV 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1251 TLEDQMNEhRSKA-----EETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGK---LTYTQQLEDLKRQLEEE 1322
Cdd:TIGR02169 643 TLEGELFE-KSGAmtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEI 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1323 VKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQwrtkYETDAIQRTEELEEAKKKLAQrlqeaeE 1402
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE----LEEDLHKLEEALNDLEARLSH------S 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1403 AVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELF 1482
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1483 KLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEgKILRAQ 1562
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-EIPEEE 950
|
810
....*....|....*.
gi 1034587182 1563 LEFNQIKAEIERKLAE 1578
Cdd:TIGR02169 951 LSLEDVQAELQRVEEE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
978-1860 |
1.81e-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: 102.45 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 978 LTEEMAGLDEIIAKLTKEKKALQEAHQQaLDDLQAEEDKVNtltkakvkleQQVDDLEGslEQEKKVR-MDLERAKRKLE 1056
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEEN-IERLDLIIDEKR----------QQLERLRR--EREKAERyQALLKEKREYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1057 GDLKLTQesIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEaeRTARAKVEKLR 1136
Cdd:TIGR02169 225 GYELLKE--KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ--LRVKEKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1137 SDLS---RELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATA---AALRKKHADSVAELGEQIDNL 1210
Cdd:TIGR02169 301 AEIAsleRSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTeeyAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1211 QRVKQKLekekSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEetqrsvnDLTSQRAKLQTENGELSRQ 1290
Cdd:TIGR02169 381 AETRDEL----KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA-------GIEAKINELEEEKEDKALE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1291 LDEKEALISQLTRGKLTYTQQLEDLK---RQLEEEV-KAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKAnS 1366
Cdd:TIGR02169 450 IKKQEWKLEQLAADLSKYEQELYDLKeeyDRVEKELsKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTV-A 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1367 EVAQWRTKYETdaiqrteELEEAkkkLAQRLQEAEEAVEAVNAKCSSLEKTKH--RLQ----NEIEDLMVDVERSNAAAA 1440
Cdd:TIGR02169 529 QLGSVGERYAT-------AIEVA---AGNRLNNVVVEDDAVAKEAIELLKRRKagRATflplNKMRDERRDLSILSEDGV 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1441 A--------LDKKQRN-----------FDKILAEWKQ-------------------------KYEESQSELESSQKEARS 1476
Cdd:TIGR02169 599 IgfavdlveFDPKYEPafkyvfgdtlvVEDIEAARRLmgkyrmvtlegelfeksgamtggsrAPRGGILFSRSEPAELQR 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1477 LSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVR-------KQLEAEKMELQSALEEAEA 1549
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEeklkerlEELEEDLSSLEQEIENVKS 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1550 SLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDslqtsldaETRSRNEALrvkkkmegdLNEMEIQL 1629
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE--------EEVSRIEAR---------LREIEQKL 821
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1630 SHANRMAAEAQKQVKSLQSLlkdtqiqlddavraNDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIET 1709
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQ--------------RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1710 SErvqllhsqntslinQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKkeqdtsaHLERMKKNMEQt 1789
Cdd:TIGR02169 888 KK--------------ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS-------EIEDPKGEDEE- 945
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1790 ikdlqhrlDEAEQIALKGGKKQLQKLEARVRELE-------NELEAEQKRNAESVKGMRK--SERR-IKELTYQTEEDRK 1859
Cdd:TIGR02169 946 --------IPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKleEERKaILERIEEYEKKKR 1017
|
.
gi 1034587182 1860 N 1860
Cdd:TIGR02169 1018 E 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
841-1512 |
3.33e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 101.67 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKM-------VSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKI 913
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLetlrskvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 914 QL-----EAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKV---KNLTEEMAGL 985
Cdd:TIGR02168 425 ELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQENLEGF 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 986 DEIIAKLTKEKKALQEAHQQALDDLQAEED---KVNT-----LTKAKVKLEQQVDDLEGSLEQEKKVRMDL-------ER 1050
Cdd:TIGR02168 505 SEGVKALLKNQSGLSGILGVLSELISVDEGyeaAIEAalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFlpldsikGT 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1051 AKRKLEGDLKLTQESIMDLENDKQQLDERLKK------------KDFElNALNARIE----------------------- 1095
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggvlvvDDLD-NALELAKKlrpgyrivtldgdlvrpggvitg 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1096 -DEQALGSQLQKK--LKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnkkrEAEFQ 1172
Cdd:TIGR02168 664 gSAKTNSSILERRreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL--------------SRQIS 729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1173 KMRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTL 1252
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1253 EDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHA 1332
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1333 LQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCS 1412
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1413 SLEKTKHRLQNEIEDLmvdverSNAAAAALDKkqrnfdkiLAEWKQKYEESQselessqKEARSLSTELFKLKNAYEE-- 1490
Cdd:TIGR02168 969 EARRRLKRLENKIKEL------GPVNLAAIEE--------YEELKERYDFLT-------AQKEDLTEAKETLEEAIEEid 1027
|
730 740
....*....|....*....|....*
gi 1034587182 1491 ---SLEHLETFKRENKNLQEEISDL 1512
Cdd:TIGR02168 1028 reaRERFKDTFDQVNENFQRVFPKL 1052
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
917-1793 |
1.18e-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: 99.76 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 917 AKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRdIDDLELTLAKVE-----KEKHATENKVKNLTEEMAGLDEIIAK 991
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 992 LTKEKKALQEAHQQALDDLQAEEDKVNTLTKAK-VKLEQQVDDLEGSLEQekkvrmdlerakrkLEGDLKLTQESIMDLE 1070
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAEIAS--------------LERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1071 NDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERL 1150
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1151 EEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHAdsvaelgeqidnlqrvkqKLEKEKSEFKLELDD 1230
Cdd:TIGR02169 402 NEL-----------KRELDRLQEELQRLSEELADLNAAIAGIEAKIN------------------ELEEEKEDKALEIKK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1231 VTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEA-------LISQLTR 1303
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1304 GKLTYTQQLEDLKRQ------LEEEVKAKNA--LAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKY 1375
Cdd:TIGR02169 533 VGERYATAIEVAAGNrlnnvvVEDDAVAKEAieLLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1376 ETD---AIQRT---EELEEAKK--------KLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAA 1441
Cdd:TIGR02169 613 EPAfkyVFGDTlvvEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1442 LDKKQRNFDKILAEWKQKyeesqselessqkeARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGK 1521
Cdd:TIGR02169 693 LQSELRRIENRLDELSQE--------------LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1522 TIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEF-NQIKAEIERKLAEKDeemeqAKRNHLRVVDSLQTS 1600
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKlEEEVSRIEARLREIE-----QKLNRLTLEKEYLEK 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1601 LDAETRSRNEALRVKKKMEGD-LNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDavranddlkeniaiverrnn 1679
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKeIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE-------------------- 893
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1680 lLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKM------DADLSQLQTEVEEAVQECRNAEE 1753
Cdd:TIGR02169 894 -LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipeeELSLEDVQAELQRVEEEIRALEP 972
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 1034587182 1754 KAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDL 1793
Cdd:TIGR02169 973 VNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1286-1828 |
6.16e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.31 E-value: 6.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1286 ELSRQLDEKEALISQLTRGKLTytQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKAN 1365
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELE--AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1366 SEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKK 1445
Cdd:COG1196 295 AELAR--------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1446 QRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHE 1525
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1526 LEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEM---EQAKRNHLR---------- 1592
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflEGVKAALLLaglrglagav 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1593 -VVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEI-------QLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRAN 1664
Cdd:COG1196 527 aVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAieylkaaKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1665 DDLKENIAIVERRNNLLQAELEELRA--------VVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQ 1736
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLeaalrravTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1737 LQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLE 1816
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
570
....*....|....*
gi 1034587182 1817 ---ARvreLENELEA 1828
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 |
1.10e-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: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 220 IIQANPALEAFGNAKTVRNDNSSRFGKF--IRIHFGATG---KLASADIETYLLEKSRVIFQL------KAERDYHIFYQ 288
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 289 ILSNKKPELLDMLLITNNPYD------YAFISQGETTVASIDDAEELMATD--------NAFDVLGFTSEEKNSMYKLTG 354
Cdd:cd14894 329 MVAGVNAFPFMRLLAKELHLDgidcsaLTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 355 AIMHFGNMKFKLKQREEQAEPDGT---EEADKSAYLMGLNSADLLKGLCHPR---VKVGNEYVTKGQNVQQVIYATGALA 428
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 429 KAVYERMFNWMV------TRINATLETKQPRQY-----------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLqqffnh 491
Cdd:cd14894 489 RLLYQLAFNYVVfvmneaTKMSALSTDGNKHQMdsnasapeavsLLKIVDVFGFEDLTHNSLDQLCINYLSEKL------ 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 492 hmFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTF-----KAKLFDNHL--GKSANFQ 564
Cdd:cd14894 563 --YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIydRNSSRLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 565 KPRNIKGKPEAH---------FSLIHYAGIVDYNIIGWLQKNKDPL-NETVVGLYQKSSLKLLSTLFANYAGADAPIEKG 634
Cdd:cd14894 641 EPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLNESSQLGWSPNTNR 720
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034587182 635 KGKAKKGSSFQTVSAL---HRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICR 706
Cdd:cd14894 721 SMLGSAESRLSGTKSFvgqFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
847-1589 |
2.82e-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: 95.13 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 847 KEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERL 926
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 927 EDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAhqqa 1006
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE---- 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1007 lddLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLK----- 1081
Cdd:TIGR02169 450 ---IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgt 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1082 -------KKDFEL-------NALNARIEDEQALGSQLQKKLKELQArieeleeeleaERTARAKVEKLRsDLSRELEEIS 1147
Cdd:TIGR02169 527 vaqlgsvGERYATaievaagNRLNNVVVEDDAVAKEAIELLKRRKA-----------GRATFLPLNKMR-DERRDLSILS 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1148 ErlEEAGGATSVQIEMNKKREAEFQKMRRD------LEEA----------TLQHE-------ATAAALRKKHADSVA-EL 1203
Cdd:TIGR02169 595 E--DGVIGFAVDLVEFDPKYEPAFKYVFGDtlvvedIEAArrlmgkyrmvTLEGElfeksgaMTGGSRAPRGGILFSrSE 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1204 GEQIDNLQRVKQKLEKEKSEFKLELddvtsnmeqiikakanlekmcRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTE 1283
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSEL---------------------RRIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1284 NGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQsarhdcDLLREQYEEETEakaELQRVLSK 1363
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN------DLEARLSHSRIP---EIQAELSK 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1364 ANSEVAQWRtkyetdaiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALD 1443
Cdd:TIGR02169 803 LEEEVSRIE--------ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1444 KKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKnlqeEISDLTEQLGSSGKTI 1523
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEEE 950
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034587182 1524 HELEKVRKQLEAEKMELQsALEEAE--ASLEHEEGKILRAQLEFNQIKAEIERK-LAEKDEEMEQAKRN 1589
Cdd:TIGR02169 951 LSLEDVQAELQRVEEEIR-ALEPVNmlAIQEYEEVLKRLDELKEKRAKLEEERKaILERIEEYEKKKRE 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
841-1435 |
5.14e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.82 E-value: 5.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSllQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIqlEAKVK 920
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE--EKKKADEAKKKAEEAKKADEAKKKAEEAKKKA--DAAKK 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 921 EMNERLEDEEEMNAELTAKKRKLEDecSELKRDIDDLEltlaKVEKEKHATENKVKnlTEEMAGLDEIIAKLTKEKKALQ 1000
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEA--AEEKAEAAEKK----KEEAKKKADAAKKK--AEEKKKADEAKKKAEEDKKKAD 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1001 EAHQQALDDLQAEEdkvntlTKAKVKLEQQVDDLEGSLEQEKKVrmdlERAKRKLEGDLKltqesimdLENDKQQLDERL 1080
Cdd:PTZ00121 1409 ELKKAAAAKKKADE------AKKKAEEKKKADEAKKKAEEAKKA----DEAKKKAEEAKK--------AEEAKKKAEEAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1081 KKKDFELNALNARIEDEqalgsqLQKKLKELQARIEELEEELEAERTA---RAKVEKLRSDLSRELEEiSERLEEAGGAT 1157
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADE------AKKKAEEAKKKADEAKKAAEAKKKAdeaKKAEEAKKADEAKKAEE-AKKADEAKKAE 1543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1158 SVQI--EMNKKREAEFQKMRRDLEEATLQHEATAAALRKkhadsvAELGEQIDNlQRVKQKLEKEKSEFKLELDDVTSNM 1235
Cdd:PTZ00121 1544 EKKKadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK------AEEAKKAEE-ARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1236 EQIIKAkanlekmcrtledqmnEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDL 1315
Cdd:PTZ00121 1617 EAKIKA----------------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1316 KRQLEEEVKAKNALAHALQSARhDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEEL---EEAKKK 1392
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEAkkdEEEKKK 1758
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1034587182 1393 LAQRLQEAEEAVEAVNAKCSSLekTKHRLQNEIEDLMVDVERS 1435
Cdd:PTZ00121 1759 IAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKK 1799
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
987-1801 |
6.41e-19 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 94.03 E-value: 6.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 987 EIIAKLTKE--KKALQEAHQQaLDDLQAEEDKVNTL-TKAKVKLEQQVDDLEGSLEQ---EKKVRMDLERAKRKLEGDLK 1060
Cdd:pfam15921 66 KIIAYPGKEhiERVLEEYSHQ-VKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1061 -LTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQAR-----IEELEEELEAERTARAKVEK 1134
Cdd:pfam15921 145 nQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEAsgkkiYEHDSMSTMHFRSLGSAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1135 LRSDLSRELEEISERLEEAGGA-TSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRV 1213
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQlEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1214 KQKLEKEKSEFKLELDDVTSNMEQIikaKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLde 1293
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLESTVSQL---RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL-- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1294 kEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHalqsarhdcdlLREQYEEETEAKAELQRVLSKANSEvAQWRT 1373
Cdd:pfam15921 380 -QKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDH-----------LRRELDDRNMEVQRLEALLKAMKSE-CQGQM 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1374 KYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLmvdversnaaAAALDKKQRNFDKIL 1453
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL----------TASLQEKERAIEATN 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1454 AEwkqkYEESQSELESSQKEARSLSTELFKLKNAYEESlEHLETFKRENKN----LQEEISDLTEQLGSSGKTIHELEKV 1529
Cdd:pfam15921 517 AE----ITKLRSRVDLKLQELQHLKNEGDHLRNVQTEC-EALKLQMAEKDKvieiLRQQIENMTQLVGQHGRTAGAMQVE 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1530 RKQLEAE----KMELQS---ALEEAEASLEHEEGKILRAQLE-FNQIKAEIERKLAEKDEEMEQAK-RNHLRVVDSLQTS 1600
Cdd:pfam15921 592 KAQLEKEindrRLELQEfkiLKDKKDAKIRELEARVSDLELEkVKLVNAGSERLRAVKDIKQERDQlLNEVKTSRNELNS 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1601 LDAETRSRNEALRVK-KKMEGDLNEMEIQLShanrmaaEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNN 1679
Cdd:pfam15921 672 LSEDYEVLKRNFRNKsEEMETTTNKLKMQLK-------SAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID 744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1680 LLQAELEELRAVVEQTERSRKLAEQELIETSERVqllhsqnTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAI 1759
Cdd:pfam15921 745 ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL-------STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 1034587182 1760 TDAAMMAEELKKEQDTSAHLErmkknmeqtikdLQHRLDEAE 1801
Cdd:pfam15921 818 LQFAECQDIIQRQEQESVRLK------------LQHTLDVKE 847
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1128-1907 |
7.04e-19 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 94.03 E-value: 7.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1128 ARAKVEKLRSDLSRELEEISERLEEAGgatsvqiEMNKKREAEFQK----MRRDLEEATLQHEATAAaLRKKHADSVAEL 1203
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESN-------ELHEKQKFYLRQsvidLQTKLQEMQMERDAMAD-IRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1204 GEQidnLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLED-----------QMNEHRSKAEETQRSVND 1272
Cdd:pfam15921 144 RNQ---LQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSilvdfeeasgkKIYEHDSMSTMHFRSLGS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1273 LTSQRAK-LQTENGELSRQL----DEKEALISQLTRGKLTYTQQLEDLKRQL--EEEVKAkNALAHALQSARHDCDLLRE 1345
Cdd:pfam15921 221 AISKILReLDTEISYLKGRIfpveDQLEALKSESQNKIELLLQQHQDRIEQLisEHEVEI-TGLTEKASSARSQANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1346 QYE----EETEAKAELQRVLSKANSEVAQWRTkyetdaiqrteELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHR- 1420
Cdd:pfam15921 300 QLEiiqeQARNQNSMYMRQLSDLESTVSQLRS-----------ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQf 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1421 ------LQNEIEDLMVDV-ERSNAAAAALDKKQRNFDKILAEwKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLE 1493
Cdd:pfam15921 369 sqesgnLDDQLQKLLADLhKREKELSLEKEQNKRLWDRDTGN-SITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQME 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1494 -HLETFKRENKNLqEEISDLTEQLGSsgkTIHELEKVRKQLEAEKMELQSA---LEEAEASLEHEEGKILRAQLEFNQIK 1569
Cdd:pfam15921 448 rQMAAIQGKNESL-EKVSSLTAQLES---TKEMLRKVVEELTAKKMTLESSertVSDLTASLQEKERAIEATNAEITKLR 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1570 AEIERKLaekdEEMEQAKR--NHLRVVdslQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQ 1647
Cdd:pfam15921 524 SRVDLKL----QELQHLKNegDHLRNV---QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLE 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1648 SLLKDTQIQLDDAVRANDdlKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQElietSERVQLLHSQNTSLiNQK 1727
Cdd:pfam15921 597 KEINDRRLELQEFKILKD--KKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIK----QERDQLLNEVKTSR-NEL 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1728 KKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEE----LKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAE-- 1801
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQtrntLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQsk 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1802 ----QIALKGGKKQLQKLEARVRELENELEA---EQKRNAESVKGMRKSERRIKEltyqteedrkNLLRLQDLVDKLQLK 1874
Cdd:pfam15921 750 iqflEEAMTNANKEKHFLKEEKNKLSQELSTvatEKNKMAGELEVLRSQERRLKE----------KVANMEVALDKASLQ 819
|
810 820 830
....*....|....*....|....*....|...
gi 1034587182 1875 VkAYKRQAEEAEEQANTNLskfrKVQHELDEAE 1907
Cdd:pfam15921 820 F-AECQDIIQRQEQESVRL----KLQHTLDVKE 847
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
845-1525 |
7.20e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.44 E-value: 7.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 845 REKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQleaKVKEMNE 924
Cdd:PTZ00121 1158 RKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAE---AVKKAEE 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 925 RLEDEEEmnAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNlTEEMAGLDEiiAKLTKEKKALQEAHQ 1004
Cdd:PTZ00121 1235 AKKDAEE--AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADE--AKKAEEKKKADEAKK 1309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1005 QALDDLQAEEDKVNT------LTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDE 1078
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAeeakkkADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1079 RLKKKDfelnaLNARIEDEQALGSQLQKKLKElqaRIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATS 1158
Cdd:PTZ00121 1390 KKKADE-----AKKKAEEDKKKADELKKAAAA---KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEE 1461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1159 VQIEMNKKREAEfqKMRRDLEEATLQHEATAAALR-KKHADSVAELGEQIDNLQRVKQKLEKEKSEfKLELDDVTSNMEQ 1237
Cdd:PTZ00121 1462 AKKKAEEAKKAD--EAKKKAEEAKKADEAKKKAEEaKKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEEAKKADE 1538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1238 IIKA--KANLEKMCRTLEDQMNEHRSKAEETQRSvndltSQRAKLQTENGELSRQLDEKEaLISQLTRGKLTYTQQLEDL 1315
Cdd:PTZ00121 1539 AKKAeeKKKADELKKAEELKKAEEKKKAEEAKKA-----EEDKNMALRKAEEAKKAEEAR-IEEVMKLYEEEKKMKAEEA 1612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1316 KRQLEEEVKAKNalAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEEL----EEAKK 1391
Cdd:PTZ00121 1613 KKAEEAKIKAEE--LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaeEDEKK 1689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1392 KLAQRLQEAEEA--VEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSnaaaaaldKKQRNFDKILAEWKQKYEESQSELES 1469
Cdd:PTZ00121 1690 AAEALKKEAEEAkkAEELKKKEAEEKKKAEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587182 1470 SQKEARSLSTELFKLKNAYEEslehlETFKRENKNLQEEISDLTEQLGSSGKTIHE 1525
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
870-1425 |
1.84e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 92.41 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 870 RKELEEKmvsllqEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTakkrkledecsE 949
Cdd:PRK02224 193 KAQIEEK------EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE-----------T 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 950 LKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKE---KKALQEAHQQALDDLQAEEDKV-NTLTKAKV 1025
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglDDADAEAVEARREELEDRDEELrDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1026 KLEQQVDDLEGSLEQEKKVRmdlERAKRK------LEGDLKLTQESIMDLENDKQQLDErlkkkdfELNALNARIEDEQA 1099
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLE---ERAEELreeaaeLESELEEAREAVEDRREEIEELEE-------EIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1100 LGSQLQKKLKELQARIEEleeeleaertARAKVEKLRSDLSRELEEISE--RLEEAGG--------ATSVQIEMNKKREA 1169
Cdd:PRK02224 406 DLGNAEDFLEELREERDE----------LREREAELEATLRTARERVEEaeALLEAGKcpecgqpvEGSPHVETIEEDRE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1170 EFQKMRRDLEEATLQHEATAAALRKkhADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMC 1249
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLER--AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1250 RTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSR---QLDEKEALISQLT--RGKLTYTQQLEDLKR-QLEEEV 1323
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtLLAAIADAEDEIErlREKREALAELNDERReRLAEKR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1324 KAKNALAHALQSARhdcdllreqYEEETEAKAELQRVLSKANSEVAQWRTkyETDAIQRT--------EELEEAKKKLAQ 1395
Cdd:PRK02224 634 ERKRELEAEFDEAR---------IEEAREDKERAEEYLEQVEEKLDELRE--ERDDLQAEigavenelEELEELRERREA 702
|
570 580 590
....*....|....*....|....*....|
gi 1034587182 1396 rLQEAEEAVEAVNAKCSSLEKTKHRLQNEI 1425
Cdd:PRK02224 703 -LENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1077-1883 |
3.17e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.13 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1077 DERLK--KKDFELNALNARIEDEQAlgSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAG 1154
Cdd:PTZ00121 1069 DEGLKpsYKDFDFDAKEDNRADEAT--EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR 1146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1155 GATSVQIEMNKKREAEFQKMR--RDLEEATLQHEA-TAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEfKLELDDV 1231
Cdd:PTZ00121 1147 KAEDAKRVEIARKAEDARKAEeaRKAEDAKKAEAArKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKK 1225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1232 TSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSvnDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQ 1311
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA--HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1312 LEDLKRQLEEEVKAKNALAHAlQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRteelEEAKK 1391
Cdd:PTZ00121 1304 ADEAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK----EEAKK 1378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1392 KLAQRLQEAEEAVEAVNAKCSSLEktkhrlqneiedlmvdversnaaaaalDKKQRNFDKILAEWKQKyEESQSELESSQ 1471
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEAKKKAEE---------------------------DKKKADELKKAAAAKKK-ADEAKKKAEEK 1430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1472 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASL 1551
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1552 EHEEGKilRAQlefNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEmeiqlsh 1631
Cdd:PTZ00121 1511 KADEAK--KAE---EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM------- 1578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1632 ANRMAAEAQKQVKSlqsllkdtqiQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSE 1711
Cdd:PTZ00121 1579 ALRKAEEAKKAEEA----------RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1712 RVQLLHSQNTSLINQkkkmdADLSQLQTEVEEAVQECRNAEEKAKKAitdaammAEELKKEQDTSAHLERMKKNMEQTIK 1791
Cdd:PTZ00121 1649 AEELKKAEEENKIKA-----AEEAKKAEEDKKKAEEAKKAEEDEKKA-------AEALKKEAEEAKKAEELKKKEAEEKK 1716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1792 dlqhrldEAEQIalkggKKQLQKLEARVRELENELEaEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKL 1871
Cdd:PTZ00121 1717 -------KAEEL-----KKAEEENKIKAEEAKKEAE-EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
810
....*....|..
gi 1034587182 1872 QLKVKAYKRQAE 1883
Cdd:PTZ00121 1784 ELDEEDEKRRME 1795
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1253-1927 |
3.48e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 91.78 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1253 EDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLD-------EKEALISQLTRGKLTYTQQLEDLKRQLEEEVKA 1325
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1326 KNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEeLEEAKKKLAQRLQEAEEAVE 1405
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK-LSKERKLLEERISEFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1406 AVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLK 1485
Cdd:pfam01576 170 EEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1486 NAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEF 1565
Cdd:pfam01576 250 ARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1566 NQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKS 1645
Cdd:pfam01576 330 TELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1646 LQSLLKDTQIQLDDAVRANDDLKEniaiverRNNLLQAELEELRAVVEQTE-RSRKLA------EQELIETSERVQLLHS 1718
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAE-------KLSKLQSELESVSSLLNEAEgKNIKLSkdvsslESQLQDTQELLQEETR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1719 QNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLD 1798
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1799 EAEQIALKggkkqLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTyqtEEDRKNLLRLQDLVDKlqlkvkay 1878
Cdd:pfam01576 563 EKAAAYDK-----LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQML---AEEKAISARYAEERDR-------- 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1034587182 1879 krqaeeAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1927
Cdd:pfam01576 627 ------AEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDL 669
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1230-1911 |
8.06e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.97 E-value: 8.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1230 DVTSNMEQIIKAKANLEKMcRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQ----TENGELSRQLDEKEALISQLTRGK 1305
Cdd:PTZ00121 1051 DIDGNHEGKAEAKAHVGQD-EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEeakkTETGKAEEARKAEEAKKKAEDARK 1129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1306 LTYTQQLEDLkRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQR--VLSKANSEVAQWRTKYETDAIQRT 1383
Cdd:PTZ00121 1130 AEEARKAEDA-RKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARkaEEVRKAEELRKAEDARKAEAARKA 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1384 EE---LEEAKK----KLAQRLQEAEEA-VEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAE 1455
Cdd:PTZ00121 1209 EEerkAEEARKaedaKKAEAVKKAEEAkKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1456 WKQKYEESQSELESSQKEARSLSTELFK---LKNAYEESLEHLETFKR--ENKNLQEEISDLTEQlgssgKTIHELEKVR 1530
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAKKKAEEAKKadeAKKKAEEAKKKADAAKKkaEEAKKAAEAAKAEAE-----AAADEAEAAE 1363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1531 KQLEAEKMELQSALEEAEASLEHEEGKI----LRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETR 1606
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKkadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA 1443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1607 SRNEALRvKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLlKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAE-- 1684
Cdd:PTZ00121 1444 KKADEAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEea 1521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1685 --LEELRAVvEQTERSRKLAEQELIETSERV----QLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQ-ECRNAEEKAKK 1757
Cdd:PTZ00121 1522 kkADEAKKA-EEAKKADEAKKAEEKKKADELkkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKL 1600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1758 AITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQI-----------ALKGGKKQLQKLEARVRELENEL 1826
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkaeelkkaeeENKIKAAEEAKKAEEDKKKAEEA 1680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1827 ---EAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAE---EQANTNLSKFRKVQ 1900
Cdd:PTZ00121 1681 kkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIA 1760
|
730
....*....|.
gi 1034587182 1901 HELDEAEERAD 1911
Cdd:PTZ00121 1761 HLKKEEEKKAE 1771
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
843-1455 |
2.14e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.97 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 843 AEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM 922
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 923 NERLE-------DEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKE 995
Cdd:TIGR02169 454 EWKLEqlaadlsKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSV 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 996 KKALQEAHQQAL----------DDLQAEED--------------------KVNTLTKAKVKLEQQVDDLEGSLEQEKKVR 1045
Cdd:TIGR02169 534 GERYATAIEVAAgnrlnnvvveDDAVAKEAiellkrrkagratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPKYE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1046 -------------MDLERAKR--------KLEGDL--------------KLTQESIMDLENDKQQLDERLKKKDFELNAL 1090
Cdd:TIGR02169 614 pafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGELfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1091 NARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnkkrEAE 1170
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV--------------KSE 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1171 FQKMRRDLEEatlqHEATAAALRKKHADSVAELG-EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMC 1249
Cdd:TIGR02169 760 LKELEARIEE----LEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1250 RTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEevkaknaL 1329
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-------L 908
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1330 AHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNA 1409
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE--ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 1410 KCSSLEKTKHRLQNEIEDL-----MVDVERSNAAAAALDKKQRNFDKILAE 1455
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
931-1785 |
3.56e-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: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 931 EMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDL 1010
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1011 QAEEDKVNTLTKAKVKLEQQvddlegSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNAL 1090
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEE------KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1091 NARIEdeqalgsQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAE 1170
Cdd:pfam02463 320 EKEKK-------KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1171 FQKM----------RRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIK 1240
Cdd:pfam02463 393 KEEElelkseeekeAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1241 AKANLEKMCRTLEDQMNEHRSKAEEtqrsvnDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLE 1320
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEE------RSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1321 EEVKAKNALAHAlqsarhDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEA 1400
Cdd:pfam02463 547 TAVIVEVSATAD------EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1401 EEAVEAVNAKCSSLEKTKHRLQNEIEDLM--VDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLS 1478
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRkgVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1479 TELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKI 1558
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1559 LRAQLEFNQIKAEIERKLAEKDEEMEQAKRNH----LRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQlsHANR 1634
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEeaelLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE--ELER 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1635 MAAEAQKQVKSLQSLLKDTQIQLDDAVRanddlkENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQ 1714
Cdd:pfam02463 859 LEEEITKEELLQELLLKEEELEEQKLKD------ELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLK 932
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 1715 LLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKN 1785
Cdd:pfam02463 933 YEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
858-1573 |
5.92e-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: 87.38 E-value: 5.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 858 RLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLiKNKIQ-LEAKVKEMNERLEDEEEMNAEL 936
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNS-NNKIKiLEQQIKDLNDKLKKNKDKINKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 937 TAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATE-------NKVKNLTEEMAGLDEIIAKLTKEKKALqeahqqaldd 1009
Cdd:TIGR04523 102 NSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEEL---------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1010 lqaeEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLErakrKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNA 1089
Cdd:TIGR04523 172 ----ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1090 LNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEaggatsvqiEMNKKREA 1169
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ---------DWNKELKS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1170 EFQKMRRDLEEATLQheataaalRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMC 1249
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQ--------ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1250 RTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLtrgkltyTQQLEDLKRQLEEEVKAKNAL 1329
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN-------NSEIKDLTNQDSVKELIIKNL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1330 AHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQEAEEAVEAVNA 1409
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL---------------KKLNEEKKELEEKVKDLTKKISSLKE 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1410 KCSSLEKTKHRLQNEIEDLMVDVER--SNAAAAALDKKQRNFDKILAEWKQKYEesqselessqkearslstelfKLKNA 1487
Cdd:TIGR04523 525 KIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQK---------------------SLKKK 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1488 YEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQ 1567
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPE 663
|
....*.
gi 1034587182 1568 IKAEIE 1573
Cdd:TIGR04523 664 IIKKIK 669
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
854-1729 |
1.49e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 86.56 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 854 EEFTRLKEALEKsearRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERcdQLIKNKIQLEAKVKEMNERLEDEEEMN 933
Cdd:pfam02463 166 RLKRKKKEALKK----LIEETENLAELIIDLEELKLQELKLKEQAKKALEY--YQLKEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 934 AELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAE 1013
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1014 EDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEgdlkltqesiMDLENDKQQLDERLKKKDFELNALNAR 1093
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE----------KLQEKLEQLEEELLAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1094 IEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQK 1173
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1174 MRRDLEEATLQHEATAAALRkkhadsvaelgEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLE 1253
Cdd:pfam02463 470 SEDLLKETQLVKLQEQLELL-----------LSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAV 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1254 DQMNEHRSKAEETQRS-VNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHA 1332
Cdd:pfam02463 539 ENYKVAISTAVIVEVSaTADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADED 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1333 LQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDaiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCS 1412
Cdd:pfam02463 619 DKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV--KASLSELTKELLEIQELQEKAESELAKEEILR 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1413 SLEKTKHRLQNEIEDL-MVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNaYEES 1491
Cdd:pfam02463 697 RQLEIKKKEQREKEELkKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL-KEKE 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1492 LEHLETFKRENKNLQEEISDLTEQLGSsgktihELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAE 1571
Cdd:pfam02463 776 LAEEREKTEKLKVEEEKEEKLKAQEEE------LRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1572 IERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLShanRMAAEAQKQVKSLQSLLK 1651
Cdd:pfam02463 850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK---LNLLEEKENEIEERIKEE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1652 DTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQ--ELIETSERVQLLHSQNTSLINQKKK 1729
Cdd:pfam02463 927 AEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAieEFEEKEERYNKDELEKERLEEEKKK 1006
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
972-1654 |
3.00e-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: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 972 ENKVKNLTEEMAGLDEIIAKLTKEKKALQEahqqalDDLQAEEDKVNTLTKAKvKLEQQVDDLEGSLEQEKKVRMDLERA 1051
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDK------NLNKDEEKINNSNNKIK-ILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1052 KRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAK 1131
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1132 VEKLRSDLSRELEEISERLeeaggatsVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQ 1211
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLL--------SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1212 RVKQKLEKEKSEfkleLDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEetQRSVNDLTSQRAKLQTENGELSRQL 1291
Cdd:TIGR04523 257 QLKDEQNKIKKQ----LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1292 DEKEALISQLTrgkltytQQLEDLKRQLEEEVKAKNalahalqsarhdcdllrEQYEEETEAKAELQRVLSKANSEvaqw 1371
Cdd:TIGR04523 331 SQNNKIISQLN-------EQISQLKKELTNSESENS-----------------EKQRELEEKQNEIEKLKKENQSY---- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1372 rtkyetdaIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDK 1451
Cdd:TIGR04523 383 --------KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1452 ILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRK 1531
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1532 QLEAEKMELQSALEEaeasleheegkilraqLEFNQIKAEIERKLAEKDEEMEQAKRNhlrvvdslQTSLDAETRSRNEA 1611
Cdd:TIGR04523 535 EKESKISDLEDELNK----------------DDFELKKENLEKEIDEKNKEIEELKQT--------QKSLKKKQEEKQEL 590
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1034587182 1612 LRVKKKMEGDLN----EMEIQLSHANRMAAEAQKQVKSLQSLLKDTQ 1654
Cdd:TIGR04523 591 IDQKEKEKKDLIkeieEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1270-1927 |
1.05e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.58 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1270 VNDLTSQRAKLQTENGELSRQLDEKEALISQLTrgkltytQQLEDLKRQLEEEVKAKN-----------ALAHALQSARH 1338
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKR-------QQLERLRREREKAERYQAllkekreyegyELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1339 DCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTK 1418
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1419 HRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETF 1498
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1499 KRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIER---K 1575
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDlkeE 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1576 LAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEG------DLNEME------IQLSHANRM-------- 1635
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGvhgtvaQLGSVGeryataIEVAAGNRLnnvvvedd 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1636 --AAEAQKQVKS-------------LQSLLKDTQIQLDDAVRAN-------DDLKENIAIVERRNNLLQAELEELRAVVE 1693
Cdd:TIGR02169 558 avAKEAIELLKRrkagratflplnkMRDERRDLSILSEDGVIGFavdlvefDPKYEPAFKYVFGDTLVVEDIEAARRLMG 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1694 Q----------------------TERSRKL----AEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQE 1747
Cdd:TIGR02169 638 KyrmvtlegelfeksgamtggsrAPRGGILfsrsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1748 CRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEAR-----VREL 1822
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE-DLHKLEEALNDLEARlshsrIPEI 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1823 ENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHE 1902
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
730 740
....*....|....*....|....*
gi 1034587182 1903 LDEAEERADIAESQVNKLRAKSRDI 1927
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLREL 901
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1258-1840 |
1.08e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.17 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1258 EHRSKAEETQRSVNDLTSQRaklQTENGELSRQLDEKEA--LISQLTRgkltytqqLEDLKRQLEEEVKAKNALAHALQS 1335
Cdd:PRK02224 166 EYRERASDARLGVERVLSDQ---RGSLDQLKAQIEEKEEkdLHERLNG--------LESELAELDEEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1336 ARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYET------DAIQRTEELEEAKKKLAQRLQEAEEAVEAVNA 1409
Cdd:PRK02224 235 TRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREElaeevrDLRERLEELEEERDDLLAEAGLDDADAEAVEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1410 KCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQkyeesqselessqkEARSLSTELfklknayE 1489
Cdd:PRK02224 315 RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE--------------EAAELESEL-------E 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1490 ESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIK 1569
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1570 -----------------AEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDA-ETRSRNEALRVKKKMEGDL-NEMEIQLS 1630
Cdd:PRK02224 454 cpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDLvEAEDRIERLEERREDLEELiAERRETIE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1631 HANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERsRKLAEQELIETS 1710
Cdd:PRK02224 534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLR 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1711 ERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEA-VQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQT 1789
Cdd:PRK02224 613 EKREALAELNDERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1034587182 1790 IKDLQHRLDeaeqiALKGGKKQLQKLEARVRELEN---ELEAE-QKRNAESVKGM 1840
Cdd:PRK02224 693 LEELRERRE-----ALENRVEALEALYDEAEELESmygDLRAElRQRNVETLERM 742
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1174-1871 |
1.08e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 83.43 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1174 MRRDLEEATLQHEATAAAlrKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDvtsnmEQIIKAKANLEKmcrtLE 1253
Cdd:COG4913 240 AHEALEDAREQIELLEPI--RELAERYAAARERLAELEYLRAALRLWFAQRRLELLE-----AELEELRAELAR----LE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1254 DQMNEHRSKAEETQRSVNDLTSQRAKLQTEN-GELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHA 1332
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1333 LQSARHDCDLLREQYEEeteAKAELQRVLSKANSEVAQWRTkyETDAIQRT-----EELEEAKKKLAQRLQEAEEAVEAV 1407
Cdd:COG4913 389 AAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEA--EIASLERRksnipARLLALRDALAEALGLDEAELPFV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1408 nakCSSLE-KTKHRL-QNEIE--------DLMVDVERSNAAAAALDK---KQR-NFDKIlaewkqkyEESQSELESSQKE 1473
Cdd:COG4913 464 ---GELIEvRPEEERwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPRLD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1474 ARSLSTELFKLKNAYEESLEHL-------------ETFKRENKNLQEE--ISDLTE--------------QLGSSGKT-I 1523
Cdd:COG4913 533 PDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRAITRAgqVKGNGTrhekddrrrirsryVLGFDNRAkL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1524 HELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILR----AQLEFNQIK-AEIERKLAEKDEEMEQAKRNHlRVVDSLQ 1598
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEIDvASAEREIAELEAELERLDASS-DDLAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1599 TSLDAetrsrnealrvkkkMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAvranddlkeniaiVERRN 1678
Cdd:COG4913 692 EQLEE--------------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA-------------EDLAR 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1679 NLLQAELEELRAVVEQTERSRKLAEQelietservqllhsqntsLINQKKKMDADLSQLQTEVEEAVQE-CRNAEEKAKK 1757
Cdd:COG4913 745 LELRALLEERFAAALGDAVERELREN------------------LEERIDALRARLNRAEEELERAMRAfNREWPAETAD 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1758 AITDAAMMAEELK-----KEQDTSAHLERMK----KNMEQTIKDLQHRLDEAEQIAlkggKKQLQKLEARVRELE-NE-- 1825
Cdd:COG4913 807 LDADLESLPEYLAlldrlEEDGLPEYEERFKellnENSIEFVADLLSKLRRAIREI----KERIDPLNDSLKRIPfGPgr 882
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 1826 ---LEAEQKRNAEsVKGMRKSERRIKELTYQTEED--RKNLLRLQDLVDKL 1871
Cdd:COG4913 883 ylrLEARPRPDPE-VREFRQELRAVTSGASLFDEElsEARFAALKRLIERL 932
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1484-1926 |
2.29e-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: 82.47 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1484 LKNAYEESLEHLETfkreNKNLQEEIsdlteqLGSSGKTIHELEKVRKQLEAEKMELQSAL---EEAEASLEHEEGKIlr 1560
Cdd:pfam15921 143 LRNQLQNTVHELEA----AKCLKEDM------LEDSNTQIEQLRKMMLSHEGVLQEIRSILvdfEEASGKKIYEHDSM-- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1561 AQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTsLDAETRSRNEAL--RVKKKMEGDLNEMEIQLSHANRMAAE 1638
Cdd:pfam15921 211 STMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEA-LKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1639 AQKQVKSLQSLLKDTQIQlddavranddlkeniaiVERRNNLLQAELEELRAVVEQTE---RSRKLAEQELIETSERVQL 1715
Cdd:pfam15921 290 ARSQANSIQSQLEIIQEQ-----------------ARNQNSMYMRQLSDLESTVSQLRselREAKRMYEDKIEELEKQLV 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1716 LhsqntslinqkkkMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQH 1795
Cdd:pfam15921 353 L-------------ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRR 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1796 RLDEAEQialkggkkQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKV 1875
Cdd:pfam15921 420 ELDDRNM--------EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1876 KAYKR----------QAEEAEEQANTNLSKFR--------KVQHELDEAEERADI-AESQVNKLRAKSRD 1926
Cdd:pfam15921 492 ESSERtvsdltaslqEKERAIEATNAEITKLRsrvdlklqELQHLKNEGDHLRNVqTECEALKLQMAEKD 561
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
845-1580 |
3.47e-15 |
|
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: 82.02 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 845 REKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLadaeeRCDQLIKNKIQLEAKVKEMNE 924
Cdd:TIGR00606 310 HQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHI-----RARDSLIQSLATRLELDGFER 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 925 RLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQ 1004
Cdd:TIGR00606 385 GPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1005 QALDDLQAEEDKVNTLTKAKVKLEQ-----QVDDLEGSLEQEKKVRMDLERAKRKLEGDL------KLTQESIMDLENDK 1073
Cdd:TIGR00606 465 QLEGSSDRILELDQELRKAERELSKaeknsLTETLKKEVKSLQNEKADLDRKLRKLDQEMeqlnhhTTTRTQMEMLTKDK 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1074 QQLDERLKKKDF----ELNALNARIEDEQALGSQLQKKLKE---LQARIEELEEELEAERTARAKVEKLRSDLSRELEEI 1146
Cdd:TIGR00606 545 MDKDEQIRKIKSrhsdELTSLLGYFPNKKQLEDWLHSKSKEinqTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1147 SERLEEAGGATSVQIEMNKKREaEFQKMRRDLE-------------EATLQHEATAAALRKKHADSVAELGEQIDNLQRV 1213
Cdd:TIGR00606 625 EDKLFDVCGSQDEESDLERLKE-EIEKSSKQRAmlagatavysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSK 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1214 KQKLEKEKSEFKLELDDVTSNMEQII---KAKAN-LEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSR 1289
Cdd:TIGR00606 704 LRLAPDKLKSTESELKKKEKRRDEMLglaPGRQSiIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEES 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1290 QLDEK------EALISQLTRGKLTYTQQLE-----DLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQ 1358
Cdd:TIGR00606 784 AKVCLtdvtimERFQMELKDVERKIAQQAAklqgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLK 863
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1359 RVLSKANSEVAQWRTkyetdAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAA 1438
Cdd:TIGR00606 864 SKTNELKSEKLQIGT-----NLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK 938
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1439 AA-ALDKKQRNFDKILAEWK--QKYEESQSELESSQKEarslsTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQ 1515
Cdd:TIGR00606 939 AQdKVNDIKEKVKNIHGYMKdiENKIQDGKDDYLKQKE-----TELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQ 1013
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1516 ---------LGSSGKTIHELEKVRKQLEAEKMELQ--------SALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAE 1578
Cdd:TIGR00606 1014 erwlqdnltLRKRENELKEVEEELKQHLKEMGQMQvlqmkqehQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
..
gi 1034587182 1579 KD 1580
Cdd:TIGR00606 1094 PQ 1095
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
840-1401 |
4.40e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 81.70 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 840 LKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNladAEERCDQLIKNKIQLEAKV 919
Cdd:pfam15921 250 LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 920 kemnerledeEEMNAELTAKKRKLEDECSELKRD--IDDLELTLAKVEKEKHATENkvKNLTEEmagLDEIIAKLTKEKK 997
Cdd:pfam15921 327 ----------SQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQ---LQKLLADLHKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 998 ALQEAHQQ--------------------ALDDLQAEEDKVNTLTKA-----KVKLEQQVDDLEG---SLEQEKKVRMDLE 1049
Cdd:pfam15921 392 ELSLEKEQnkrlwdrdtgnsitidhlrrELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneSLEKVSSLTAQLE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1050 RAKRKLEGDLKLTQESIMDLENDKQ---QLDERLKKKDFELNALNARIedeQALGSQLQKKLKELQ------ARIEELEE 1120
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLESSERtvsDLTASLQEKERAIEATNAEI---TKLRSRVDLKLQELQhlknegDHLRNVQT 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1121 ELEAERTARAKVEKLRSDLSRELEEISERLEEAG-GATSVQIEmNKKREAEFQKMRRDLEEATLqheataaaLRKKHADS 1199
Cdd:pfam15921 549 ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGrTAGAMQVE-KAQLEKEINDRRLELQEFKI--------LKDKKDAK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1200 VAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIK----AKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTS 1275
Cdd:pfam15921 620 IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNevktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKM 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1276 QRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQ----------LEEEVKAKNALAHALQSARH------- 1338
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQidalqskiqfLEEAMTNANKEKHFLKEEKNklsqels 779
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034587182 1339 -----------DCDLLREQYEEETEAKAELQRVLSKANSEVAQWRtkyetDAIQRTEElEEAKKKLAQRLQEAE 1401
Cdd:pfam15921 780 tvateknkmagELEVLRSQERRLKEKVANMEVALDKASLQFAECQ-----DIIQRQEQ-ESVRLKLQHTLDVKE 847
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
900-1574 |
1.63e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.57 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 900 DAEERCDQLIKNKIQLEakvkEMNERLEDEEEmNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATenKVKNLT 979
Cdd:COG4913 222 DTFEAADALVEHFDDLE----RAHEALEDARE-QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR--RLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 980 EEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTL-TKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGD 1058
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1059 LKLTQEsimDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIeeleeeleaertarAKVEKLRSD 1138
Cdd:COG4913 375 LPASAE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI--------------ASLERRKSN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1139 LSRELEEISERLEEAGGATSVQ-------IEMnKKREAEFqkmrRDLEEATLQHEATAAALRKKHADSVAELGEQID--- 1208
Cdd:COG4913 438 IPARLLALRDALAEALGLDEAElpfvgelIEV-RPEEERW----RGAIERVLGGFALTLLVPPEHYAAALRWVNRLHlrg 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1209 --NLQRVKQKLEKEKSEF--------KLELDD--VTSNMEQIIKAKANLEKmCRTLEDQMNEHRS-------KAEETQRS 1269
Cdd:COG4913 513 rlVYERVRTGLPDPERPRldpdslagKLDFKPhpFRAWLEAELGRRFDYVC-VDSPEELRRHPRAitragqvKGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1270 VNDLTSQRAKLQT--ENGelsRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQy 1347
Cdd:COG4913 592 KDDRRRIRSRYVLgfDNR---AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE- 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1348 EEETEAKAELQRvLSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIED 1427
Cdd:COG4913 668 REIAELEAELER-LDASSDDL---------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1428 LMVDVErsnaAAAALDKKQRNFDkiLAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNlqe 1507
Cdd:COG4913 732 LQDRLE----AAEDLARLELRAL--LEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPA--- 802
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1508 EISDLTEQLGSsgktIHELEKVRKQLEAEKM-ELQSALEEAEASLEHEEGKILRAQL--EFNQIKAEIER 1574
Cdd:COG4913 803 ETADLDADLES----LPEYLALLDRLEEDGLpEYEERFKELLNENSIEFVADLLSKLrrAIREIKERIDP 868
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
852-1516 |
2.01e-14 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 79.00 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 852 MKEEFTRLKEALEKSEARRKELEEKMVSLlqeKNDLQLQVQAEQDNLADAEercdqliKNKIQLEAKVKEMNERLED-EE 930
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDL---NNNIEKMILAFEELRVQAE-------NARLEMHFKLKEDHEKIQHlEE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 931 EMNAELTAKKRK---LEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQAL 1007
Cdd:pfam05483 230 EYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSM 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1008 DDLQAEEDKVNTLTKAKVKL----EQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKK 1083
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1084 DFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISErLEEAGGATSVQIEM 1163
Cdd:pfam05483 390 SSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHD-LEIQLTAIKTSEEH 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1164 NKKreaEFQKMRRDLEEATLQHeataaalrkkhadsvAELGEQIDNLQRVKQKLEKEKSEFKLELDDvtsNMEQIIKAKA 1243
Cdd:pfam05483 469 YLK---EVEDLKTELEKEKLKN---------------IELTAHCDKLLLENKELTQEASDMTLELKK---HQEDIINCKK 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1244 NLEKMCRTLEDqmnehrskAEETQRSV-NDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQ---L 1319
Cdd:pfam05483 528 QEERMLKQIEN--------LEEKEMNLrDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnnL 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1320 EEEVKAKNALAHALQsarHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQE 1399
Cdd:pfam05483 600 KKQIENKNKNIEELH---QENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1400 AEEAVEAVNAKCSSLEKTKHRLQNEIEDLMvdversnaaaAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLST 1479
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRCQHKIAEMV----------ALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI 746
|
650 660 670
....*....|....*....|....*....|....*..
gi 1034587182 1480 ELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQL 1516
Cdd:pfam05483 747 ELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAIL 783
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
962-1428 |
2.09e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.31 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 962 AKVEKEKHAT----ENKVKNLTEEMAGLDE--IIAKLTKEKKALQ-EAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDL 1034
Cdd:PRK02224 198 EKEEKDLHERlnglESELAELDEEIERYEEqrEQARETRDEADEVlEEHEERREELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1035 EGSLEQEKKVRMDLERAKRKLEGDLKLT-------QESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKK 1107
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDdadaeavEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1108 LKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEA----GGATSVQIEMN------KKREAEFQKMRRD 1177
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDApvdlGNAEDFLEELReerdelREREAELEATLRT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1178 LEEATLQHEATAAALR----------KKHADSVAELGEQIDnlqrvkqKLEKEKSEFKLELDDVTSNMEQIIKAKA---- 1243
Cdd:PRK02224 438 ARERVEEAEALLEAGKcpecgqpvegSPHVETIEEDRERVE-------ELEAELEDLEEEVEEVEERLERAEDLVEaedr 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1244 --NLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTEnGELSRQLDEKEALISQLTRGKL-TYTQQLEDLKRQLE 1320
Cdd:PRK02224 511 ieRLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE-AEEKREAAAEAEEEAEEAREEVaELNSKLAELKERIE 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1321 EEVKAKNALAhALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQEA 1400
Cdd:PRK02224 590 SLERIRTLLA-AIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARI---EEAREDKERAEEYLEQV 665
|
490 500
....*....|....*....|....*...
gi 1034587182 1401 EEAVEAVNAKCSSLEKTKHRLQNEIEDL 1428
Cdd:PRK02224 666 EEKLDELREERDDLQAEIGAVENELEEL 693
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
880-1700 |
2.81e-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: 79.11 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 880 LLQEKNDLQLQVQAEQDNLADAEERC---DQLIKNKIQLEAK---VKEMNERLEDEEEMNAEltaKKRKLEDECSELKRD 953
Cdd:pfam12128 153 TLLGRERVELRSLARQFALCDSESPLrhiDKIAKAMHSKEGKfrdVKSMIVAILEDDGVVPP---KSRLNRQQVEHWIRD 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 954 IDdlelTLAKVEKEKHatenKVKNLTEEMAGLDEIIAKLTKEKKALQEaHQQALDDLQAEEDKvntltkAKVKLEQQVDD 1033
Cdd:pfam12128 230 IQ----AIAGIMKIRP----EFTKLQQEFNTLESAELRLSHLHFGYKS-DETLIASRQEERQE------TSAELNQLLRT 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1034 LEGSLeqekkvrmdlerakrklegdlkltQESIMDLENDKQQLDERLKKKDFELNALNARiedeqalgsqlqkKLKELQA 1113
Cdd:pfam12128 295 LDDQW------------------------KEKRDELNGELSAADAAVAKDRSELEALEDQ-------------HGAFLDA 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1114 RIEeleeeleaerTARAKVEKLRSdLSRELEEISERLE-EAGGATSVQIEMNKKREAEFQKMRRDL-----------EEA 1181
Cdd:pfam12128 338 DIE----------TAAADQEQLPS-WQSELENLEERLKaLTGKHQDVTAKYNRRRSKIKEQNNRDIagikdklakirEAR 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1182 TLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANlekmcrtlEDQMNEHRS 1261
Cdd:pfam12128 407 DRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENF--------DERIERARE 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1262 KAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTrgkltytQQLEDLKRQL------------EEEVKAKNAL 1329
Cdd:pfam12128 479 EQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQ-------SALDELELQLfpqagtllhflrKEAPDWEQSI 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1330 AHALQSAR-HDCDLLREQYEEETEAKAELQRV-LSKANSEVAQWrtkyetdaIQRTEELEEakkklaqRLQEAEEAVEAV 1407
Cdd:pfam12128 552 GKVISPELlHRTDLDPEVWDGSVGGELNLYGVkLDLKRIDVPEW--------AASEEELRE-------RLDKAEEALQSA 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1408 NAKCSSLEKTKHRLQNEIEDLmvDVERSNAAAA---ALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKL 1484
Cdd:pfam12128 617 REKQAAAEEQLVQANGELEKA--SREETFARTAlknARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQL 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1485 KNAYEESLEHLETFKRENKN-----LQEEISDLTEQLGSSGKTIhelEKVRKQLEAEKMELQSALEEAEASLEHEEGKIL 1559
Cdd:pfam12128 695 DKKHQAWLEEQKEQKREARTekqayWQVVEGALDAQLALLKAAI---AARRSGAKAELKALETWYKRDLASLGVDPDVIA 771
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1560 RaqlefnqIKAEIeRKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRvkkKMEGDLNEMEIQLShanRMAAEA 1639
Cdd:pfam12128 772 K-------LKREI-RTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLS---NIERAISELQQQLA---RLIADT 837
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587182 1640 QKQVKSLQSLLK---DTQIQLDDAVRANDDLKENIAIVERRNNLLQAELE--ELRAVVEQTERSRK 1700
Cdd:pfam12128 838 KLRRAKLEMERKaseKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSigERLAQLEDLKLKRD 903
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
841-1414 |
3.45e-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: 78.68 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAE--------------QDNLADAEERCD 906
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEeeakrnverqlstlQAQLSDMKKKLE 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 907 QLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLD 986
Cdd:pfam01576 535 EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEK 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 987 EIIAKLT------------KEKKALQEAHqqALDDLQaeeDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRK 1054
Cdd:pfam01576 615 AISARYAeerdraeaeareKETRALSLAR--ALEEAL---EAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRA 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1055 LEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIE-DEQALGSQLQKKLKELQARIEELEEELEAERTARAKVE 1133
Cdd:pfam01576 690 LEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFErDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAV 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1134 KLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEA--------------------------TLQHEA 1187
Cdd:pfam01576 770 AAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEArasrdeilaqskesekklknleaellQLQEDL 849
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1188 TAAALRKKHADSVA-ELGEQIDN-------LQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEH 1259
Cdd:pfam01576 850 AASERARRQAQQERdELADEIASgasgksaLQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAE 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1260 RSKAEETQrsvndltSQRAKLQTENGELSRQLDEKEALI-SQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARH 1338
Cdd:pfam01576 930 RSTSQKSE-------SARQQLERQNKELKAKLQEMEGTVkSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEK 1002
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587182 1339 DCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSL 1414
Cdd:pfam01576 1003 KLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE-EAEEEASRANAARRKLQRELDDATESNESMNREVSTL 1077
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1053-1800 |
3.56e-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: 78.14 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1053 RKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKelqarieeleeeleaerTARAKV 1132
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLK-----------------KNKDKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1133 EKLRSDLSRELEEISERLEEaggatsvqieMNKKrEAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQR 1212
Cdd:TIGR04523 99 NKLNSDLSKINSEIKNDKEQ----------KNKL-EVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1213 VKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSkaeetqrsvndLTSQRAKLQTENGELSRQLD 1292
Cdd:TIGR04523 167 QKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKS-----------LESQISELKKQNNQLKDNIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1293 EKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAknalahaLQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQ-W 1371
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ-------LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1372 RTKYETDAIQRTEELEEAKKKLAQrlqeAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDK 1451
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQ----NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1452 ILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRK 1531
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1532 QLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAE---IERKLAEKDEEMEQAKRNhLRVVDSLQTSLDAETRSR 1608
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEkkeLEEKVKDLTKKISSLKEK-IEKLESEKKEKESKISDL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1609 NEALrVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEEL 1688
Cdd:TIGR04523 544 EDEL-NKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1689 RAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKA----KKAIT---- 1760
Cdd:TIGR04523 623 KKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELslhyKKYITrmir 702
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1034587182 1761 --DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEA 1800
Cdd:TIGR04523 703 ikDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
32-76 |
3.77e-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: 3.77e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1034587182 32 DLKKDVFVPDDKQEFVKAKIVSREGGKVTAETEYGKTVTVKEDQV 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
901-1548 |
3.99e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.18 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 901 AEERCDQLIKNKIQ-LEAKVKEMNERLEDEEEMNAELtAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLT 979
Cdd:PRK03918 187 RTENIEELIKEKEKeLEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 980 EEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLtKAKVKLEQQVDDLE---GSLEQEKKVRMDLERAKRKLE 1056
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEeeiNGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1057 GDLKLTQESIMDLENDKQQLDERLKKKDfELNALNARIEDEQAlgSQLQKKLKELQARIEELEEELEAERTARAKVEKLR 1136
Cdd:PRK03918 345 KKLKELEKRLEELEERHELYEEAKAKKE-ELERLKKRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1137 SDLSRELEEiserLEEAGGATSVQiemnkKREAEFQKMRRDLEEATLQheataaalRKKHADSVAELGEQIDNLQRVKQK 1216
Cdd:PRK03918 422 KELKKAIEE----LKKAKGKCPVC-----GRELTEEHRKELLEEYTAE--------LKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1217 LEKeksefklelddVTSNMEQIIKAKANLEKMcRTLEDQMNEHR-SKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKE 1295
Cdd:PRK03918 485 LEK-----------VLKKESELIKLKELAEQL-KELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1296 ALISQLTrgkltytqQLEDLKRQLEEEVKaknalahalqsarhdcDLLREQYEEETEAKAELQRvlskansevaqwrtky 1375
Cdd:PRK03918 553 ELKKKLA--------ELEKKLDELEEELA----------------ELLKELEELGFESVEELEE---------------- 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1376 etdaiqRTEELEEAKKKLaqrlqeaeeaVEAVNAkcsslEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAE 1455
Cdd:PRK03918 593 ------RLKELEPFYNEY----------LELKDA-----EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1456 WKQKYeeSQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQ---EEISDLTEQLGSSGKTIHELEKVRKQ 1532
Cdd:PRK03918 652 LEKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKeelEEREKAKKELEKLEKALERVEELREK 729
|
650
....*....|....*..
gi 1034587182 1533 LEAEKMEL-QSALEEAE 1548
Cdd:PRK03918 730 VKKYKALLkERALSKVG 746
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
843-1385 |
4.34e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.18 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 843 AEREKEMASMKEEFTRLKEaLEKSEARRKELEEKMVSLLQEKNDLQlqvqaeqdnladaeercdqliKNKIQLEAKVKEM 922
Cdd:PRK03918 269 EELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIE---------------------KRLSRLEEEINGI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 923 NERLEDEEEMNAELtakkRKLEDECSELKRDIDDLEltlakvekEKHATENKVKNLTEEMAGLDEIIAKLTKEK--KALQ 1000
Cdd:PRK03918 327 EERIKELEEKEERL----EELKKKLKELEKRLEELE--------ERHELYEEAKAKKEELERLKKRLTGLTPEKleKELE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1001 EAHQQALDdlqaEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGD-----LKLTQESIMDLENDKQQ 1075
Cdd:PRK03918 395 ELEKAKEE----IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1076 LDERLKKKDFELNALNARIEDEQALGSQLQ--KKLKELQARIEELEeeleaertarakVEKLRSDlSRELEEISERLEEA 1153
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYN------------LEELEKK-AEEYEKLKEKLIKL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1154 GGATSVqIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsVAELG-EQIDNLQRVKQKLEKEKSEFkLELDDVT 1232
Cdd:PRK03918 538 KGEIKS-LKKELEKLEELKKKLAELEKKLDELEEELAELLKE----LEELGfESVEELEERLKELEPFYNEY-LELKDAE 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1233 SNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTS-----QRAKLQTENGELSRQLDEKEALISQLTRGKLT 1307
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1308 YTQQLEDLKRQLEEEVKAKNALaHALQSARHDCDLLREQY-----EEETEAKAELQRVLSKANSEVAQwrTKYETDAIQR 1382
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKEL-EKLEKALERVEELREKVkkykaLLKERALSKVGEIASEIFEELTE--GKYSGVRVKA 768
|
...
gi 1034587182 1383 TEE 1385
Cdd:PRK03918 769 EEN 771
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1077-1923 |
7.88e-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: 7.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1077 DERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEEleaertARAKVEKLRSDLSRELEEISERLEEAGGA 1156
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELK------LQELKLKEQAKKALEYYQLKEKLELEEEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1157 TSVQIEMnkKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNME 1236
Cdd:pfam02463 226 LLYLDYL--KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1237 Q-------IIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYT 1309
Cdd:pfam02463 304 KlerrkvdDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1310 QQLEDLKRQLEEEvkaknaLAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEA 1389
Cdd:pfam02463 384 ERLSSAAKLKEEE------LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1390 KKKLAQRLQEAEEAVEAVNAKCsSLEKTKHRLQNEIEDLMVDVERSNAA---AAALDKKQRNFDKILAEWKQKYEESQSE 1466
Cdd:pfam02463 458 LKLLKDELELKKSEDLLKETQL-VKLQEQLELLLSRQKLEERSQKESKArsgLKVLLALIKDGVGGRIISAHGRLGDLGV 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1467 LESSQKEARSLST-ELFKLKNAYEESLEHLETFKRENKN----LQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQ 1541
Cdd:pfam02463 537 AVENYKVAISTAViVEVSATADEVEERQKLVRALTELPLgarkLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1542 SALEEAEASLEHEEGKILraqlefnqiKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGD 1621
Cdd:pfam02463 617 EDDKRAKVVEGILKDTEL---------TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAES 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1622 LNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIV---ERRNNLLQAELEELRAVVEQTERS 1698
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLlkqKIDEEEEEEEKSRLKKEEKEEEKS 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1699 RKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKA----ITDAAMMAEELKKEQD 1774
Cdd:pfam02463 768 ELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEekikEEELEELALELKEEQK 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1775 TSAHLE---RMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELT 1851
Cdd:pfam02463 848 LEKLAEeelERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEA 927
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034587182 1852 YQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1923
Cdd:pfam02463 928 EILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
843-1602 |
8.72e-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: 8.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 843 AEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM 922
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 923 NERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEA 1002
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1003 HQQALDDLQA--EEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERL 1080
Cdd:pfam02463 435 EEESIELKQGklTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1081 KKKDFEL------------------NALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRE 1142
Cdd:pfam02463 515 LIKDGVGgriisahgrlgdlgvaveNYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSI 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1143 LEEISERL--EEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAElGEQIDNLQRVKQKLEKE 1220
Cdd:pfam02463 595 AVLEIDPIlnLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEE-GLAEKSEVKASLSELTK 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1221 KSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQ---LDEKEAL 1297
Cdd:pfam02463 674 ELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQkidEEEEEEE 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1298 ISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDC----DLLREQYEEETEAKAELQRVLSKANSEVAQWRT 1373
Cdd:pfam02463 754 KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLkaqeEELRALEEELKEEAELLEEEQLLIEQEEKIKEE 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1374 KYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKiL 1453
Cdd:pfam02463 834 ELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL-L 912
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1454 AEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLE-HLETFKRENKNLQEEISDLTEQLGSSgktIHELEKVRKQ 1532
Cdd:pfam02463 913 EEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEEnNKEEEEERNKRLLLAKEELGKVNLMA---IEEFEEKEER 989
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1533 LEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLD 1602
Cdd:pfam02463 990 YNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSG 1059
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1381-1926 |
3.30e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.10 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1381 QRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKhrlqNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKy 1460
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1461 eesqselESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVR---KQLEAEK 1537
Cdd:PRK03918 275 -------IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1538 MELQSALEEAEASLE-HEEGKILRAQLEfnQIKAEIE----RKLAEKDEEMEQAK---RNHLRVVDSLQTSLDAETRSRN 1609
Cdd:PRK03918 348 KELEKRLEELEERHElYEEAKAKKEELE--RLKKRLTgltpEKLEKELEELEKAKeeiEEEISKITARIGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1610 EALRVKKKMEGD--LNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLkENIAIVERRNNLLQAELEE 1687
Cdd:PRK03918 426 KAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQ 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1688 LRAVVEQTErsrKLAEQELIETSERVQLLHSQNTslinqkkKMDADLSQLQTEVEEAvqecrNAEEKAKKAITDAAMMAE 1767
Cdd:PRK03918 505 LKELEEKLK---KYNLEELEKKAEEYEKLKEKLI-------KLKGEIKSLKKELEKL-----EELKKKLAELEKKLDELE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1768 ELKKEQdtsahLERMKKNMEQTIKDLQHRLDEAEQ-----IALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRK 1842
Cdd:PRK03918 570 EELAEL-----LKELEELGFESVEELEERLKELEPfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1843 SERRIKELTYQ-TEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERAD---IAESQVN 1918
Cdd:PRK03918 645 LRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEkleKALERVE 724
|
....*...
gi 1034587182 1919 KLRAKSRD 1926
Cdd:PRK03918 725 ELREKVKK 732
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1253-1925 |
4.07e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1253 EDQMNEHRSKAEETQRSVNDltsQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKrqLEEEVKAKNALAHA 1332
Cdd:PTZ00121 1050 EDIDGNHEGKAEAKAHVGQD---EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGK--AEEARKAEEAKKKA 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1333 LQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKK----KLAQRLQEAEEAVEAVN 1408
Cdd:PTZ00121 1125 EDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKaeevRKAEELRKAEDARKAEA 1204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1409 AKCSSLEKT-----KHRLQNEIEDLM-VDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELF 1482
Cdd:PTZ00121 1205 ARKAEEERKaeearKAEDAKKAEAVKkAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1483 KLknayEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQ 1562
Cdd:PTZ00121 1285 KA----EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1563 LEFNQIKAEiERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAEtRSRNEALRVKKKMEgdlnemeiqlshANRMAAEAQKQ 1642
Cdd:PTZ00121 1361 AAEEKAEAA-EKKKEEAKKKADAAKKKAEEKKKADEAKKKAE-EDKKKADELKKAAA------------AKKKADEAKKK 1426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1643 VKSLQSllKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTS 1722
Cdd:PTZ00121 1427 AEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1723 LINQKKKMDadlSQLQTEVEEAVQECRNAEEKAKkaiTDAAMMAEELKKEQDTSAhLERMKKNMEQTIKDLQHRLDEAEQ 1802
Cdd:PTZ00121 1505 AAEAKKKAD---EAKKAEEAKKADEAKKAEEAKK---ADEAKKAEEKKKADELKK-AEELKKAEEKKKAEEAKKAEEDKN 1577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1803 IALKGGKKQLQKLEARVRELENELEAEQKRNAESVKgmRKSERRIK-ELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQ 1881
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1034587182 1882 AEE----AEEQANTNLSKFRKVQhELDEAEERADIAESQVNKLRAKSR 1925
Cdd:PTZ00121 1656 EEEnkikAAEEAKKAEEDKKKAE-EAKKAEEDEKKAAEALKKEAEEAK 1702
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
831-1327 |
5.13e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 74.29 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 831 KLYFKIKPLLKSA-EREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADaeercdqlI 909
Cdd:TIGR04523 121 KLEVELNKLEKQKkENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK--------I 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 910 KNKI-QLEAKVKEMNERLEDEEEMNAELT---AKKRKLEDECSELKRDIDDLELTLAKVE-------------------- 965
Cdd:TIGR04523 193 KNKLlKLELLLSNLKKKIQKNKSLESQISelkKQNNQLKDNIEKKQQEINEKTTEISNTQtqlnqlkdeqnkikkqlsek 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 966 -KEKHATENKVKNLTEEMAGLDEIIAKLTKEKKalQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKV 1044
Cdd:TIGR04523 273 qKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1045 RMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEA 1124
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1125 ERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAAL------RKKHAD 1198
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkklneeKKELEE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1199 SVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNmeqIIKAKANLEKmcRTLEDQMNEHRSKAEETQRSVNDLTSQRA 1278
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE---LNKDDFELKK--ENLEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1034587182 1279 KLQTEngelsrqLDEKEALISQLTRGKLTYTQQLEDLKRQLeEEVKAKN 1327
Cdd:TIGR04523 586 EKQEL-------IDQKEKEKKDLIKEIEEKEKKISSLEKEL-EKAKKEN 626
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
843-1300 |
9.86e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 9.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 843 AEREKEMASMKEEFTRLKEAL---------------------EKSEARRKELEEKMVSLLQEKNDLQLQVQA-------E 894
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLeeleeerddllaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAhneeaesL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 895 QDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENK 974
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 975 VKNLTEEMAGLDEIIAkltkEKKALQEA--------------HQQALDDlqaEEDKVNTLTKAKVKLEQQVDDLEGSLEQ 1040
Cdd:PRK02224 428 EAELEATLRTARERVE----EAEALLEAgkcpecgqpvegspHVETIEE---DRERVEELEAELEDLEEEVEEVEERLER 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1041 EKKVRmDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEE 1120
Cdd:PRK02224 501 AEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1121 ELEAERTARAKVEKLRSDLSrELEEISERLEEAGGATSVQIEMNKKRE---AEFQKMRRDLEEATLQHEATAAALRKKHA 1197
Cdd:PRK02224 580 KLAELKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDERRerlAEKRERKRELEAEFDEARIEEAREDKERA 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1198 DS-VAELGEQIDNLQRVKQKLEKEKSEFKLELDdvtsNMEQIIKAKANLEKMCRTLEDQMNEhrskAEETQRSVNDLtsq 1276
Cdd:PRK02224 659 EEyLEQVEEKLDELREERDDLQAEIGAVENELE----ELEELRERREALENRVEALEALYDE----AEELESMYGDL--- 727
|
490 500
....*....|....*....|....*
gi 1034587182 1277 RAKLQTEN-GELSRQLDEKEALISQ 1300
Cdd:PRK02224 728 RAELRQRNvETLERMLNETFDLVYQ 752
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
860-1209 |
1.48e-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: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 860 KEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDnLADAEERCDQLIKNKI---QLEAKVKEMNERLEDEEEMNAEL 936
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE-RREALQRLAEYSWDEIdvaSAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 937 takkRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEmagLDEIIAKLTKEKKALQEAHQQALDDLQAEEDK 1016
Cdd:COG4913 688 ----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE---LDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1017 VNTLTKAKVKLEQQVDDLEGSLEQ-EKKVRMDLERAKRKLEGDLKLTQESIMDLEndkqqlderlkkkdfELNALNARIE 1095
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLP---------------EYLALLDRLE 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1096 DEqalgsqlqkKLKELQARIEELEEeleaeRTARAKVEKLRSDLSRELEEISERLEEA---------GGATSVQIEMNKK 1166
Cdd:COG4913 826 ED---------GLPEYEERFKELLN-----ENSIEFVADLLSKLRRAIREIKERIDPLndslkripfGPGRYLRLEARPR 891
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1034587182 1167 REAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDN 1209
Cdd:COG4913 892 PDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
835-1511 |
1.59e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 835 KIKPLLKSAEREKEMAsmKEEFTRLKEALEKSEARRKELEEKmvsllqekndlqlqvqaeqdnladaeercdqliKNKIQ 914
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKA--DAAKKKAEEAKKAAEAAKAEAEAA---------------------------------ADEAE 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 915 LEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRdiddleltlaKVEKEKHATEnKVKNLTEEMAGLDEIIAKLTK 994
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK----------KAEEDKKKAD-ELKKAAAAKKKADEAKKKAEE 1429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 995 EKKAlQEAHQQALDDLQAEEdkvntlTKAKVKLEQQVDDLEGSLEQEKKVrmdlERAKRKLEgDLKLTQESIMDLENDKQ 1074
Cdd:PTZ00121 1430 KKKA-DEAKKKAEEAKKADE------AKKKAEEAKKAEEAKKKAEEAKKA----DEAKKKAE-EAKKADEAKKKAEEAKK 1497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1075 QLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQArieeleeeleaeRTARAKVEKLRSDLSRELEEISERLEEAg 1154
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA------------DEAKKAEEKKKADELKKAEELKKAEEKK- 1564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1155 gatsvQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEfklelDDVTSN 1234
Cdd:PTZ00121 1565 -----KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKK 1634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1235 MEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRsvndltsqRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLED 1314
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK--------KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1315 LKRQLEEEVKAKNALAHALQSARHDCDLLREQyEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEEL-----EEA 1389
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeavieEEL 1785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1390 KKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKilAEWKQKYEESQSELES 1469
Cdd:PTZ00121 1786 DEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEAD--AFEKHKFNKNNENGED 1863
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1034587182 1470 SQKEARSlSTELFKLKNAYEESLEHLETFKRENKNLQEEISD 1511
Cdd:PTZ00121 1864 GNKEADF-NKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1037-1926 |
1.64e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 73.16 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1037 SLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFElNALNARIEDEQALGSQLQKKLKELQARIE 1116
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS-REIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1117 ELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGatsvQIEMNKKREA-EFQKMRRDLEEATLQHEATAAALRKK 1195
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLN----DLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1196 HADSVAELGE-----QIDNLQRVKQKLEKEKSEFKLELD------DVTSNMEQIIK-AKANLEKMCRTLEDQMNEHRSKA 1263
Cdd:TIGR00606 342 KTELLVEQGRlqlqaDRHQEHIRARDSLIQSLATRLELDgfergpFSERQIKNFHTlVIERQEDEAKTAAQLCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1264 EETQRSVNDLTSQRAKL----QTENGELSRQLDEKEALISQLTRGkltyTQQLEDLKRQLEEEVKAKNALAHALQSARHD 1339
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLgrtiELKKEILEKKQEELKFVIKELQQL----EGSSDRILELDQELRKAERELSKAEKNSLTE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1340 CDLLREQYEEETeaKAELQRVLSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRL-----QEAEEAVEAVN--AKCS 1412
Cdd:TIGR00606 498 TLKKEVKSLQNE--KADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQIrkiksRHSDELTSLLGyfPNKK 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1413 SLEKTKHRLQNEI---EDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEES-------------QSELESSQKEARS 1476
Cdd:TIGR00606 574 QLEDWLHSKSKEInqtRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgsqdeesdLERLKEEIEKSSK 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1477 LSTELFKLKNAYEESLEHLET------------FKREnKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSAL 1544
Cdd:TIGR00606 654 QRAMLAGATAVYSQFITQLTDenqsccpvcqrvFQTE-AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLA 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1545 EEAEASLEHEEGKILRAQLEFNQIKAEIERKLA--EKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDL 1622
Cdd:TIGR00606 733 PGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNdiEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQA 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1623 NEMEiqlshanrmAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRA----VVEQTERS 1698
Cdd:TIGR00606 813 AKLQ---------GSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklqIGTNLQRR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1699 RKLAEQeLIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQecrNAEEKAKKAITDAAMMAEELKK------- 1771
Cdd:TIGR00606 884 QQFEEQ-LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS---SKETSNKKAQDKVNDIKEKVKNihgymkd 959
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1772 -EQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENELEAE--QKRNAESVKGMRKSERRIK 1848
Cdd:TIGR00606 960 iENKIQDGKDDYLKQKETELNTVNAQLEECEK--------HQEKINEDMRLMRQDIDTQkiQERWLQDNLTLRKRENELK 1031
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587182 1849 ELtyqtEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRD 1926
Cdd:TIGR00606 1032 EV----EEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYRE 1105
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1487-1924 |
2.30e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.38 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1487 AYEESLEHLETfkrenknLQEEISDLTEqlgssgkTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFN 1566
Cdd:PRK02224 245 EHEERREELET-------LEAEIEDLRE-------TIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1567 QIKAEIErKLAEKDEEMEQAKRNHLrvVDSLQTSLDAET--------RSRNEALRVK-KKMEGDLNEMEIQLSHANRMAA 1637
Cdd:PRK02224 311 AVEARRE-ELEDRDEELRDRLEECR--VAAQAHNEEAESlredaddlEERAEELREEaAELESELEEAREAVEDRREEIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1638 EAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSR---KLAE--QElIETSER 1712
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagKCPEcgQP-VEGSPH 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1713 VQLLHSQNtsliNQKKKMDADLSQLQTEVEEAvqecrnaEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTIKD 1792
Cdd:PRK02224 467 VETIEEDR----ERVEELEAELEDLEEEVEEV-------EERLERA--------EDLVEAEDRIERLEERREDLEELIAE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1793 LQHRLDEAEQialkggkkQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEE---DRKNLLRLQDLVD 1869
Cdd:PRK02224 528 RRETIEEKRE--------RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAElkeRIESLERIRTLLA 599
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 1870 KLQLKVKAYKRQAEEAEEQANTN------LSKFRKVQHELDEAEERADIAESQVNKLRAKS 1924
Cdd:PRK02224 600 AIADAEDEIERLREKREALAELNderrerLAEKRERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1488-1828 |
5.05e-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: 70.87 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1488 YEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQsaleEAEASLEHEEGKILRAQLEFNQ 1567
Cdd:pfam05622 140 YKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1568 IKA-------EIERKLAEKD---EEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAA 1637
Cdd:pfam05622 216 LEEklealqkEKERLIIERDtlrETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1638 EAQKQvkSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRavveqtersRKLAEQElietservqllh 1717
Cdd:pfam05622 296 LGQEG--SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQ---------KALQEQG------------ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1718 SQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---T 1789
Cdd:pfam05622 353 SKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksV 432
|
330 340 350
....*....|....*....|....*....|....*....
gi 1034587182 1790 IKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEA 1828
Cdd:pfam05622 433 IKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEK 471
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
830-1599 |
7.61e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 70.77 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 830 MKLYFKIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLI 909
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 910 KNKIQ-------------LEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVK 976
Cdd:pfam02463 312 DEEKLkesekekkkaekeLKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 977 NLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLE 1056
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1057 GDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLqKKLKELQARIEELEEELEAERTARAKVEKLR 1136
Cdd:pfam02463 472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDG-VGGRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1137 SDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQK 1216
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILK 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1217 LEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRqldeKEA 1296
Cdd:pfam02463 631 DTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK----KEQ 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1297 LISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYE 1376
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKL 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1377 TDAIQRTE-----ELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVErsnaAAAALDKKQRNFDK 1451
Cdd:pfam02463 787 KVEEEKEEklkaqEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL----EKLAEEELERLEEE 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1452 ILAEWK------QKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHE 1525
Cdd:pfam02463 863 ITKEELlqelllKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034587182 1526 LEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQT 1599
Cdd:pfam02463 943 EEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
840-1255 |
1.14e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.80 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 840 LKSAERE-KEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQD--NLADAEERCDQLIKNKIQLE 916
Cdd:COG4717 73 LKELEEElKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 917 AKVKEMNERLEDEEEMNAELTAKKRKLEDEC-----------SELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL 985
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 986 DEIIAKLTKEKKALQE-----------AHQQALDDLQAEEDKV---------------NTLTKAKVKLEQQVDDLEGSLE 1039
Cdd:COG4717 233 ENELEAAALEERLKEArlllliaaallALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1040 QEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKkdfelnalnARIEDEQALGSQLQKKLKELQARIEELE 1119
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE---------AEELEEELQLEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1120 EELEAertARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKR--EAEFQKMRRDLEEATLQHEataaALRKKHA 1197
Cdd:COG4717 384 EEELR---AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELE----ELREELA 456
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1198 DSVAELG--EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMeqiiKAKANLEKMCRTLEDQ 1255
Cdd:COG4717 457 ELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALK----LALELLEEAREEYREE 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1473-1918 |
1.87e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.56 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1473 EARSLSTELFKLKNAYEESLEhletfKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEasLE 1552
Cdd:COG4913 226 AADALVEHFDDLERAHEALED-----AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1553 HEEGKILRAQLEFNQIKAEIERkLAEKDEEMEQAKRNH-LRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSH 1631
Cdd:COG4913 299 ELRAELARLEAELERLEARLDA-LREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1632 A----NRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEN-------IAIVERRNNLLQAELEELRAVVEqteRSRK 1700
Cdd:COG4913 378 SaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRElreleaeIASLERRKSNIPARLLALRDALA---EALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1701 LAEQ------ELIETS----------ERVqlLHSQNTSL-------------INQKK----------------------- 1728
Cdd:COG4913 455 LDEAelpfvgELIEVRpeeerwrgaiERV--LGGFALTLlvppehyaaalrwVNRLHlrgrlvyervrtglpdperprld 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1729 ------KMDADLSQLQTEVEEAVQE------CRNAEE--KAKKAITDAAMMAEELKK-EQDTSAHLER---MKKNMEQTI 1790
Cdd:COG4913 533 pdslagKLDFKPHPFRAWLEAELGRrfdyvcVDSPEElrRHPRAITRAGQVKGNGTRhEKDDRRRIRSryvLGFDNRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1791 KDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQK--RNAESVKGMRKSERRIKELtyqtEEDRKNLLRLQDLV 1868
Cdd:COG4913 613 AALEAELAELEE-ELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL----EAELERLDASSDDL 687
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1869 DKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVN 1918
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
914-1858 |
2.71e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 69.31 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 914 QLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKekhatenkvknLTEEMAGLDEIIAKLT 993
Cdd:TIGR00606 214 QYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMK-----------LDNEIKALKSRKKQME 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 994 KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVK-LEQQVDDLEGSLEQEKKVRMDLERAKRKLEgdlklTQESIMDLEND 1072
Cdd:TIGR00606 283 KDNSELELKMEKVFQGTDEQLNDLYHNHQRTVReKERELVDCQRELEKLNKERRLLNQEKTELL-----VEQGRLQLQAD 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1073 KQQldERLKKKDFELNALNARIE-DEQALGSQLQKKLKelQARIEELEEELEAERTARAKVEKLRSDLS---RELEEISE 1148
Cdd:TIGR00606 358 RHQ--EHIRARDSLIQSLATRLElDGFERGPFSERQIK--NFHTLVIERQEDEAKTAAQLCADLQSKERlkqEQADEIRD 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1149 RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHE---ATAAALRKKHAD-SVAELGEQIDNLQRVKQKLEKEKSEF 1224
Cdd:TIGR00606 434 EKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDrilELDQELRKAERElSKAEKNSLTETLKKEVKSLQNEKADL 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1225 KLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQraklqtengelsrqldekealisqltRG 1304
Cdd:TIGR00606 514 DRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSL--------------------------LG 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1305 KLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTkYETDAIQRTE 1384
Cdd:TIGR00606 568 YFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQD-EESDLERLKE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1385 ELEEAKKKLA----------QRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDL----MVDVERSNAAAAALDKKQRNFD 1450
Cdd:TIGR00606 647 EIEKSSKQRAmlagatavysQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLqsklRLAPDKLKSTESELKKKEKRRD 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1451 KIL--AEWKQKYEESQSELESSQKEA-RSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLT--EQLgssgktIHE 1525
Cdd:TIGR00606 727 EMLglAPGRQSIIDLKEKEIPELRNKlQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTimERF------QME 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1526 LEKVRKQLEAEKMELQSAleEAEASLEHEEGKILRAQLEFNQIKAEIErkLAEKDEEMEQAKRNHLRvvdSLQTSLDAET 1605
Cdd:TIGR00606 801 LKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKIE--LNRKLIQDQQEQIQHLK---SKTNELKSEK 873
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1606 RSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANddlkeniaivERRNNLLQAEL 1685
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK----------ETSNKKAQDKV 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1686 EELRAVVEQTERSRKLAEQELIETSERvqllhsqntslinQKKKMDADLSQLQTEVEEAVQECRNAEE--KAKKAITDAA 1763
Cdd:TIGR00606 944 NDIKEKVKNIHGYMKDIENKIQDGKDD-------------YLKQKETELNTVNAQLEECEKHQEKINEdmRLMRQDIDTQ 1010
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1764 MMAEELKKEQDTSAHLERMKKNMEQTIKdlQHrLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKS 1843
Cdd:TIGR00606 1011 KIQERWLQDNLTLRKRENELKEVEEELK--QH-LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHF 1087
|
970
....*....|....*
gi 1034587182 1844 ERRIKELTYQTEEDR 1858
Cdd:TIGR00606 1088 KKELREPQFRDAEEK 1102
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1310-1847 |
3.01e-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: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1310 QQLEDLKRQLEEEVKAKNALAHALQSArhdcdllrEQYEEETEAKAELQRVLSKANSEVAQwrTKYETdAIQRTEELEEA 1389
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELA--------ERYAAARERLAELEYLRAALRLWFAQ--RRLEL-LEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1390 KKKLAQRLQEAEEAVEAVNAKCSSLE--------KTKHRLQNEIEDLMVDVERSNAAAAALDKKQRN-----------FD 1450
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAAlglplpasaeeFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1451 KILAEWKQkyeesqselessqkEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEIsdltEQLGSSGKTI-HELEKV 1529
Cdd:COG4913 384 ALRAEAAA--------------LLEALEEELEALEEALAEAEAALRDLRRELRELEAEI----ASLERRKSNIpARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1530 RKQLE-------------AEKMEL-------QSALEEA---------------EASLEHEEGKILRAQLEFNQIKAeier 1574
Cdd:COG4913 446 RDALAealgldeaelpfvGELIEVrpeeerwRGAIERVlggfaltllvppehyAAALRWVNRLHLRGRLVYERVRT---- 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1575 klAEKDEEMEQAKRNHL-RVVDS----LQTSLDAETRSRNEALRVkkkmegdlnEMEIQLSHAnRMAAEAQKQVKSLQSL 1649
Cdd:COG4913 522 --GLPDPERPRLDPDSLaGKLDFkphpFRAWLEAELGRRFDYVCV---------DSPEELRRH-PRAITRAGQVKGNGTR 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1650 L-KDTQIQLD-------DAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAE--QELIETSERVQLLHSQ 1719
Cdd:COG4913 590 HeKDDRRRIRsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAERE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1720 NTSLINQKKKMDA---DLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELkkeqdtsahlermkKNMEQTIKDLQHR 1796
Cdd:COG4913 670 IAELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL--------------EQAEEELDELQDR 735
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587182 1797 LDEAEQIALKGGKKQLQKL------EARVRELENELEAEQKRNAESvkgMRKSERRI 1847
Cdd:COG4913 736 LEAAEDLARLELRALLEERfaaalgDAVERELRENLEERIDALRAR---LNRAEEEL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
851-1405 |
3.08e-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: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 851 SMKEEFTRLKEA---LEKSEARRKELE------EKMVSLLQEKNDLQ-----LQVQAEQDNLADAEERCDQLIKNKIQLE 916
Cdd:COG4913 229 ALVEHFDDLERAheaLEDAREQIELLEpirelaERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 917 AKVKEMNERLEDEEEMNAELTAKKRKLE-DECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKE 995
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 996 KKALQEAHQQALDDLQAEEDKvntLTKAKVKLEQQVDDLEG---SLEQeKKVRMD--LERAKRKLEGDLKLTQESIM--- 1067
Cdd:COG4913 389 AAALLEALEEELEALEEALAE---AEAALRDLRRELRELEAeiaSLER-RKSNIParLLALRDALAEALGLDEAELPfvg 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1068 DLendkqqLDERLKKKDFElNALnariedEQALGSQ----L--QKKLKE---------LQARIEELEEELEAERTARAK- 1131
Cdd:COG4913 465 EL------IEVRPEEERWR-GAI------ERVLGGFaltlLvpPEHYAAalrwvnrlhLRGRLVYERVRTGLPDPERPRl 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1132 -----VEKLRSDLSRELEEISERLEEAGGATSVQiemnkkREAEFQKMRRDL-EEATLQHEATAAALRKKHA-DSVAELG 1204
Cdd:COG4913 532 dpdslAGKLDFKPHPFRAWLEAELGRRFDYVCVD------SPEELRRHPRAItRAGQVKGNGTRHEKDDRRRiRSRYVLG 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1205 EqiDNLQRVKQkLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLE--DQMNEHRSKAEETQRSVNDLTSQRAKLQT 1282
Cdd:COG4913 606 F--DNRAKLAA-LEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1283 ENGELSRQLDEKEALisqltrgkltyTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRvls 1362
Cdd:COG4913 683 SSDDLAALEEQLEEL-----------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--- 748
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1034587182 1363 kanSEVAQWRTKYETDAIQRT--EELEEAKKKLAQRLQEAEEAVE 1405
Cdd:COG4913 749 ---ALLEERFAAALGDAVERElrENLEERIDALRARLNRAEEELE 790
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
861-1658 |
4.18e-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: 68.46 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 861 EALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDnlaDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAK- 939
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTL---CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKr 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 940 -----KRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKnlteemagldeiIAKLTKEKKALQEAHQQALDDLQAEE 1014
Cdd:TIGR00618 250 eaqeeQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK------------AAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1015 DKVNTLTKAKVKLEQQVDDlEGSLEQEKKVRMDLERAKRKLEgDLKLTQESIMDLENDKQQLDERLKKKDFELNALnari 1094
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQ-QSSIEEQRRLLQTLHSQEIHIR-DAHEVATSIREISCQQHTLTQHIHTLQQQKTTL---- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1095 EDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKlrsdlSRELEEISERLEEAGGATSVQIEmnKKREAEFQKM 1174
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKK-----QQELQQRYAELCAAAITCTAQCE--KLEKIHLQES 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1175 RRDLEEATlQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVtsnmeqiikakANLEKMCRTLED 1254
Cdd:TIGR00618 465 AQSLKERE-QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI-----------DNPGPLTRRMQR 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1255 QMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRgkltYTQQLEDLkRQLEEEVKaknalahalq 1334
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR----SKEDIPNL-QNITVRLQ---------- 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1335 sarhdcDLLREQYEEETEAKAELQRVLSKANSEVAqwrtKYETDAIQRTEELEEAKKKLAqrlqeaeeaveavnakcssl 1414
Cdd:TIGR00618 598 ------DLTEKLSEAEDMLACEQHALLRKLQPEQD----LQDVRLHLQQCSQELALKLTA-------------------- 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1415 ektkhrLQNEIEDLMVDVERSNAAAAALDKKQRnfdkilaewkqkyeesqselessqkeARSLSTELFKLKNAYEESLEH 1494
Cdd:TIGR00618 648 ------LHALQLTLTQERVREHALSIRVLPKEL--------------------------LASRQLALQKMQSEKEQLTYW 695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1495 LETFKRENKNLQEEIsdltEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIER 1574
Cdd:TIGR00618 696 KEMLAQCQTLLRELE----THIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1575 KLAEKDEEMEQAKRNHLRVVDSLQTSLdAETRSRNEALRVKKKMEGDLNEMEIQLshanrmAAEAQKQVKSLQSLLKDTQ 1654
Cdd:TIGR00618 772 AALQTGAELSHLAAEIQFFNRLREEDT-HLLKTLEAEIGQEIPSDEDILNLQCET------LVQEEEQFLSRLEEKSATL 844
|
....
gi 1034587182 1655 IQLD 1658
Cdd:TIGR00618 845 GEIT 848
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
901-1140 |
4.43e-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: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 901 AEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTE 980
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 981 EMAGLDEIIAKLTKekkALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLK 1060
Cdd:COG4942 98 ELEAQKEELAELLR---ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1061 LTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIE--ELEEELEAERTARAKVEKLRSD 1138
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIArlEAEAAAAAERTPAAGFAALKGK 254
|
..
gi 1034587182 1139 LS 1140
Cdd:COG4942 255 LP 256
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
847-1695 |
7.90e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 67.67 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 847 KEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQliKNKIQ--------LEAK 918
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQ--QEKIEryqadleeLEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 919 VKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDL-------------------------------ELTLAKVEKE 967
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYqqaldvqqtraiqyqqavqalerakqlcglpDLTADNAEDW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 968 KHATENKVKNLTEEMAGL-------DEIIAKLTKEKKALQ---------EAHQQALDDL-QAEEDKVntLTKAKVKLEQQ 1030
Cdd:PRK04863 444 LEEFQAKEQEATEELLSLeqklsvaQAAHSQFEQAYQLVRkiagevsrsEAWDVARELLrRLREQRH--LAEQLQQLRMR 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1031 VDDLEGSLEQEKkvrmDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKkkdfelnALNARIEDEQALGSQLQKKLKE 1110
Cdd:PRK04863 522 LSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE-------SLSESVSEARERRMALRQQLEQ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1111 LQARIEELEEELEAERTARAKVEKLRSDLSRELEEiSERLEEAggatsvqiemnkkreaeFQKMRRDLEEATLQHEATAA 1190
Cdd:PRK04863 591 LQARIQRLAARAPAWLAAQDALARLREQSGEEFED-SQDVTEY-----------------MQQLLERERELTVERDELAA 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1191 ALRkkhadsvaELGEQIDNLQ--------RVKQKLEKEKSEFKLEL-DDVTSN------------MEQII-----KAKAN 1244
Cdd:PRK04863 653 RKQ--------ALDEEIERLSqpggsedpRLNALAERFGGVLLSEIyDDVSLEdapyfsalygpaRHAIVvpdlsDAAEQ 724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1245 LEKMCRTLED---------QMNEHRSKAEETQRSVNDLTSQRAklqtengelSRqldekealISQLTR----GKLTYTQQ 1311
Cdd:PRK04863 725 LAGLEDCPEDlyliegdpdSFDDSVFSVEELEKAVVVKIADRQ---------WR--------YSRFPEvplfGRAAREKR 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1312 LEDLKRQLEEEVkaknalahalqsarhdcdllrEQYEEETEAKAELQRVLSKANSEVA-------QWRTKYETDAIQRT- 1383
Cdd:PRK04863 788 IEQLRAEREELA---------------------ERYATLSFDVQKLQRLHQAFSRFIGshlavafEADPEAELRQLNRRr 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1384 -------EELEEAKKKLAQRLQEAEEAVEAVN--AKCSSLEKTKHrLQNEIEDLMVDVERSNAAAAALDKKQRNFDKI-- 1452
Cdd:PRK04863 847 veleralADHESQEQQQRSQLEQAKEGLSALNrlLPRLNLLADET-LADRVEEIREQLDEAEEAKRFVQQHGNALAQLep 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1453 -----------LAEWKQKYEESQSELESSQKEARSLsTELFKLKN--AYEESLEHLetfkrenknlqEEISDLTEQLgss 1519
Cdd:PRK04863 926 ivsvlqsdpeqFEQLKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAhfSYEDAAEML-----------AKNSDLNEKL--- 990
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1520 gktiheleKVR-KQLEAEKMELQSALEEAEAslEHEEGKILRAQLE-----FNQIKAEIERKLAE----KDEEMEQAKRN 1589
Cdd:PRK04863 991 --------RQRlEQAEQERTRAREQLRQAQA--QLAQYNQVLASLKssydaKRQMLQELKQELQDlgvpADSGAEERARA 1060
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1590 HLrvvDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQV----KSLQSLLKdtqiqlddAVRAND 1665
Cdd:PRK04863 1061 RR---DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVvnakAGWCAVLR--------LVKDNG 1129
|
970 980 990
....*....|....*....|....*....|....*
gi 1034587182 1666 dlkeniaiVERRnnLLQAEL-----EELRAVVEQT 1695
Cdd:PRK04863 1130 --------VERR--LHRRELaylsaDELRSMSDKA 1154
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1078-1753 |
8.71e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 67.05 E-value: 8.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1078 ERLKKKDFELNALNARIEDEQALGSQLQKKLK-ELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGA 1156
Cdd:pfam05483 63 EGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKvSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1157 TSVQIEMNKKREAEFQKMRRDLE---EATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDvts 1233
Cdd:pfam05483 143 NKDLIKENNATRHLCNLLKETCArsaEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKE--- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1234 NMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSqrakLQTENGELSRQLDEKEAL----ISQLTRGKLTYT 1309
Cdd:pfam05483 220 DHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTF----LLEESRDKANQLEEKTKLqdenLKELIEKKDHLT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1310 QQLEDLKRQLEEEVKAKNALAHALQSA-RHDCDLLRE---QYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEE 1385
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIAtKTICQLTEEkeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QRLEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1386 LEEAKKKLAQRLQ----EAEEAVEAVNAKCSSLEKTKHRLqNEIEDLMVDVERSNAAAAALDKKQRNF-------DKILA 1454
Cdd:pfam05483 375 NEDQLKIITMELQkkssELEEMTKFKNNKEVELEELKKIL-AEDEKLLDEKKQFEKIAEELKGKEQELifllqarEKEIH 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1455 EWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTI----HELEKVR 1530
Cdd:pfam05483 454 DLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIinckKQEERML 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1531 KQ---LEAEKMELQSALEEAEASL--EHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAET 1605
Cdd:pfam05483 534 KQienLEEKEMNLRDELESVREEFiqKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEEL 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1606 RSRNEALRVKKKMEG-DLNEMEIQLSHANRMAAEAQKQ----VKSLQSLLKDTQIQ----LDDAVRANDDLKENIAIVER 1676
Cdd:pfam05483 614 HQENKALKKKGSAENkQLNAYEIKVNKLELELASAKQKfeeiIDNYQKEIEDKKISeeklLEEVEKAKAIADEAVKLQKE 693
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1677 RNNLLQAELEELRAVVEQTERS-RKLAEQELIE-------TSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQEC 1748
Cdd:pfam05483 694 IDKRCQHKIAEMVALMEKHKHQyDKIIEERDSElglyknkEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLK 773
|
....*
gi 1034587182 1749 RNAEE 1753
Cdd:pfam05483 774 MEAKE 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
835-1271 |
1.14e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 835 KIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQ 914
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 915 LEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHatENKVKnlTEEMAGLDEIIAKLTK 994
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIK--AAEEAKKAEEDKKKAE 1678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 995 EKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDlENDKQ 1074
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKK 1757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1075 QLDERlkKKDFELNALNARIEDEQALGSQLQKKlkelqarieeleeeleaERTARAKVEKLRSDLSRELEEISERLEEAG 1154
Cdd:PTZ00121 1758 KIAHL--KKEEEKKAEEIRKEKEAVIEEELDEE-----------------DEKRRMEVDKKIKDIFDNFANIIEGGKEGN 1818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1155 GATSVQIEM---NKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDV 1231
Cdd:PTZ00121 1819 LVINDSKEMedsAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDI 1898
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1034587182 1232 TSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVN 1271
Cdd:PTZ00121 1899 EREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
844-1272 |
1.69e-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: 66.20 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 844 EREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMN 923
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 924 ERLEDE--EEMNAELTAKKRKLE-----------------DECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAG 984
Cdd:TIGR04523 302 NQKEQDwnKELKSELKNQEKKLEeiqnqisqnnkiisqlnEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 985 LDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQ--------------VDDLEGSLEQEKKVRMDLER 1050
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEierlketiiknnseIKDLTNQDSVKELIIKNLDN 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1051 AKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIedeqalgSQLQKKLKELQARIEELEEELEAERTARA 1130
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK-------KELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1131 KVEKLRSDLSRELEEISERLEEAGGATSVQ-----IEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsVAELGE 1205
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKENLEKEIDeknkeIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE----IEEKEK 610
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587182 1206 QIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVND 1272
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1026-1669 |
2.30e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1026 KLEQQVDDLEGSLEQEKKVRMDLERAKRKLE--GDLKLTQESIMDLENDKQQLDE-----RLKKKDFELNALNARIEDEQ 1098
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1099 ALGSQLQKKLKELQARIEELEEELEAERTARAKVE-KLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRD 1177
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEER-----------ERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1178 LEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMN 1257
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1258 EHRSKAEETQRSVNDLtsqrakLQTENGELS--------------------RQLDEKEALISQL-TRGKLTYtQQLEDLK 1316
Cdd:COG4913 451 EALGLDEAELPFVGEL------IEVRPEEERwrgaiervlggfaltllvppEHYAAALRWVNRLhLRGRLVY-ERVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1317 RQLEEEVKAKNALAHALQSARHDC-DLLREQYEEET-----EAKAELQRV--------LSKANSEVAQ------WRTKYE 1376
Cdd:COG4913 524 PDPERPRLDPDSLAGKLDFKPHPFrAWLEAELGRRFdyvcvDSPEELRRHpraitragQVKGNGTRHEkddrrrIRSRYV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1377 T--DAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQN--EIEDLMVDVERSNAAAAALDKKQRNFDKI 1452
Cdd:COG4913 604 LgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDAS 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1453 LAEWKQkyeesqselessqkearsLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEqlgssgktihELEKVRKQ 1532
Cdd:COG4913 684 SDDLAA------------------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE----------ELDELQDR 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1533 LE-AEKMELQSALEEAEASLEHEEGKILRAQL--EFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRN 1609
Cdd:COG4913 736 LEaAEDLARLELRALLEERFAAALGDAVERELreNLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1610 EALRVKKKMEGD------------LNEMEIQ-----LSHANRMAAEAQKQVKSLQSLLK------DTQIQLDDAVRANDD 1666
Cdd:COG4913 816 EYLALLDRLEEDglpeyeerfkelLNENSIEfvadlLSKLRRAIREIKERIDPLNDSLKripfgpGRYLRLEARPRPDPE 895
|
...
gi 1034587182 1667 LKE 1669
Cdd:COG4913 896 VRE 898
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1481-1909 |
3.26e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1481 LFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAE------ASLEHE 1554
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkeeiEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1555 EGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNhLRVVDSLQTslDAETRSRNEALRVKKKMEgdLNEMEIQLSHANR 1634
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKE--KAEEYIKLSEFYEEYLDE--LREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1635 MAAEAQKQVKSLQSLLKDTQiqlddavrandDLKENIAIVERRNNLLQA---ELEELRAVVEQTERSRK-LAEQELIETS 1710
Cdd:PRK03918 322 EINGIEERIKELEEKEERLE-----------ELKKKLKELEKRLEELEErheLYEEAKAKKEELERLKKrLTGLTPEKLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1711 ERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAvqecRNAEEKAKKAITDAAMMAEELKKEqdtsaHLERMKKNMEQTI 1790
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKEL----KKAIEELKKAKGKCPVCGRELTEE-----HRKELLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1791 KDLQHRLDEAEqialkggkKQLQKLEARVRELENELEAEQK--RNAESVKGMRKSERRIKELTYQT-EEDRKNLLRLQDL 1867
Cdd:PRK03918 462 KRIEKELKEIE--------EKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEK 533
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1034587182 1868 VDKLQLKVKAYKRQAEEAEEQANtnlsKFRKVQHELDEAEER 1909
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEE 571
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
914-1343 |
3.45e-10 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 64.92 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 914 QLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 993
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 994 KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDK 1073
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1074 QQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSreleeiserleEA 1153
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS-----------SM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1154 GGATSvqiemnkKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTS 1233
Cdd:pfam07888 264 AAQRD-------RTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1234 NMEQIIKAKANL--EKMCrtledqmneHRSKAEETQRsvnDLTSQRAKLQTENGELSRQLDEKEALisqltrgkLTYTQQ 1311
Cdd:pfam07888 337 ERMEREKLEVELgrEKDC---------NRVQLSESRR---ELQELKASLRVAQKEKEQLQAEKQEL--------LEYIRQ 396
|
410 420 430
....*....|....*....|....*....|..
gi 1034587182 1312 LEdlkRQLEEEVKAKNALAHALQSARHDCDLL 1343
Cdd:pfam07888 397 LE---QRLETVADAKWSEAALTSTERPDSPLS 425
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
839-1293 |
3.71e-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: 65.23 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 839 LLKSAEREKEMAS----------MKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQL 908
Cdd:pfam10174 264 LLHTEDREEEIKQmevykshskfMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 909 iknkiqlEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEI 988
Cdd:pfam10174 344 -------QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 989 IAKLTKEKKALQEAHQQA------LDDLQAEEDKV-NTLTKAKVKLEQQVDDlegSLEQEKKVRMDLERAKRKLEGDLKL 1061
Cdd:pfam10174 417 LAGLKERVKSLQTDSSNTdtalttLEEALSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1062 TQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQarieeleeelEAERTARAKVEklRSDLSR 1141
Cdd:pfam10174 494 KESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH----------NAEEAVRTNPE--INDRIR 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1142 ELE-EISERLEEAGGA-TSVQIEMNKKREAEFQKMRRDLEEATLQheataaALRKKHADSVAELGEQIDNLQRVKQKLEK 1219
Cdd:pfam10174 562 LLEqEVARYKEESGKAqAEVERLLGILREVENEKNDKDKKIAELE------SLTLRQMKEQNKKVANIKHGQQEMKKKGA 635
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034587182 1220 EKSEFKLELDDVTSNMEQIIKAKANLEKMCRTlEDQMNEHRSKAEETQRSvndLTSQRAKLQTENGELSRQLDE 1293
Cdd:pfam10174 636 QLLEEARRREDNLADNSQQLQLEELMGALEKT-RQELDATKARLSSTQQS---LAEKDGHLTNLRAERRKQLEE 705
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1423-1927 |
4.10e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1423 NEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSlSTELFKLKNAYE-ESLEHLETFKRE 1501
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARK-AEDARKAEEARKaEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1502 NKNLQEEISDLTEQlGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASleHEEGKILRAQLEFNQIKAEIERKLAEKDE 1581
Cdd:PTZ00121 1161 EDARKAEEARKAED-AKKAEAARKAEEVRKAEELRKAEDARKAEAARKA--EEERKAEEARKAEDAKKAEAVKKAEEAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1582 EMEQAKR----NHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDlnemEIQLSHANRMAAEAQK--QVKSLQSLLKDTQi 1655
Cdd:PTZ00121 1238 DAEEAKKaeeeRNNEEIRKFEEARMAHFARRQAAIKAEEARKAD----ELKKAEEKKKADEAKKaeEKKKADEAKKKAE- 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1656 qlddAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSlinQKKKMDadls 1735
Cdd:PTZ00121 1313 ----EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE---AKKKAD---- 1381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1736 qlqtEVEEAVQECRNAEEKAKKAITDAAMmAEELKKEQDTSAHLERMKKNMEQTIKdlqhrLDEAEQialkggkkqlqKL 1815
Cdd:PTZ00121 1382 ----AAKKKAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKK-----ADEAKK-----------KA 1440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1816 EARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKnllrlqdlVDKLQLKVKAYKRQAEEAE--EQANTNL 1893
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK--------ADEAKKKAEEAKKKADEAKkaAEAKKKA 1512
|
490 500 510
....*....|....*....|....*....|....*....
gi 1034587182 1894 SKFRKVQH-----ELDEAEERADIAESQVNKLRAKSRDI 1927
Cdd:PTZ00121 1513 DEAKKAEEakkadEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1313-1917 |
5.69e-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: 64.74 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1313 EDLKRQLEEEVKAKNALAHALQSARHDCDLLRE--------------QYEEETEAKAELQRVLSKANSEVAQWRTKYETD 1378
Cdd:pfam05483 130 EKVSLKLEEEIQENKDLIKENNATRHLCNLLKEtcarsaektkkyeyEREETRQVYMDLNNNIEKMILAFEELRVQAENA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1379 AIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQ 1458
Cdd:pfam05483 210 RLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1459 KyeesqselessqkeARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSgktIHELEKVRKQLEAEKM 1538
Cdd:pfam05483 290 K--------------KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQ---MEELNKAKAAHSFVVT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1539 ELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKdEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKK-- 1616
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL-EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKia 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1617 ---------------KMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLK-ENIAIVERRNNL 1680
Cdd:pfam05483 432 eelkgkeqelifllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLlENKELTQEASDM 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1681 LQaeleELRAVVEQTERSRKLAEQELietsERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQEcrnAEEKAKKAIT 1760
Cdd:pfam05483 512 TL----ELKKHQEDIINCKKQEERML----KQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK---SEENARSIEY 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1761 DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRlDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGM 1840
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQE-NKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1841 RK-------SERRIKELTYQTEEDRKNLLRLQDLVDK-LQLKV-------KAYKRQAEEAEEQANTNLSKFRKVQHELDE 1905
Cdd:pfam05483 660 QKeiedkkiSEEKLLEEVEKAKAIADEAVKLQKEIDKrCQHKIaemvalmEKHKHQYDKIIEERDSELGLYKNKEQEQSS 739
|
650
....*....|..
gi 1034587182 1906 AEERADIAESQV 1917
Cdd:pfam05483 740 AKAALEIELSNI 751
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1477-1923 |
5.89e-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: 64.66 E-value: 5.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1477 LSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEA---EASLEH 1553
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIknkLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1554 ---------EEGKILRAQL-----EFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQ------TSLDAETRSRNEALR 1613
Cdd:TIGR04523 202 llsnlkkkiQKNKSLESQIselkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDeqnkikKQLSEKQKELEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1614 VKKKMEGDLNEMEIQLSHANRMAA-----EAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEEL 1688
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1689 RAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEE 1768
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1769 LKKEQDTSAHLERMKKNMEQTIKDLQHRLD-------------EAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAE 1835
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqnlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1836 SVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQL-KVKAYKRQAEEAEEQANTNLSKfrkvqhELDEAEERADIAE 1914
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLeKEIDEKNKEIEELKQTQKSLKK------KQEEKQELIDQKE 595
|
....*....
gi 1034587182 1915 SQVNKLRAK 1923
Cdd:TIGR04523 596 KEKKDLIKE 604
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1228-1705 |
9.41e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 9.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1228 LDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGK-- 1305
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLql 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1306 LTYTQQLEDLKRQLEEEVKAKNALAHALQSARHdcdlLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEE 1385
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1386 LEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTK--HRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEES 1463
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1464 QSELEssqkearsLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSA 1543
Cdd:COG4717 284 GLLAL--------LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1544 LEEAEASLEHEEGKILRAQLeFNQIKAEIERKLAEKDEEMEQAkRNHLRVVDSLQTSLDAETRSRNEALRvkkkmEGDLN 1623
Cdd:COG4717 356 AEELEEELQLEELEQEIAAL-LAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLE-----ALDEE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1624 EMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRAN--DDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKL 1701
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
....
gi 1034587182 1702 AEQE 1705
Cdd:COG4717 509 YREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1615-1836 |
1.08e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1615 KKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQ 1694
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1695 TER--SRKLAEQELIETSERVQLLHSQNTS--LINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELK 1770
Cdd:COG4942 102 QKEelAELLRALYRLGRQPPLALLLSPEDFldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587182 1771 KEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKRNAES 1836
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1472-1935 |
1.40e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1472 KEARSLSTELFKLknayEESLEHLETFKRENKNLQEEISDLTEQLGSsgktiheLEKVRKQLEAEKMELQSALEEAEASL 1551
Cdd:PRK03918 207 REINEISSELPEL----REELEKLEKEVKELEELKEEIEELEKELES-------LEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1552 EHEEGKILRaqLEFNQIKAEIERKLAEKDEEMEQAKRNhlrvVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSH 1631
Cdd:PRK03918 276 EELEEKVKE--LKELKEKAEEYIKLSEFYEEYLDELRE----IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1632 ANRMAAEAQKQVKSLQSLL-KDTQIQLDDAVRAN---DDLKENIAIVERRNNLLQAELEEL---RAVVEQTERSRKLAEQ 1704
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKaKKEELERLKKRLTGltpEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1705 ELIETSERVQLLHSQNTSliNQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAitdaammAEELKKEQDTSAHLERMKK 1784
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTE--EHRKELLEEYTAELKRIEKELKEIEEKERKLRKE-------LRELEKVLKKESELIKLKE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1785 NMEQtIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAeQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLR- 1863
Cdd:PRK03918 501 LAEQ-LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS-LKKELEKLEELKKKLAELEKKLDELEEELAELLKe 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1864 --------LQDLVDKLQLKVKAYKR--QAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLN 1933
Cdd:PRK03918 579 leelgfesVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
..
gi 1034587182 1934 EE 1935
Cdd:PRK03918 659 EE 660
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1440-1880 |
1.60e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1440 AALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLtEQLGSS 1519
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1520 GKTIHELEKVRKQLEAEKMELQsALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQT 1599
Cdd:COG4717 128 LPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1600 SLDAETRSRNEALRVKKKMEGDLNEMEIQLshanrMAAEAQKQVKSLQSLLK--DTQIQLDDAVRANDDLKENIA----- 1672
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARLLLLiaAALLALLGLGGSLLSLILTIAgvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1673 ------IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQ 1746
Cdd:COG4717 282 vlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1747 ECRNAEEKAKKA----------ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALkggKKQLQKLE 1816
Cdd:COG4717 362 ELQLEELEQEIAallaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL---EEELEELE 438
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034587182 1817 ARVRELENELEAEQKRnaesvkgMRKSERRIKELTyQTEEDRKNLLRLQDLVDKLQLKVKAYKR 1880
Cdd:COG4717 439 EELEELEEELEELREE-------LAELEAELEQLE-EDGELAELLQELEELKAELRELAEEWAA 494
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
862-1567 |
2.10e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 62.53 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 862 ALEKSEARRKE-LEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKK 940
Cdd:pfam10174 46 ALRKEEAARISvLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 941 RKLEDECSELKRDIDDLELtlaKVEKEKHATENKvknlteemaglDEIIAKLtkekkaLQEAHQQALDDLQAEEDkvNTL 1020
Cdd:pfam10174 126 ERQAKELFLLRKTLEEMEL---RIETQKQTLGAR-----------DESIKKL------LEMLQSKGLPKKSGEED--WER 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1021 TKAKVKLEQQVDDLEGSLEQEKKVRMDL-ERAKRKLEGDLKLTQESIMdlendkQQLDERLKKKDFELNALNARIEDE-Q 1098
Cdd:pfam10174 184 TRRIAEAEMQLGHLEVLLDQKEKENIHLrEELHRRNQLQPDPAKTKAL------QTVIEMKDTKISSLERNIRDLEDEvQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1099 ALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSR---ELEEISERLEEAGGATS---VQIEMNKKREAEfq 1172
Cdd:pfam10174 258 MLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKkesELLALQTKLETLTNQNSdckQHIEVLKESLTA-- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1173 kmrRDLEEATLQHEATAAALRKKHADSVaeLGEQIDNLQRvkqkLEKEKSEFKLELDDVtSNMEQIIKAKAN-LEKMCRT 1251
Cdd:pfam10174 336 ---KEQRAAILQTEVDALRLRLEEKESF--LNKKTKQLQD----LTEEKSTLAGEIRDL-KDMLDVKERKINvLQKKIEN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1252 LEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLtrgkltyTQQLEDLKRQLEEEVKaknALAH 1331
Cdd:pfam10174 406 LQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERL-------KEQREREDRERLEELE---SLKK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1332 ALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKK-----KLAQRLQEAEEAVEA 1406
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKlenqlKKAHNAEEAVRTNPE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1407 VNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELfKLKN 1486
Cdd:pfam10174 556 INDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEM-KKKG 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1487 AYEESLEHLETFKRENKNLQEEISDLTEqlgssgktihELEKVRKQLEAEKMEL---QSALEEAEA---SLEHEEGKILR 1560
Cdd:pfam10174 635 AQLLEEARRREDNLADNSQQLQLEELMG----------ALEKTRQELDATKARLsstQQSLAEKDGhltNLRAERRKQLE 704
|
....*..
gi 1034587182 1561 AQLEFNQ 1567
Cdd:pfam10174 705 EILEMKQ 711
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1063-1283 |
2.57e-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: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1063 QESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRE 1142
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1143 LEEISERLEE-------AGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRkkhadsvaelgEQIDNLQRVKQ 1215
Cdd:COG4942 99 LEAQKEELAEllralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR-----------ADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587182 1216 KLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTE 1283
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1487-1934 |
3.51e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1487 AYEESLEHLETFKRENKNLQEEISDLTEQLGSSgktihelEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFN 1566
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKTETGKAEEARKAEEAKKKA-------EDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1567 qiKAEIERKlAEKDEEMEQAKRnhlrvvdSLQTSLDAETRSRNEAlrvkKKMEGDLNEMEIQLSHANRMAAEAQK--QVK 1644
Cdd:PTZ00121 1165 --KAEEARK-AEDAKKAEAARK-------AEEVRKAEELRKAEDA----RKAEAARKAEEERKAEEARKAEDAKKaeAVK 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1645 SLQSLLKDTQiqldDAVRANddlKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNtsli 1724
Cdd:PTZ00121 1231 KAEEAKKDAE----EAKKAE---EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE---- 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1725 nQKKKMDadlsqlqtEVEEAVQECRNAEEKAKKAiTDAAMMAEELKKEQdtsahlERMKKNMEQTIKDLQHRLDEAEQIA 1804
Cdd:PTZ00121 1300 -EKKKAD--------EAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKA------EEAKKAAEAAKAEAEAAADEAEAAE 1363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1805 LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQlKVKAYKRQAEE 1884
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEE 1442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1034587182 1885 AE--EQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLNE 1934
Cdd:PTZ00121 1443 AKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1038-1447 |
6.36e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1038 LEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQalgsqLQKKLKELQARIEE 1117
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-----LEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1118 LEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHA 1197
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1198 DSVAELgeqidNLQRVKQKLEKEKSEFKLE------LDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVN 1271
Cdd:COG4717 231 QLENEL-----EAAALEERLKEARLLLLIAaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1272 DLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALahALQSARHDCDLLREQY---- 1347
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAgved 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1348 EEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKK-LAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIE 1426
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeLEEELEELEEELEELEEELEELREELAELEAELE 463
|
410 420
....*....|....*....|.
gi 1034587182 1427 DLMVDVERSNAAAAALDKKQR 1447
Cdd:COG4717 464 QLEEDGELAELLQELEELKAE 484
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
837-1428 |
8.29e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 837 KPLLKSAEREKEMASMKEEFTRLKEALEKSEARRK--ELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQ 914
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRleLLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 915 LEakvkemNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTK 994
Cdd:COG4913 335 NG------GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 995 EKKALQEAHQQALDDLQAEedkVNTLTKAKVKLEQQVDDLEGSLEQEKKV---------------------RMDLERA-- 1051
Cdd:COG4913 409 EAEAALRDLRRELRELEAE---IASLERRKSNIPARLLALRDALAEALGLdeaelpfvgelievrpeeerwRGAIERVlg 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1052 ---------------------KRKLEGDL-----KLTQESIMDLENDKQQLDERLKKKD--------FELNALNARI--E 1095
Cdd:COG4913 486 gfaltllvppehyaaalrwvnRLHLRGRLvyervRTGLPDPERPRLDPDSLAGKLDFKPhpfrawleAELGRRFDYVcvD 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1096 DEQAL-----GSQLQKKLKELQARIEELEEELEAER-----TARAKVEKLRsdlsRELEEISERLEEAggatsvqiemnk 1165
Cdd:COG4913 566 SPEELrrhprAITRAGQVKGNGTRHEKDDRRRIRSRyvlgfDNRAKLAALE----AELAELEEELAEA------------ 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1166 krEAEFQKMRRDLEEATLQHEATAAALRKKHAD-SVAELGEQIDNLQRVKQKLEKEKSEFklelddvtsnmeqiikakan 1244
Cdd:COG4913 630 --EERLEALEAELDALQERREALQRLAEYSWDEiDVASAEREIAELEAELERLDASSDDL-------------------- 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1245 lekmcRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLT-RGKLTYTQQLEDLKRQLEEEv 1323
Cdd:COG4913 688 -----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdLARLELRALLEERFAAALGD- 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1324 KAKNALAHALQSARHDCDLLREQYEEETEAKaeLQRVLSKANSEVAQWRTKYET----DAI---QRTEELEEAKKKLAQR 1396
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERA--MRAFNREWPAETADLDADLESlpeyLALldrLEEDGLPEYEERFKEL 839
|
650 660 670
....*....|....*....|....*....|..
gi 1034587182 1397 LQEAEEavEAVNAKCSSLEKTKHRLQNEIEDL 1428
Cdd:COG4913 840 LNENSI--EFVADLLSKLRRAIREIKERIDPL 869
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1214-1441 |
8.90e-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: 59.78 E-value: 8.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1214 KQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDE 1293
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1294 KEALISQLTRgkltyTQQLEDLKRQLEEEVKAKNA--LAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQW 1371
Cdd:COG4942 102 QKEELAELLR-----ALYRLGRQPPLALLLSPEDFldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1372 RTKYETDAIQRtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAA 1441
Cdd:COG4942 177 EALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1668-1925 |
9.85e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 9.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1668 KENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQ-----------ELIETSERVQLLHSQNTSLINQKKKMDADLSQ 1736
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERQAEKAERYRELKEElkeleaellllKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1737 LQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLE 1816
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE-ELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1817 ARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDlvdklQLKVKAYKRQAEEAEEQANTN-LSK 1895
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR-----AAAELAAQLEELEEAEEALLErLER 418
|
250 260 270
....*....|....*....|....*....|
gi 1034587182 1896 FRKVQHELDEAEERADIAESQVNKLRAKSR 1925
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
945-1152 |
1.06e-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: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 945 DECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQeahqqalDDLQAEEDKVNTLTKAK 1024
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-------QELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1025 VKLEQQVDDLEGSLEQEKKVrmdLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQL 1104
Cdd:COG4942 93 AELRAELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034587182 1105 QKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEE 1152
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
831-1145 |
1.17e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 831 KLYFKIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIK 910
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 911 NKIQLEAKVKEMNERLedeeemnAELTAKKRKLEDEC-SELKRDIDDLE------LTLAKVEKEKHATENKVKNLTEEma 983
Cdd:PRK03918 557 KLAELEKKLDELEEEL-------AELLKELEELGFESvEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEE-- 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 984 gLDEIIAKLTKEKKALQEAHQQaLDDLQAEEDKvntltkakvkleqqvDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQ 1063
Cdd:PRK03918 628 -LDKAFEELAETEKRLEELRKE-LEELEKKYSE---------------EEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1064 ESIMDLENDKQQLDERLKKKDfELNALNARIEDEQAlgsqLQKKLKELQARIeeleeeleaERTARAKVEKLRSDLSREL 1143
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKK-ELEKLEKALERVEE----LREKVKKYKALL---------KERALSKVGEIASEIFEEL 756
|
..
gi 1034587182 1144 EE 1145
Cdd:PRK03918 757 TE 758
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1592-1894 |
1.58e-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: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1592 RVVDSLQ--TSLDAETRSRNEAL-----RVKKKMEGDLNEMEIQLSHANrmAAEAQKQVKSLQSLLKDTQIQLddavran 1664
Cdd:COG3206 98 RVVDKLNldEDPLGEEASREAAIerlrkNLTVEPVKGSNVIEISYTSPD--PELAAAVANALAEAYLEQNLEL------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1665 ddlkeNIAIVERRNNLLQAELEELRAVVEQTERSRK--LAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVE 1742
Cdd:COG3206 169 -----RREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1743 eAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNMEQTIKDLQHRLDEAEQIALKGGKKQL 1812
Cdd:COG3206 244 -ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1813 QKLEARVRELENELEAEQKRnaesVKGMRKSERRIKELTYQTEEDRKNllrLQDLVDKLQlkvkaykrQAEEAEEQANTN 1892
Cdd:COG3206 323 EALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVAREL---YESLLQRLE--------EARLAEALTVGN 387
|
..
gi 1034587182 1893 LS 1894
Cdd:COG3206 388 VR 389
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
853-1428 |
3.53e-08 |
|
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: 58.81 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 853 KEEFTRLKEALEK--SEARRKELEEKMVSLLQEKNDLQLQVQAEQD---NLADAEERCDQLIKNKIQLEAKVKEMNERLE 927
Cdd:COG3096 471 RRQFEKAYELVCKiaGEVERSQAWQTARELLRRYRSQQALAQRLQQlraQLAELEQRLRQQQNAERLLEEFCQRIGQQLD 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 928 DEEEmnaeltakkrkLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL----------DEIIAKLTKE-- 995
Cdd:COG3096 551 AAEE-----------LEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELaarapawlaaQDALERLREQsg 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 996 -----KKALQEAHQQALDD---LQAEEDKvntLTKAKVKLEQQV------------------------------DD---- 1033
Cdd:COG3096 620 ealadSQEVTAAMQQLLERereATVERDE---LAARKQALESQIerlsqpggaedprllalaerlggvllseiyDDvtle 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1034 -------LEGSLEQEKKVRmDLERAKRKLEGdLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQK 1106
Cdd:COG3096 697 dapyfsaLYGPARHAIVVP-DLSAVKEQLAG-LEDCPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSDRQWRYSRFPE 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1107 klkelqarieeleeeleAERTARAKVEKLRSDLSRELEEISERLEEAggATSVQiemnkkreaEFQKMRRDLEEATLQH- 1185
Cdd:COG3096 775 -----------------VPLFGRAAREKRLEELRAERDELAEQYAKA--SFDVQ---------KLQRLHQAFSQFVGGHl 826
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1186 --------EATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKL--------ELDDVTSNMEQIIKAKANLEKmC 1249
Cdd:COG3096 827 avafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLlnkllpqaNLLADETLADRLEELREELDA-A 905
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1250 RTLEDQMNEHRSKAEETQRSVNDLTS---QRAKLQTENGELSRQLDEKEALISQLT-----RGKLTYtqqlEDLKRQLEE 1321
Cdd:COG3096 906 QEAQAFIQQHGKALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSevvqrRPHFSY----EDAVGLLGE 981
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1322 EVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSevaQWRTKYET--DAIQRTEELE-----EAKKKLA 1394
Cdd:COG3096 982 NSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKS---SRDAKQQTlqELEQELEELGvqadaEAEERAR 1058
|
650 660 670
....*....|....*....|....*....|....
gi 1034587182 1395 QRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDL 1428
Cdd:COG3096 1059 IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSL 1092
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1647-1897 |
3.54e-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: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1647 QSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQllhsqntSLINQ 1726
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1727 KKKMDADLSQLQTEVEEAVqecRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQI--A 1804
Cdd:COG4942 92 IAELRAELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALraE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1805 LKGGKKQLQKLEARVRELENELEAEQKRNAESVKgmrKSERRIKELTYQTEEDRKNLLRLQDLVDKLQlkvkayKRQAEE 1884
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLE------AEAAAA 239
|
250
....*....|...
gi 1034587182 1885 AEEQANTNLSKFR 1897
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
861-1082 |
3.76e-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: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 861 EALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKK 940
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 941 RKLEDECSELKRDIddleltlakvekEKHATENKVKNLT-----EEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEED 1015
Cdd:COG4942 100 EAQKEELAELLRAL------------YRLGRQPPLALLLspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587182 1016 KVNTLTKAKVKLEQQVDDLEGSLEQEKKVRmdlERAKRKLEGDLKLTQESIMDLENDKQQLDERLKK 1082
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1681-1928 |
4.66e-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: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1681 LQAELEELRAVVEQteRSRKLaEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEavQECRNAEEKAKKAIT 1760
Cdd:pfam01576 55 LCAEAEEMRARLAA--RKQEL-EEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE--EEAARQKLQLEKVTT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1761 DAAM--MAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlKGGKKQLQKLEARVRELENELEAEQKRNAESVK 1838
Cdd:pfam01576 130 EAKIkkLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA-KSLSKLKNKHEAMISDLEERLKKEEKGRQELEK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1839 GMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVN 1918
Cdd:pfam01576 209 AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN 288
|
250
....*....|
gi 1034587182 1919 KLRAKSRDIG 1928
Cdd:pfam01576 289 KAEKQRRDLG 298
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1010-1223 |
6.26e-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: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1010 LQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNA 1089
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1090 LNARIEDEQALGSQLQKKL--KELQARIEELEEELEAERTARA-----KVEKLRSDLSRELEEISERLEEAGGATSVQIE 1162
Cdd:COG4942 95 LRAELEAQKEELAELLRALyrLGRQPPLALLLSPEDFLDAVRRlqylkYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034587182 1163 MNKKREAEFQKMRRDLEEATLQHEATAAALRKK---HADSVAELGEQIDNLQRVKQKLEKEKSE 1223
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKElaeLAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1240-1921 |
6.49e-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: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1240 KAKANLEKMCRTLEDQ-----MNEHRSKAEETQRSVNDLTSQRAKLQTengeLSRQLDEKEALISQLTRGKLTYTQQLED 1314
Cdd:pfam12128 215 KSRLNRQQVEHWIRDIqaiagIMKIRPEFTKLQQEFNTLESAELRLSH----LHFGYKSDETLIASRQEERQETSAELNQ 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1315 LKRQLEEEVKAK--------NALAHALQSARHDCDLLREQYEEETEAKAElqrVLSKANSEVAQWRTKyetdaiqrTEEL 1386
Cdd:pfam12128 291 LLRTLDDQWKEKrdelngelSAADAAVAKDRSELEALEDQHGAFLDADIE---TAAADQEQLPSWQSE--------LENL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1387 EEAKKKLAQRLQEAEEAVEAVNAKCSSlektkhRLQNEIEDLMVDVERSNAAAAALDKKQRN-FDKILAEWKQKYEESQS 1465
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKE------QNNRDIAGIKDKLAKIREARDRQLAVAEDdLQALESELREQLEAGKL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1466 ELESSQKEARSLSTELFKLKN---AYEESLEHLETFkrenknlQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQS 1542
Cdd:pfam12128 434 EFNEEEYRLKSRLGELKLRLNqatATPELLLQLENF-------DERIERAREEQEAANAEVERLQSELRQARKRRDQASE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1543 ALEEAEASLEHEEGKILRAQ----------LEFNQIKAEIERKLAEKDEEMEQAKRNHLR-VVDSLQTS---------LD 1602
Cdd:pfam12128 507 ALRQASRRLEERQSALDELElqlfpqagtlLHFLRKEAPDWEQSIGKVISPELLHRTDLDpEVWDGSVGgelnlygvkLD 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1603 AETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRAnddLKENIAIVERRNNLLQ 1682
Cdd:pfam12128 587 LKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA---LKNARLDLRRLFDEKQ 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1683 AELeelRAVVEQTERSRKLAEqelietsERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAiTDA 1762
Cdd:pfam12128 664 SEK---DKKNKALAERKDSAN-------ERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDA-QLA 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1763 AMMAEELKKEQDTSAHLERMKKNMEqtiKDLQHRLDEAEQIAlkggkkqlqKLEARVRELENELEAEQKRNAESVKGMRK 1842
Cdd:pfam12128 733 LLKAAIAARRSGAKAELKALETWYK---RDLASLGVDPDVIA---------KLKREIRTLERKIERIAVRRQEVLRYFDW 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1843 SERRI----KELTYQTEEDRKNLLRLQDLVDKLQLKVKAyKRQAEEAEEQANtnlskfRKVQHELDEAEERADIAESQVN 1918
Cdd:pfam12128 801 YQETWlqrrPRLATQLSNIERAISELQQQLARLIADTKL-RRAKLEMERKAS------EKQQVRLSENLRGLRCEMSKLA 873
|
...
gi 1034587182 1919 KLR 1921
Cdd:pfam12128 874 TLK 876
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1356-1930 |
8.63e-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: 57.34 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1356 ELQRVLSKANSEVA---QWRTKYETDAIQRTEELEEAKKKLAQRLQE---AEEAVEAVNAKCSSLEKTKHRLQNEIEDLM 1429
Cdd:TIGR04523 100 KLNSDLSKINSEIKndkEQKNKLEVELNKLEKQKKENKKNIDKFLTEikkKEKELEKLNNKYNDLKKQKEELENELNLLE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1430 VDversnaaaaaLDKKQRNFDKILAEWKQKYEESQSELESSQKEaRSLSTELFKLKNAYEESLEHLETFKRENKNLQEEI 1509
Cdd:TIGR04523 180 KE----------KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1510 SDLTEQLGSsgkTIHELEKVRKQLEAEKMELQSAleeaeasleheEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRN 1589
Cdd:TIGR04523 249 SNTQTQLNQ---LKDEQNKIKKQLSEKQKELEQN-----------NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1590 HLRVVDS----LQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRAND 1665
Cdd:TIGR04523 315 ELKNQEKkleeIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1666 DLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAV 1745
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1746 QECRNAEEKAKKaitdaamMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDE--AEQIALKGGKKQLQK--------- 1814
Cdd:TIGR04523 475 RSINKIKQNLEQ-------KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSlkEKIEKLESEKKEKESkisdledel 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1815 -----------LEARVRELENELEaEQKRNAESVKgmrKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVkayKRQAE 1883
Cdd:TIGR04523 548 nkddfelkkenLEKEIDEKNKEIE-ELKQTQKSLK---KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL---EKELE 620
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1034587182 1884 EAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTK 1930
Cdd:TIGR04523 621 KAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKK 667
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
851-1033 |
9.40e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.93 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 851 SMKEEFTRLKEaLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLE-DE 929
Cdd:COG1579 1 AMPEDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 930 EEMNAELTAKKRK-LEDECSELKRDIDDLEltlakvEKEKHATEnKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALD 1008
Cdd:COG1579 80 EQLGNVRNNKEYEaLQKEIESLKRRISDLE------DEILELME-RIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180
....*....|....*....|....*
gi 1034587182 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, ... |
1240-1455 |
9.96e-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: 56.31 E-value: 9.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1240 KAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQL 1319
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1320 EEEVKA-KNALAHALQSARHDCDLLREQYEEETEAKAELQRVlskanSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQ 1398
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL-----KYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587182 1399 EAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAE 1455
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1185-1926 |
1.05e-07 |
|
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: 57.54 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1185 HEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAE 1264
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1265 etqrsvNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQsarhdcDLLR 1344
Cdd:pfam12128 308 ------GELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQ------DVTA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1345 EQYEEETEAKAELQRVLSKANSEVAQwrtKYETDAIQRTEElEEAKKKLAQRLQEAEEAVEAvnakcsSLEKTKHRLQNE 1424
Cdd:pfam12128 376 KYNRRRSKIKEQNNRDIAGIKDKLAK---IREARDRQLAVA-EDDLQALESELREQLEAGKL------EFNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1425 IEDLMVdveRSNAAAAALDKK--QRNFDKILAEWKQKyeesqseLESSQKEARSLSTELFKLKNAYEESLEHLETFKREN 1502
Cdd:pfam12128 446 LGELKL---RLNQATATPELLlqLENFDERIERAREE-------QEAANAEVERLQSELRQARKRRDQASEALRQASRRL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1503 KNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAE---KMELQSALEEAEASLEHEEGKIlRAQLEFNQIKAEIERKLAEK 1579
Cdd:pfam12128 516 EERQSALDELELQLFPQAGTLLHFLRKEAPDWEQsigKVISPELLHRTDLDPEVWDGSV-GGELNLYGVKLDLKRIDVPE 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1580 DEEMEQAKRNHLrvvDSLQTSLDAEtRSRNEALrvkkkmegdlnemEIQLSHANRMAAEAQKQVKSLQSLLK---DTQIQ 1656
Cdd:pfam12128 595 WAASEEELRERL---DKAEEALQSA-REKQAAA-------------EEQLVQANGELEKASREETFARTALKnarLDLRR 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1657 LDDAVRANDDLKENiaIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETServqllhSQNTSLINQKKK-----MD 1731
Cdd:pfam12128 658 LFDEKQSEKDKKNK--ALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQK-------REARTEKQAYWQvvegaLD 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1732 ADLSQLQTEVeEAVQECRNAEEKAKKaitdaAMMAEELKK---EQDTSAHLERMKKNMEQTIKDLQHRLDEA---EQIAL 1805
Cdd:pfam12128 729 AQLALLKAAI-AARRSGAKAELKALE-----TWYKRDLASlgvDPDVIAKLKREIRTLERKIERIAVRRQEVlryFDWYQ 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1806 KGGKKQLQKLEARVRELEN---ELEAEQKRNAESVKgmrkseRRIKELtyqtEEDRKNLLRLQDLVDKLQLKVKAYKRQA 1882
Cdd:pfam12128 803 ETWLQRRPRLATQLSNIERaisELQQQLARLIADTK------LRRAKL----EMERKASEKQQVRLSENLRGLRCEMSKL 872
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1034587182 1883 EEAEEQANTNlSKFRKVQHELDEAEERADIAESQVNKLRAKSRD 1926
Cdd:pfam12128 873 ATLKEDANSE-QAQGSIGERLAQLEDLKLKRDYLSESVKKYVEH 915
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
833-1283 |
1.23e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 56.77 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 833 YFKIKPLLKSAER-----EKEMASMKEEFTRLKEALEKSEARRKELEEKMvsllqekNDLQLQVQAEQDNLADAEErcdq 907
Cdd:PRK04778 100 FRKAKHEINEIESlldliEEDIEQILEELQELLESEEKNREEVEQLKDLY-------RELRKSLLANRFSFGPALD---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 908 liknkiQLEAKVKEMNERLEDEEEMNAE---LTAKK--RKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKN----L 978
Cdd:PRK04778 169 ------ELEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 979 TEEMAGLDEIiaKLTKEKKALQEAHQQALDDLQAEEdkvntLTKAKVKLEQ---QVDDLEGSLEQEKKVRMDLERAKRKL 1055
Cdd:PRK04778 243 VEEGYHLDHL--DIEKEIQDLKEQIDENLALLEELD-----LDEAEEKNEEiqeRIDQLYDILEREVKARKYVEKNSDTL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1056 EGDLKLTQESIMDLENDKQQLDERlkkkdFELNalnariEDEQALGSQLQKKLKELQARIEELEEELeaertarAKVEKL 1135
Cdd:PRK04778 316 PDFLEHAKEQNKELKEEIDRVKQS-----YTLN------ESELESVRQLEKQLESLEKQYDEITERI-------AEQEIA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1136 RSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsvaelgeqidnLQRVKQ 1215
Cdd:PRK04778 378 YSELQEELEEILKQLEEI-----------EKEQEKLSEMLQGLRKDELEAREKLERYRNK--------------LHEIKR 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034587182 1216 KLEKEK-----SEFKLELDDVTSNMEQiikakanlekmcrtLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTE 1283
Cdd:PRK04778 433 YLEKSNlpglpEDYLEMFFEVSDEIEA--------------LAEELEEKPINMEAVNRLLEEATEDVETLEEE 491
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
833-1408 |
1.26e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.83 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 833 YFKIKPLLKSAERE-KEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQA---EQDNLADAEERCDQL 908
Cdd:PRK01156 168 YDKLKDVIDMLRAEiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNamdDYNNLKSALNELSSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 909 IKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLedecselkrdiddLELTLAKVEKEKHATeNKVKNLTEEMAGLDEI 988
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYKELEERH-------------MKIINDPVYKNRNYI-NDYFKYKNDIENKKQI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 989 IAKLTKEKKALQEAHQQaLDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSleqekkvRMDLERAKRKLEGDLKLTQESIMD 1068
Cdd:PRK01156 314 LSNIDAEINKYHAIIKK-LSVLQKDYNDYIKKKSRYDDLNNQILELEGY-------EMDYNSYLKSIESLKKKIEEYSKN 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1069 LENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARA------------------ 1130
Cdd:PRK01156 386 IERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlgee 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1131 KVEKLRSDLSRELEEISE---RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQI 1207
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEkirEIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKH 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1208 DnlqrvkqKLEKEKSEFK-LELDDVTSNMEQIIKAKANLEKM-CRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENG 1285
Cdd:PRK01156 546 D-------KYEEIKNRYKsLKLEDLDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYID 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1286 ELSRQLDEKealiSQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKAN 1365
Cdd:PRK01156 619 KSIREIENE----ANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAK 694
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1034587182 1366 SEVAQWRTKYETDaIQRTEELEEAKKKLAQRLQEAEEAVEAVN 1408
Cdd:PRK01156 695 ANRARLESTIEIL-RTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
839-1056 |
1.37e-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: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 839 LLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAK 918
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 919 VKEMNERLEDEEEMNAELTAKKRKLEDEcSELK-----RDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 993
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQ-PPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034587182 994 KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLE 1056
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
929-1424 |
1.52e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 929 EEEMNAELTAKKRKLEDECSELKRDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALqEAHQQALD 1008
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1009 DLQAEEDKVNTLTKAKVKLEQqvddlegsLEQEKKVRMDLERAKRKLEGDLKLTQESI-MDLENDKQQLDERLKKKDFEL 1087
Cdd:COG4717 130 LYQELEALEAELAELPERLEE--------LEERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1088 NALNARIEDEQALGSQLQKKLKELQARIEeleeeleaertaRAKVEKLRSDLSRELEEISERLEEAGG-----ATSVQIE 1162
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELE------------QLENELEAAALEERLKEARLLLLIAAAllallGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1163 MNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQID----NLQRVKQKLEKEKSEFKLELDDVTSNMEQI 1238
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleeeELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1239 IKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQtengelsrQLDEKEALisqltrgkltyTQQLEDLKRQ 1318
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALE--------QAEEYQEL-----------KEELEELEEQ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1319 LEEEVKAKNALAhalqsARHDCDLLREQYEEETEAKAELQRVLSKANSEVAqwRTKYETDAIQRTEELEEAKKKLAQRLQ 1398
Cdd:COG4717 411 LEELLGELEELL-----EALDEEELEEELEELEEELEELEEELEELREELA--ELEAELEQLEEDGELAELLQELEELKA 483
|
490 500
....*....|....*....|....*....
gi 1034587182 1399 EAEEAVEAVNAKC---SSLEKTKHRLQNE 1424
Cdd:COG4717 484 ELRELAEEWAALKlalELLEEAREEYREE 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1317-1775 |
1.53e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1317 RQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWrtkyetDAIQRTEELEEAKKKLAQR 1396
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL------PLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1397 LQEAEEAVEAVN---AKCSSLEKTKHRLQNEIEDLMVDVerSNAAAAALDKKQRNFDKILAEWKQkyeesqselesSQKE 1473
Cdd:COG4717 148 LEELEERLEELReleEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEELEELQQRLAE-----------LEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1474 ARSLSTELfklkNAYEESLEHLETfKRENKNLQEEISDLTEQLGSSGkTIHELEKVRKQLEAEKMELQSALEEAEASLEH 1553
Cdd:COG4717 215 LEEAQEEL----EELEEELEQLEN-ELEAAALEERLKEARLLLLIAA-ALLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1554 EEGKILRAQLEFNQIKAEIERKLAEKDEEMEQakrnhlrvVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHAN 1633
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEE--------LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1634 RmAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLA---------EQ 1704
Cdd:COG4717 361 E-ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeleeeleelEE 439
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034587182 1705 ELIETSERVQLLHSQNTSLINQKKKM--DADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT 1775
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
651-675 |
2.03e-07 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 52.73 E-value: 2.03e-07
10 20
....*....|....*....|....*
gi 1034587182 651 HRENLNKLMTNLRSTHPHFVRCIIP 675
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
859-1874 |
2.20e-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: 56.60 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 859 LKEALEKSEARRKeLEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIK--NKIQLEAKVKEMNerLEDEEEMNAEL 936
Cdd:TIGR01612 546 LKESYELAKNWKK-LIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIyiNKLKLELKEKIKN--ISDKNEYIKKA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 937 TAKKRKLEDECSElkrdIDDleltLAKVEKEKhatenkvknLTEEMAGLDEIIAKLTKEkkaLQEAHQQALDDLQ----- 1011
Cdd:TIGR01612 623 IDLKKIIENNNAY----IDE----LAKISPYQ---------VPEHLKNKDKIYSTIKSE---LSKIYEDDIDALYnelss 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1012 --AEEDKVNTLTKAKvkleqqVDDLEGSLEQEKKVRMDLERAKRKLegdlkltqeSIMDLENDKQQLDE---RLKKKDF- 1085
Cdd:TIGR01612 683 ivKENAIDNTEDKAK------LDDLKSKIDKEYDKIQNMETATVEL---------HLSNIENKKNELLDiivEIKKHIHg 747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1086 ELNA-LNARIEDeqalgsqLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMN 1164
Cdd:TIGR01612 748 EINKdLNKILED-------FKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYI 820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1165 KK---REAEFQKM---RRDLEEATLQHEATAAALRKKHADSVAELGEQIDNL-QRVKQKLEKEK-SEFKLELDDVTSNME 1236
Cdd:TIGR01612 821 KTisiKEDEIFKIineMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELtNKIKAEISDDKlNDYEKKFNDSKSLIN 900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1237 QIIKAKANLEKMCRTLEdQMNEHRSKAEETQRSVNDLTSQRAKL------------QTENGELSRQLDEKEALISQLTRG 1304
Cdd:TIGR01612 901 EINKSIEEEYQNINTLK-KVDEYIKICENTKESIEKFHNKQNILkeilnknidtikESNLIEKSYKDKFDNTLIDKINEL 979
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1305 KLTYTQ-QLEDLKRQLEEEVKAKNALAHALQSARHdcDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRT 1383
Cdd:TIGR01612 980 DKAFKDaSLNDYEAKNNELIKYFNDLKANLGKNKE--NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNII 1057
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1384 EELEEAKKKLAQRLQeaEEAVEAVNAKCSSLEKTKHRLQ----------------NEIEDLMVDVErsnaaaaALDKKQR 1447
Cdd:TIGR01612 1058 DEIEKEIGKNIELLN--KEILEEAEINITNFNEIKEKLKhynfddfgkeenikyaDEINKIKDDIK-------NLDQKID 1128
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1448 NFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKN--AYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHE 1525
Cdd:TIGR01612 1129 HHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDpeEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTS 1208
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1526 LEKVR---------------KQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKlaekdEEMEQAKRNH 1590
Cdd:TIGR01612 1209 LEEVKginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIK-----AEMETFNISH 1283
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1591 LRVVDSLQTSLDAE---TRSRNEALRVKKKM--EGDLNEMEIQLshaNRMAAEAQKQVKSLQSLLKDTQ-----IQLDDA 1660
Cdd:TIGR01612 1284 DDDKDHHIISKKHDeniSDIREKSLKIIEDFseESDINDIKKEL---QKNLLDAQKHNSDINLYLNEIAniyniLKLNKI 1360
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1661 VRANDDLKENIAIVERRNNLLQAE----------------LEELRAVVEQTERSRKLAE--QELIETSERVQLLHSQNTS 1722
Cdd:TIGR01612 1361 KKIIDEVKEYTKEIEENNKNIKDEldkseklikkikddinLEECKSKIESTLDDKDIDEciKKIKELKNHILSEESNIDT 1440
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1723 LINQKKKMDADLSQLQTEVEEAVQECRN-AEEKAKKAITDAAMMAEELKKEQDTS-----------AHLERMKKNMEQTI 1790
Cdd:TIGR01612 1441 YFKNADENNENVLLLFKNIEMADNKSQHiLKIKKDNATNDHDFNINELKEHIDKSkgckdeadknaKAIEKNKELFEQYK 1520
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1791 KDLQHRLDEAEQIALKGG----KKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQD 1866
Cdd:TIGR01612 1521 KDVTELLNKYSALAIKNKfaktKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQL 1600
|
....*...
gi 1034587182 1867 LVDKLQLK 1874
Cdd:TIGR01612 1601 SLENFENK 1608
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
847-1447 |
2.20e-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: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 847 KEMASMKEEFTRLKEALEKSEARRKELEEKMVS------LLQEKNDLQLQVQAEQDNLADAEERcdqliknkiqLEakvk 920
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAasdhlnLVQTALRQQEKIERYQEDLEELTER----------LE---- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 921 EMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDL-------------------------------ELTLAKVEKEKH 969
Cdd:COG3096 365 EQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYqqaldvqqtraiqyqqavqalekaralcglpDLTPENAEDYLA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 970 ATENKVKNLTEEMAGLDE--IIAKLTKEK--KALQ------------EAHQQALDDLQAEEDKVNTLTKAkVKLEQQVDD 1033
Cdd:COG3096 445 AFRAKEQQATEEVLELEQklSVADAARRQfeKAYElvckiageversQAWQTARELLRRYRSQQALAQRL-QQLRAQLAE 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1034 LEGSLEQEKKVRMDLERAKRKLEGDLkltqESIMDLENDKQQLDERLKKkdfelnaLNARIEDEQALGSQLQKKLKELQA 1113
Cdd:COG3096 524 LEQRLRQQQNAERLLEEFCQRIGQQL----DAAEELEELLAELEAQLEE-------LEEQAAEAVEQRSELRQQLEQLRA 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1114 RIEELEEELEAERTARAKVEKLRsdlsrelEEISERLEEAGGATS-VQIEMNKKREAEFQKmrrdlEEATLQHEATAAAL 1192
Cdd:COG3096 593 RIKELAARAPAWLAAQDALERLR-------EQSGEALADSQEVTAaMQQLLEREREATVER-----DELAARKQALESQI 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1193 RKKHADSVAE------LGEQ---------------------------------IDNLQRVKQKL---------------- 1217
Cdd:COG3096 661 ERLSQPGGAEdprllaLAERlggvllseiyddvtledapyfsalygparhaivVPDLSAVKEQLagledcpedlyliegd 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1218 -------------------------------------------EKEKSEFKLELDDVTsnmEQIIKAKANLEKMCRTLED 1254
Cdd:COG3096 741 pdsfddsvfdaeeledavvvklsdrqwrysrfpevplfgraarEKRLEELRAERDELA---EQYAKASFDVQKLQRLHQA 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1255 -------------------QMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTrgkL----TYTQQ 1311
Cdd:COG3096 818 fsqfvgghlavafapdpeaELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAN---LladeTLADR 894
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1312 LEDLKRQLEEEVKAKNALAH-------------ALQSARHDCDLLREQYEeetEAKAELQRVLSK--ANSEVAQWRT--K 1374
Cdd:COG3096 895 LEELREELDAAQEAQAFIQQhgkalaqleplvaVLQSDPEQFEQLQADYL---QAKEQQRRLKQQifALSEVVQRRPhfS 971
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1375 YEtDAIQRTEELEEAKKKLAQRLQEAE-------EAVEAVNAKCS-------SLeKTKHR--------LQNEIEDLMVDV 1432
Cdd:COG3096 972 YE-DAVGLLGENSDLNEKLRARLEQAEearrearEQLRQAQAQYSqynqvlaSL-KSSRDakqqtlqeLEQELEELGVQA 1049
|
810
....*....|....*
gi 1034587182 1433 ErSNAAAAALDKKQR 1447
Cdd:COG3096 1050 D-AEAEERARIRRDE 1063
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1481-1927 |
2.26e-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: 55.63 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1481 LFKLKNAYEEsLEHLETFKRE--NKNLQEEISDLtEQLGSSGKTIHELEKVRKQ---LEAEKM-ELQSALEEAEASLEhe 1554
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddIVTKSLpDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1555 EGKILRAQLEFNqikaEIERKLAEKDEEMEQakrnhlrVVDSLQTSLDAETRSRNEALRVKKK----------------- 1617
Cdd:pfam06160 78 KYRFKKAKKALD----EIEELLDDIEEDIKQ-------ILEELDELLESEEKNREEVEELKDKyrelrktllanrfsygp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1618 ----MEGDLNEMEIQLSHA-NRMAA----EAQKQVKSLQSLLKDTQIQLDDavranddlkenI-AIVERRNNLLQAELEE 1687
Cdd:pfam06160 147 aideLEKQLAEIEEEFSQFeELTESgdylEAREVLEKLEEETDALEELMED-----------IpPLYEELKTELPDQLEE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1688 LRAVVEQTERSR-KLAEQELIETSERVQLLHSQNTSLINQK--KKMDADLSQLQTEVEEaVQECRNAEEKAKKaitdaam 1764
Cdd:pfam06160 216 LKEGYREMEEEGyALEHLNVDKEIQQLEEQLEENLALLENLelDEAEEALEEIEERIDQ-LYDLLEKEVDAKK------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1765 maeELKKEQDT-SAHLERMKKNMEQTIKDLQH-----RLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVK 1838
Cdd:pfam06160 288 ---YVEKNLPEiEDYLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1839 GMRKSERRIKELTYQTEEDRKNL-------LRLQDLVDKLQLKVKAYKRQAE----------------EAEEQANTNLSK 1895
Cdd:pfam06160 365 ELEEILEQLEEIEEEQEEFKESLqslrkdeLEAREKLDEFKLELREIKRLVEksnlpglpesyldyffDVSDEIEDLADE 444
|
490 500 510
....*....|....*....|....*....|..
gi 1034587182 1896 FRKVQHELDEAEERADIAESQVNKLRAKSRDI 1927
Cdd:pfam06160 445 LNEVPLNMDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
840-1097 |
2.46e-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: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 840 LKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLlqeknDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKV 919
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 920 KEMNERLEDEEEMNAELTAkkrklEDECSELKRDIDDLELTLAkvEKEKHATEN--KVKNLTEEMAGLdeiiakltkeKK 997
Cdd:COG3206 243 AALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL----------RA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 998 ALQEAHQQALDDLQAEedkVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRklegDLKLTQESIMDLENDKQQLD 1077
Cdd:COG3206 306 QLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLER----EVEVARELYESLLQRLEEAR 378
|
250 260
....*....|....*....|
gi 1034587182 1078 ERLkkkdfELNALNARIEDE 1097
Cdd:COG3206 379 LAE-----ALTVGNVRVIDP 393
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
854-1231 |
2.62e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.06 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 854 EEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIK----NKIQLEAKVKEMNERLEDE 929
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKiqeiDPDAIKKELNEINVKLQDI 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 930 EEMNAELTAKKRKLEDECSELKRD-------------------------IDDLELTLAKVEKEKHATENKVKNLTEEMAG 984
Cdd:PRK01156 422 SSKVSSLNQRIRALRENLDELSRNmemlngqsvcpvcgttlgeeksnhiINHYNEKKSRLEEKIREIEIEVKDIDEKIVD 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 985 LDEIIAKLTKEKKALQEAHQQALDDLQAE----EDKVNTLTKAKVKLEQ--------QVDDLEGSLEQEKK--------- 1043
Cdd:PRK01156 502 LKKRKEYLESEEINKSINEYNKIESARADlediKIKINELKDKHDKYEEiknrykslKLEDLDSKRTSWLNalavislid 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1044 ---VRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNAR---IEDEQALGSQLQKKLKELQARIEE 1117
Cdd:PRK01156 582 ietNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKyneIQENKILIEKLRGKIDNYKKQIAE 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1118 LEEELEAERTARAKVEKLRSDL---SRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRK 1194
Cdd:PRK01156 662 IDSIIPDLKEITSRINDIEDNLkksRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRL 741
|
410 420 430
....*....|....*....|....*....|....*....
gi 1034587182 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 ... |
1139-1791 |
2.63e-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: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1139 LSRELEEISERLEEaggaTSVQIEMNKKR-EAEFQKMRRDLEeaTLQHEATAAALRKKHADSVAELGE---QIDNLQRVK 1214
Cdd:pfam10174 128 QAKELFLLRKTLEE----MELRIETQKQTlGARDESIKKLLE--MLQSKGLPKKSGEEDWERTRRIAEaemQLGHLEVLL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1215 QKLEKEKSEFKLEL---------DDVTSNMEQIIKAK----ANLEKMCRTLEDQMNEHRSKA-------EETQRSVNDLT 1274
Cdd:pfam10174 202 DQKEKENIHLREELhrrnqlqpdPAKTKALQTVIEMKdtkiSSLERNIRDLEDEVQMLKTNGllhtedrEEEIKQMEVYK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1275 SQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLE---EEVKAKNALAHALQSarhDCDLLREQYEEEt 1351
Cdd:pfam10174 282 SHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEvlkESLTAKEQRAAILQT---EVDALRLRLEEK- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1352 eakaelQRVLSKansevaqwrtkyETDAIQRteeLEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVD 1431
Cdd:pfam10174 358 ------ESFLNK------------KTKQLQD---LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1432 VERSNAAAAALDKKQRNFDKILAEWKQKyEESQSELESSQKEARSLSTElfklknayeESLEHLETFKRENKNLQEEISD 1511
Cdd:pfam10174 417 LAGLKERVKSLQTDSSNTDTALTTLEEA-LSEKERIIERLKEQREREDR---------ERLEELESLKKENKDLKEKVSA 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1512 LTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEH--EEGKILRAQLEFNQIKAEIERK---LAEKDEEMEQA 1586
Cdd:pfam10174 487 LQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQkkEECSKLENQLKKAHNAEEAVRTnpeINDRIRLLEQE 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1587 KRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQ-LDDAVRAND 1665
Cdd:pfam10174 567 VARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQlLEEARRRED 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1666 DLKENIAiverrnnllQAELEELRAVVEQTersrklaEQELIETSERV----QLLHSQNTSLINQKKKMDADLSqlqtEV 1741
Cdd:pfam10174 647 NLADNSQ---------QLQLEELMGALEKT-------RQELDATKARLsstqQSLAEKDGHLTNLRAERRKQLE----EI 706
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 1742 EEAVQECRNAEEKAKKA-ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIK 1791
Cdd:pfam10174 707 LEMKQEALLAAISEKDAnIALLELSSSKKKKTQEEVMALKREKDRLVHQLK 757
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
921-1339 |
3.10e-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: 55.07 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 921 EMNERLEDEEEMNAELTAKKRKLEDECSEL---KRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKK 997
Cdd:pfam19220 14 EMADRLEDLRSLKADFSQLIEPIEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 998 ALQEAHQQAldDLQAEEDKVNTLTKakvklEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLD 1077
Cdd:pfam19220 94 KLEAALREA--EAAKEELRIELRDK-----TAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1078 ERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARieeleeeleaERTARAKVEKLRSDLSRELEEiSERLEEAggat 1157
Cdd:pfam19220 167 ERLALLEQENRRLQALSEEQAAELAELTRRLAELETQ----------LDATRARLRALEGQLAAEQAE-RERAEAQ---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1158 svqiemnkkreaefqkmrRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRvKQKLEKEKSEFKLElddvtSNMEQ 1237
Cdd:pfam19220 232 ------------------LEEAVEAHRAERASLRMKLEALTARAAATEQLLAEAR-NQLRDRDEAIRAAE-----RRLKE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1238 IIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKL----QTENGELSRQLDEKEAL---ISQLTR----GKL 1306
Cdd:pfam19220 288 ASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLtkalAAKDAALERAEERIASLsdrIAELTKrfevERA 367
|
410 420 430
....*....|....*....|....*....|....
gi 1034587182 1307 TYTQQLEDLKRQLEEEvKAKNALAH-ALQSARHD 1339
Cdd:pfam19220 368 ALEQANRRLKEELQRE-RAERALAQgALEIARES 400
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1619-1836 |
3.19e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1619 EGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERS 1698
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1699 rklAEQELIETSERVQLLHSQNTS-LINQKKKMDAdLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsa 1777
Cdd:COG3883 95 ---LYRSGGSVSYLDVLLGSESFSdFLDRLSALSK-IADADADLLEELKADKAELEAKKAELEAKLAELEALKAE----- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034587182 1778 hLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENELEAEQKRNAES 1836
Cdd:COG3883 166 -LEAAKAELEAQQAEQEALLAQLSA--------EEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
841-1277 |
3.28e-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: 55.50 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 841 KSAEREkEMASMKE----EFTRLKEALEKSEA---RRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKI 913
Cdd:pfam05483 389 KSSELE-EMTKFKNnkevELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 914 QLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 993
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 994 KEKKALQEAHQQALDDLQAEEDKVntltkakvklEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDK 1073
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLDKS----------EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1074 QQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELqarieeleeeleaERTARAKVEKLRSDLSRELEEISERLEEA 1153
Cdd:pfam05483 618 KALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEI-------------IDNYQKEIEDKKISEEKLLEEVEKAKAIA 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1154 GGATSVQIEMNKKREAEFQKMrrdleeatlqheataAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTS 1233
Cdd:pfam05483 685 DEAVKLQKEIDKRCQHKIAEM---------------VALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELS 749
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1034587182 1234 NMeqiikaKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQR 1277
Cdd:pfam05483 750 NI------KAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1668-1933 |
3.57e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1668 KENIAIVERRNNLLQAELEELRAVVE--QTERSRKLAEQELIETSERVQLlhsqnTSLINQKKKMDADLSQLQTEVEEAV 1745
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKREYEG-----YELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1746 QEcrnaEEKAKKAITDAAMMAEELKKEQDTSAhlERMKKNMEQTIKDLQHRLDEAEqialkggkKQLQKLEARVRELENE 1825
Cdd:TIGR02169 251 EE----LEKLTEEISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGELE--------AEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1826 LEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDE 1905
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
|
250 260
....*....|....*....|....*...
gi 1034587182 1906 AEERADIAESQVNKLRAKSRDIGTKGLN 1933
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELAD 424
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1351-1587 |
4.99e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1351 TEAKAELQRVLSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMv 1430
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE--------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1431 dvERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEIS 1510
Cdd:COG4942 90 --KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587182 1511 DLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAK 1587
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
846-1013 |
5.18e-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: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 846 EKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKiQLEAKVKEMner 925
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKEI--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 926 ledeeemnAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKhatENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQ 1005
Cdd:COG1579 99 --------ESLKRRISDLEDEILELMERIEELEEELAELEAEL---AELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
....*...
gi 1034587182 1006 ALDDLQAE 1013
Cdd:COG1579 168 LAAKIPPE 175
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1001-1162 |
6.18e-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: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1001 EAHQQALDDLQAEEDKVNTLTKAK-------VKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESImdlENDK 1073
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLkelpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI---KKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1074 QQLDERLKKKdfELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEA 1153
Cdd:COG1579 80 EQLGNVRNNK--EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
....*....
gi 1034587182 1154 GGATSVQIE 1162
Cdd:COG1579 158 LEELEAERE 166
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
835-1200 |
8.52e-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: 54.35 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 835 KIKPLLKSAEREKEM-ASMKEEFTRLKEALEKSE-------------ARRKELEEKMVSLLQEKNDLQLQ----VQAEQD 896
Cdd:pfam15921 462 KVSSLTAQLESTKEMlRKVVEELTAKKMTLESSErtvsdltaslqekERAIEATNAEITKLRSRVDLKLQelqhLKNEGD 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 897 NLADAEERCDQLiknKIQLEAK---VKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATEN 973
Cdd:pfam15921 542 HLRNVQTECEAL---KLQMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 974 KVKNLTEEMAGLDEIIAKLT-------KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQE-KKVR 1045
Cdd:pfam15921 619 KIRELEARVSDLELEKVKLVnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTtNKLK 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1046 MDLERAKRKLEGdlklTQESIMDLENDkqqlderlkkkdfELNALNARIEDEQALGSQlQKKLKELQARIEELEEELEAE 1125
Cdd:pfam15921 699 MQLKSAQSELEQ----TRNTLKSMEGS-------------DGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNA 760
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034587182 1126 RTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSV 1200
Cdd:pfam15921 761 NKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESV 835
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
841-1111 |
1.41e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 53.75 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 841 KSAEREKEMASMKEEFTRLKEALEKS-----EARRKELEEkMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKI-- 913
Cdd:PLN02939 118 NSKDGEQLSDFQLEDLVGMIQNAEKNilllnQARLQALED-LEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIhv 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 914 -----QLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKekhaTENKVKNLTEEMAGLDEI 988
Cdd:PLN02939 197 eileeQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAE----TEERVFKLEKERSLLDAS 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 989 IAKLTKEKKALQEAHQQaLDDLQAEE--DKVNTLTKAKVKLEQQVDDLEGSLEQEKkvrmDLERAKRKLEGDL------K 1060
Cdd:PLN02939 273 LRELESKFIVAQEDVSK-LSPLQYDCwwEKVENLQDLLDRATNQVEKAALVLDQNQ----DLRDKVDKLEASLkeanvsK 347
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 1061 LTQESIMDLENDKQQLDERLKKKDFElnaLNARIEDEQALGSQLQKKLKEL 1111
Cdd:PLN02939 348 FSSYKVELLQQKLKLLEERLQASDHE---IHSYIQLYQESIKEFQDTLSKL 395
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1042-1868 |
1.85e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1042 KKVRMDLERAKRKLegdlKLTQESIMDLENDKQQLDERLKK------KDFELNALNARIEDEQALGSQlqkklKELQAri 1115
Cdd:PRK04863 229 RKAFQDMEAALREN----RMTLEAIRVTQSDRDLFKHLITEstnyvaADYMRHANERRVHLEEALELR-----RELYT-- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1116 eeleeeleaERTARAKVEKLRSDLSRELEEISER---LEEAGGATS--VQIEMNKKREAE-FQKMRRDLEEATLQHEATA 1189
Cdd:PRK04863 298 ---------SRRQLAAEQYRLVEMARELAELNEAesdLEQDYQAASdhLNLVQTALRQQEkIERYQADLEELEERLEEQN 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1190 AAlrkkhadsVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNME-------QIIKAKANLEK---MCRT-------L 1252
Cdd:PRK04863 369 EV--------VEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDvqqtraiQYQQAVQALERakqLCGLpdltadnA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1253 EDQMNEHRSKAEETQRSVNDL-----TSQRAKLQTENG---------------------ELSRQLDEKEALISQLTRGKl 1306
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLeqklsVAQAAHSQFEQAyqlvrkiagevsrseawdvarELLRRLREQRHLAEQLQQLR- 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1307 tytQQLEDLKRQLEEEVKAKNALAHALQSARHDCDlLREQYEEETEAKAELQRVLSKANSEVAQWRTKYEtdaiQRTEEL 1386
Cdd:PRK04863 520 ---MRLSELEQRLRQQQRAERLLAEFCKRLGKNLD-DEDELEQLQEELEARLESLSESVSEARERRMALR----QQLEQL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1387 EEAKKKLAQRLQE---AEEAVEAVNAKCSSLEKTKHRLQNEIEDLmvdVERSNAAAAALDKKQRNFDKILAEWKQKYEES 1463
Cdd:PRK04863 592 QARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQL---LERERELTVERDELAARKQALDEEIERLSQPG 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1464 QSELESSQKEARSLSTELfkLKNAYEE-SLEH-------------------LETFKRENKNLQEEISDL------TEQLG 1517
Cdd:PRK04863 669 GSEDPRLNALAERFGGVL--LSEIYDDvSLEDapyfsalygparhaivvpdLSDAAEQLAGLEDCPEDLyliegdPDSFD 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1518 SSGKTIHELEK----------VR----------------KQLEAEKMELQSaLEEAEASLEHEEGKILRAQLEFNQIKAE 1571
Cdd:PRK04863 747 DSVFSVEELEKavvvkiadrqWRysrfpevplfgraareKRIEQLRAEREE-LAERYATLSFDVQKLQRLHQAFSRFIGS 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1572 -IERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMeiqLSHANRMAAEaqkqvkSLQSLL 1650
Cdd:PRK04863 826 hLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRL---LPRLNLLADE------TLADRV 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1651 KDTQIQLDDAVRANDDLKEN---IAIVERRNNLLQA---ELEELRAVVEQTERSRKLAEQELIETSERVQLLH----SQN 1720
Cdd:PRK04863 897 EEIREQLDEAEEAKRFVQQHgnaLAQLEPIVSVLQSdpeQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyEDA 976
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1721 TSLINQkkkmDADLS-QLQTEVEEAVQECRNAEEKAKKA---ITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHR 1796
Cdd:PRK04863 977 AEMLAK----NSDLNeKLRQRLEQAEQERTRAREQLRQAqaqLAQYNQVLASLKSSYDA---KRQMLQELKQELQDLGVP 1049
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587182 1797 LDEAEQIALKGGKKQLQKLEARVRELENELEAE---QKRNAES-VKGMRKSERRIKELTYQTEEDRKNLLRLQDLV 1868
Cdd:PRK04863 1050 ADSGAEERARARRDELHARLSANRSRRNQLEKQltfCEAEMDNlTKKLRKLERDYHEMREQVVNAKAGWCAVLRLV 1125
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1473-1829 |
1.89e-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: 52.38 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1473 EARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLE 1552
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1553 HEEGKILRAQLEFNQ---IKAEIERKLAEKDEEME------QAKRNHLRVVDSLQTSLDAETRSRNEALRV----KKKME 1619
Cdd:pfam19220 101 EAEAAKEELRIELRDktaQAEALERQLAAETEQNRaleeenKALREEAQAAEKALQRAEGELATARERLALleqeNRRLQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1620 GDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAV----RANDDLKENIAIVERRNNLLQAELEELRAVVEQT 1695
Cdd:pfam19220 181 ALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQaereRAEAQLEEAVEAHRAERASLRMKLEALTARAAAT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1696 ERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQEcRNAEEKAKKAITD-AAMMAEELKkeqD 1774
Cdd:pfam19220 261 EQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQ-FQEMQRARAELEErAEMLTKALA---A 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034587182 1775 TSAHLERMkknmEQTIKDLQHRLDEAEQIALKggkkQLQKLEARVRELENELEAE 1829
Cdd:pfam19220 337 KDAALERA----EERIASLSDRIAELTKRFEV----ERAALEQANRRLKEELQRE 383
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
934-1130 |
2.71e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 934 AELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQ-- 1011
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1012 -AEEDKVNTLTKAK---------VKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLK 1081
Cdd:COG3883 99 gGSVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034587182 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 ... |
1245-1446 |
2.83e-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: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1245 LEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVK 1324
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1325 AKNALAHALQSARHdcdllREQYEEETEAKAELQRVLSKANSevaqwrtkyeTDAI-QRTEELEEAKKKLAQRLQEAEEA 1403
Cdd:pfam09726 480 ARASAEKQLAEEKK-----RKKEEEATAARAVALAAASRGEC----------TESLkQRKRELESEIKKLTHDIKLKEEQ 544
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034587182 1404 VEAVNAKCSSLEKTKHRlQNEIEDLMvdversNAAAAALDKKQ 1446
Cdd:pfam09726 545 IRELEIKVQELRKYKES-EKDTEVLM------SALSAMQDKNQ 580
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1056-1286 |
3.40e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1056 EGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEeleeeleaerTARAKVEKL 1135
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA----------EAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1136 RSDLSRELEEISERLEEAG------GATSV-----QIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsVAELG 1204
Cdd:COG3883 85 REELGERARALYRSGGSVSyldvllGSESFsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAK----LAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1205 EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTEN 1284
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
..
gi 1034587182 1285 GE 1286
Cdd:COG3883 241 AA 242
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
845-1835 |
3.54e-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: 52.36 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 845 REKEMASMKEEFTRLKEALEKSEARRKELeekmvsllqeKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNE 924
Cdd:TIGR01612 763 KEKELSNKINDYAKEKDELNKYKSKISEI----------KNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFK 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 925 RLEDEEEMNAELTAKKRK---LEDECSElkrDIDDLELTLAKVEkekhateNKVKNLTEEmAGLDEIIAKLTKEKKALQE 1001
Cdd:TIGR01612 833 IINEMKFMKDDFLNKVDKfinFENNCKE---KIDSEHEQFAELT-------NKIKAEISD-DKLNDYEKKFNDSKSLINE 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1002 AHQQalddLQAEEDKVNTLTKakvkLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLK 1081
Cdd:TIGR01612 902 INKS----IEEEYQNINTLKK----VDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLI 973
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1082 KKDFELNAL--NARIEDEQALGSQLQKKLKELQARIEELEEEL-----EAERTARAKVEKLRSDLSRELEEI-------- 1146
Cdd:TIGR01612 974 DKINELDKAfkDASLNDYEAKNNELIKYFNDLKANLGKNKENMlyhqfDEKEKATNDIEQKIEDANKNIPNIeiaihtsi 1053
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1147 ---SERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSE 1223
Cdd:TIGR01612 1054 yniIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKA 1133
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1224 FKlELDDVTSNMEQIIKAKAN-LEKMCRTLedQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLT 1302
Cdd:TIGR01612 1134 LE-EIKKKSENYIDEIKAQINdLEDVADKA--ISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLE 1210
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1303 RGK---LTYTQQLEDL-KRQLEEEVKAKNALAHALQSARHDCDLLREQYEE-------ETEAKAELQrVLSKANSEvaqw 1371
Cdd:TIGR01612 1211 EVKginLSYGKNLGKLfLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEienemgiEMDIKAEME-TFNISHDD---- 1285
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1372 RTKYETDAIQRTEELEEAKKKLAQRLQEaeeaveavNAKCSSLEKTKHRLQNEIedlmVDVERSNAAAAALDKKQRNFDK 1451
Cdd:TIGR01612 1286 DKDHHIISKKHDENISDIREKSLKIIED--------FSEESDINDIKKELQKNL----LDAQKHNSDINLYLNEIANIYN 1353
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1452 ILaewkqkyeesqselessqkearslstELFKLKNAYEESLEHLETFKRENKNLQEEISDlTEQLGssgKTIHElekvRK 1531
Cdd:TIGR01612 1354 IL--------------------------KLNKIKKIIDEVKEYTKEIEENNKNIKDELDK-SEKLI---KKIKD----DI 1399
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1532 QLEAEKMELQSALEEAEAsleheEGKILRAQLEFNQIKAEierkLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNeA 1611
Cdd:TIGR01612 1400 NLEECKSKIESTLDDKDI-----DECIKKIKELKNHILSE----ESNIDTYFKNADENNENVLLLFKNIEMADNKSQH-I 1469
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1612 LRVKKK-----MEGDLNEMEIQLSHANRMAAEAQKQVKSLQS---LLKdtQIQLDDAVRAND----DLKENIAIVERRNN 1679
Cdd:TIGR01612 1470 LKIKKDnatndHDFNINELKEHIDKSKGCKDEADKNAKAIEKnkeLFE--QYKKDVTELLNKysalAIKNKFAKTKKDSE 1547
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1680 LLQAELEELRAVV----EQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQ--TEVEEAVQECRNAEE 1753
Cdd:TIGR01612 1548 IIIKEIKDAHKKFileaEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLkiSDIKKKINDCLKETE 1627
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1754 KAKKAITDAAMMAEE--LKKEQDTSAHLERMKKNMEQTIKDLQHRldeaeqialkggKKQLQKLEARVRELENELEaEQK 1831
Cdd:TIGR01612 1628 SIEKKISSFSIDSQDteLKENGDNLNSLQEFLESLKDQKKNIEDK------------KKELDELDSEIEKIEIDVD-QHK 1694
|
....
gi 1034587182 1832 RNAE 1835
Cdd:TIGR01612 1695 KNYE 1698
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
883-1531 |
3.55e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.21 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 883 EKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELtakkRKLEDECSELKRDIDDLELTLA 962
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKL----KSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 963 KVEKEKHATENKVKNLTEEMAGLDEIIAKLT---KEKKALQEAHQQALDDLQAEEDKVNtltkakvkleqqvdDLEGSLE 1039
Cdd:PRK01156 215 ITLKEIERLSIEYNNAMDDYNNLKSALNELSsleDMKNRYESEIKTAESDLSMELEKNN--------------YYKELEE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1040 QEKKVRMDLERAKRklegdlkltqESIMDLENDKQQLD---ERLKKKDFELNALNARIedeqalgsqlqKKLKELQArie 1116
Cdd:PRK01156 281 RHMKIINDPVYKNR----------NYINDYFKYKNDIEnkkQILSNIDAEINKYHAII-----------KKLSVLQK--- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1117 eleeeleaERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRR---DLEEATLQHEATAAALR 1193
Cdd:PRK01156 337 --------DYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERmsaFISEILKIQEIDPDAIK 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1194 KKHadsvAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEqiIKAKANLEKMCRT------LEDQMNEHRSKAEETQ 1267
Cdd:PRK01156 409 KEL----NEINVKLQDISSKVSSLNQRIRALRENLDELSRNME--MLNGQSVCPVCGTtlgeekSNHIINHYNEKKSRLE 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1268 RSVNDLTSQRAKLqteNGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQY 1347
Cdd:PRK01156 483 EKIREIEIEVKDI---DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLK 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1348 EEETEAKAElqrVLSKANSEvaqwRTKYETDAIQ-RTEELEEAKKKLAQRLQEAEEAVEAVNakcSSLEKTKHRLQNEIE 1426
Cdd:PRK01156 560 LEDLDSKRT---SWLNALAV----ISLIDIETNRsRSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEAN 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1427 DLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKeARSLSTELFKLKNAYEESLEHLETFKRENKNLQ 1506
Cdd:PRK01156 630 NLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSR-INDIEDNLKKSRKALDDAKANRARLESTIEILR 708
|
650 660
....*....|....*....|....*
gi 1034587182 1507 EEISDLTEQLGSSGKTIHELEKVRK 1531
Cdd:PRK01156 709 TRINELSDRINDINETLESMKKIKK 733
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1668-1925 |
3.77e-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: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1668 KENIAIVE--RRNNLLQAELEELRAVVEQ-------TERsRKLAEQELIETSERVQLLHSQNTSLINQKKKMdadlsQLQ 1738
Cdd:TIGR02168 135 KRSYSIIEqgKISEIIEAKPEERRAIFEEaagiskyKER-RKETERKLERTRENLDRLEDILNELERQLKSL-----ERQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1739 TEVEEAVQECRNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEAR 1818
Cdd:TIGR02168 209 AEKAERYKELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEELRLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1819 VRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRK 1898
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
250 260
....*....|....*....|....*..
gi 1034587182 1899 VQHELDEAEERADIAESQVNKLRAKSR 1925
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLE 382
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1251-1409 |
4.10e-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: 49.92 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1251 TLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAK--NA 1328
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1329 LAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVN 1408
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
.
gi 1034587182 1409 A 1409
Cdd:COG1579 174 P 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1484-1935 |
4.35e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1484 LKNAYEESLEHLETFK-RENKNLQEEISDLTEQL---GSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEgkIL 1559
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELkeaEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE--KL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1560 RAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEA 1639
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1640 QKQVKSLQSLLKDTQIQLDDavranddlkeniaiverrnnlLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQ 1719
Cdd:COG4717 205 QQRLAELEEELEEAQEELEE---------------------LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1720 NTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKKNMEQTIKDLQHRL 1797
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1798 DEAEQIalkggKKQLQKLEARVRELE-NELEAEQKRNAESVKGmrKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVK 1876
Cdd:COG4717 344 DRIEEL-----QELLREAEELEEELQlEELEQEIAALLAEAGV--EDEEELRAALEQAEEYQELKEELEELEEQLEELLG 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034587182 1877 AYKRQAEEAEEQANTnlSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLNEE 1935
Cdd:COG4717 417 ELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1273-1697 |
5.38e-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: 51.05 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1273 LTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAknaLAHALQSARHDCDLLREQYEEETE 1352
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAE---LKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1353 AKAELqrvlskanSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDV 1432
Cdd:pfam07888 109 SSEEL--------SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1433 ERSnaaaaaldkkqrnfdkilaewkqkyeesqselessQKEARSLSTELFKLKNAYEESLEHLETfkrenknLQEEISDL 1512
Cdd:pfam07888 181 QQT-----------------------------------EEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1513 TEQLGSSGKTIHELEKVRKqleaekmELQSALEEAEASLEHEEGkilraqlefnqIKAEIERKLAEKDEEMEQAKRNHLR 1592
Cdd:pfam07888 219 TQKLTTAHRKEAENEALLE-------ELRSLQERLNASERKVEG-----------LGEELSSMAAQRDRTQAELHQARLQ 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1593 VVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQ--------------IQLD 1658
Cdd:pfam07888 281 AAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREklevelgrekdcnrVQLS 360
|
410 420 430
....*....|....*....|....*....|....*....
gi 1034587182 1659 DAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTER 1697
Cdd:pfam07888 361 ESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1261-1588 |
5.49e-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: 51.55 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1261 SKAEETQRSVNDLTsqRAKLQTENGELSRQLDEKE-----ALISQLTRGKLTYTQQLEDLKRQLEEEV--KAKNALAHAL 1333
Cdd:NF033838 50 SSGNESQKEHAKEV--ESHLEKILSEIQKSLDKRKhtqnvALNKKLSDIKTEYLYELNVLKEKSEAELtsKTKKELDAAF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1334 QSARHDCDLLREQYEEETEAKAELQRvlsKANSEVAQWRTKYETDAIqRTEELEEAKKKLaqRLQEAEEAVEAVNAKCSS 1413
Cdd:NF033838 128 EQFKKDTLEPGKKVAEATKKVEEAEK---KAKDQKEEDRRNYPTNTY-KTLELEIAESDV--EVKKAELELVKEEAKEPR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1414 LEKTkhrlqneIEDLMVDVERSNAAAAALDKKQRnfDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLE 1493
Cdd:NF033838 202 DEEK-------IKQAKAKVESKKAEATRLEKIKT--DREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1494 HLETFKRENKNLQEEISDLTEQLGS----SGKTIHELEK-----------------------VRKQLEAEKMELQSALEE 1546
Cdd:NF033838 273 PATPDKKENDAKSSDSSVGEETLPSpslkPEKKVAEAEKkveeakkkakdqkeedrrnyptnTYKTLELEIAESDVKVKE 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1034587182 1547 AEASLEHEEGKILRAQLEFNQIKAEIERKLAE----------KDEEMEQAKR 1588
Cdd:NF033838 353 AELELVKEEAKEPRNEEKIKQAKAKVESKKAEatrlekiktdRKKAEEEAKR 404
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1236-1884 |
7.30e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.34 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1236 EQIIKAKANLEKmcrtLEDQMNEHRSKAEETQRSVND----LTSQRAKLQTENGELSRQ---LDEKEALISQLTRgklty 1308
Cdd:PRK10246 191 EQHKSARTELEK----LQAQASGVALLTPEQVQSLTAslqvLTDEEKQLLTAQQQQQQSlnwLTRLDELQQEASR----- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1309 TQQLedLKRQLEEEVKAKNALAhALQSARHDCDL--LREQYEEETEAKAELQRVLSKANS---EVAQWRTKYETDAIQRT 1383
Cdd:PRK10246 262 RQQA--LQQALAAEEKAQPQLA-ALSLAQPARQLrpHWERIQEQSAALAHTRQQIEEVNTrlqSTMALRARIRHHAAKQS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1384 EELEEAKKKLAQRLQEAE------EAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNA------------AAAALDK- 1444
Cdd:PRK10246 339 AELQAQQQSLNTWLAEHDrfrqwnNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltadeVAAALAQh 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1445 -KQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKnayeeslEHLETFKRENKNLQEEISDLteqlgssgKTI 1523
Cdd:PRK10246 419 aEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRN-------AALNEMRQRYKEKTQQLADV--------KTI 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1524 HELEKVRKQLEAEKMELQS-------------------------------ALEEAEASLEhEEGKILRAQLE--FNQIK- 1569
Cdd:PRK10246 484 CEQEARIKDLEAQRAQLQAgqpcplcgstshpaveayqalepgvnqsrldALEKEVKKLG-EEGAALRGQLDalTKQLQr 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1570 --------AEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEgdlneMEIQLshanrmaAEAQK 1641
Cdd:PRK10246 563 deseaqslRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHE-----LQGQI-------AAHNQ 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1642 QVKSLQSLLKDTQIQLDDAVRA-----NDDLKENIAIVER------------RNNLLQAELEELRAVVEQTERSRKLAEQ 1704
Cdd:PRK10246 631 QIIQYQQQIEQRQQQLLTALAGyaltlPQEDEEASWLATRqqeaqswqqrqnELTALQNRIQQLTPLLETLPQSDDLPHS 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1705 ELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEK---AKKAITDAAMMAEElkkeqdTSAHLER 1781
Cdd:PRK10246 711 EETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQAsvfDDQQAFLAALLDEE------TLTQLEQ 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1782 MKKNMEQTIKDLQHRLDEAEQialkggkKQLQKLEARVRELENELEAE--QKRNAESVKGMRKSERRIKELTYQTEEDRK 1859
Cdd:PRK10246 785 LKQNLENQRQQAQTLVTQTAQ-------ALAQHQQHRPDGLDLTVTVEqiQQELAQLAQQLRENTTRQGEIRQQLKQDAD 857
|
730 740
....*....|....*....|....*
gi 1034587182 1860 NLLRLQDLVdklqLKVKAYKRQAEE 1884
Cdd:PRK10246 858 NRQQQQALM----QQIAQATQQVED 878
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1437-1677 |
7.65e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1437 AAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQl 1516
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1517 gssgktiheLEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQI--KAEIERKLAEKDEEMEQAKRNHLRVV 1594
Cdd:COG4942 92 ---------IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1595 DSLQTSLDAEtrsrnealrvKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIV 1674
Cdd:COG4942 163 AALRAELEAE----------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
...
gi 1034587182 1675 ERR 1677
Cdd:COG4942 233 EAE 235
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
849-1321 |
7.94e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 50.95 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 849 MASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQliknkiqleakvkemNERLED 928
Cdd:PRK10246 428 LVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQ---------------EARIKD 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 929 EEEMNAELTAKK----------------RKLEDECSELKRdiDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKL 992
Cdd:PRK10246 493 LEAQRAQLQAGQpcplcgstshpaveayQALEPGVNQSRL--DALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSL 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 993 TKEKKALQEAHQQALDDL---QAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRmDLERAKRKLEGDLKLTQESimdL 1069
Cdd:PRK10246 571 RQEEQALTQQWQAVCASLnitLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIA-AHNQQIIQYQQQIEQRQQQ---L 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1070 ENDKQQLDERLKKKDFELNALNARiEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISER 1149
Cdd:PRK10246 647 LTALAGYALTLPQEDEEASWLATR-QQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQ 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1150 leeaggATSVQIEMNKKREAEFQKMRRdLEEATLQHEATAAALRkkHADSVAELG-----EQIDNLQRVKQKLEKeksef 1224
Cdd:PRK10246 726 ------CLSLHSQLQTLQQQDVLEAQR-LQKAQAQFDTALQASV--FDDQQAFLAalldeETLTQLEQLKQNLEN----- 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1225 klelddvtsnmeQIIKAKANLEKMCRTLEDQMN------EHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALI 1298
Cdd:PRK10246 792 ------------QRQQAQTLVTQTAQALAQHQQhrpdglDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNR 859
|
490 500
....*....|....*....|...
gi 1034587182 1299 SQLtrgkLTYTQQLEDLKRQLEE 1321
Cdd:PRK10246 860 QQQ----QALMQQIAQATQQVED 878
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1349-1909 |
8.30e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1349 EETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKL-AQR--LQEAEEAVEAVNAKCSSLEKTKHRL--QN 1423
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIeAQRkaIQELQFENEKVSLKLEEEIQENKDLikEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1424 EIEDLMVDVERSNAAAAALDKKQRNFDKilAEWKQKYEESQSELESSQKEARSLSTEL--------FKLKNAYEEsLEHL 1495
Cdd:pfam05483 151 NATRHLCNLLKETCARSAEKTKKYEYER--EETRQVYMDLNNNIEKMILAFEELRVQAenarlemhFKLKEDHEK-IQHL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1496 ET-FKRENKNLQEEIS--------------DLTEQLGSSGKTIHELEKVRK-------QLEAEKMELQSALEEAEASLEH 1553
Cdd:pfam05483 228 EEeYKKEINDKEKQVSllliqitekenkmkDLTFLLEESRDKANQLEEKTKlqdenlkELIEKKDHLTKELEDIKMSLQR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1554 EEGKILRAQLEFNQIKAEIERKLAEKDEEMEQ---AKRNHLRVVdslqTSLDAETRSRNEALRV-KKKMEGDLNEMEIql 1629
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEElnkAKAAHSFVV----TEFEATTCSLEELLRTeQQRLEKNEDQLKI-- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1630 shanrMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERrNNLLQAELEELRAVVEQTERSRKLAEQELIET 1709
Cdd:pfam05483 382 -----ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDE-KKQFEKIAEELKGKEQELIFLLQAREKEIHDL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1710 SERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMeqt 1789
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM--- 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1790 ikdlqhrldeaeqialkggKKQLQKLEARVRELENELEA---EQKRNAESVK-GMRKSERRIKELTYQTEEDRKNLLRLQ 1865
Cdd:pfam05483 533 -------------------LKQIENLEEKEMNLRDELESvreEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILE 593
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587182 1866 DL--------------VDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEER 1909
Cdd:pfam05483 594 NKcnnlkkqienknknIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK 651
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1011-1193 |
9.61e-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: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1011 QAEEDKVNTLTKAKVKLEQQVDDLEGSLEQ-EKKvrmdLERAKRK-----LEGDLKLTQESIMDLENDKQQLDERLKKKD 1084
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAA----LEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1085 FELNALNARIED---------EQALGSQLQKKLKELQARIEELEEELEAE----RTARAKVEKLRSDLSRELEEISERLE 1151
Cdd:COG3206 240 ARLAALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034587182 1152 eaggatsVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALR 1193
Cdd:COG3206 320 -------AELEALQAREASLQAQLAQLEARLAELPELEAELR 354
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1310-1578 |
1.13e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.53 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1310 QQLEDLKRQLEEEVKAKNALAHALQSARHDC-----DLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTE 1384
Cdd:pfam00038 21 RFLEQQNKLLETKISELRQKKGAEPSRLYSLyekeiEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1385 eLEEAKKKLAQRLQEAEEAVEAVNAKCSSLE------KTKHR-----LQNEIEDLMVDVERSNAaaaaldkKQRNFDKIL 1453
Cdd:pfam00038 101 -AENDLVGLRKDLDEATLARVDLEAKIESLKeelaflKKNHEeevreLQAQVSDTQVNVEMDAA-------RKLDLTSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1454 AEWKQKYEEsqselessqkearslstelfkLKNAYEESLEhlETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQL 1533
Cdd:pfam00038 173 AEIRAQYEE---------------------IAAKNREEAE--EWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSL 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587182 1534 EAE-------KMELQSALEEAEASLEHE----EGKILRAQLEFNQIKAEIERKLAE 1578
Cdd:pfam00038 230 EIElqslkkqKASLERQLAETEERYELQladyQELISELEAELQETRQEMARQLRE 285
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1175-1928 |
1.16e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1175 RRDLEEATLQHEATAAALRK------KHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVtSNMEQIIKAKANLEKM 1248
Cdd:PRK04863 282 RVHLEEALELRRELYTSRRQlaaeqyRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL-RQQEKIERYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1249 CRTLEDQM----------NEHRSKAEETQRSVNDLTSQRAklqtengelsrqlDEKEALISQLTRGkLTYTQQLedlkrQ 1318
Cdd:PRK04863 361 EERLEEQNevveeadeqqEENEARAEAAEEEVDELKSQLA-------------DYQQALDVQQTRA-IQYQQAV-----Q 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1319 LEEEVKAKNALAH-ALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYE-----TDAIQRTEELEEAKKK 1392
Cdd:PRK04863 422 ALERAKQLCGLPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvrkiAGEVSRSEAWDVAREL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1393 LAQ--RLQEAEEAVEAVNAKCSSLEKtkhRLQNeiedlmvdversnaaaaaldkkQRNFDKILAEWKQKYEESQSELEss 1470
Cdd:PRK04863 502 LRRlrEQRHLAEQLQQLRMRLSELEQ---RLRQ----------------------QQRAERLLAEFCKRLGKNLDDED-- 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1471 qkearslstELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSgktIHELEkvrkQLEAEKMELQSALEE-AEA 1549
Cdd:PRK04863 555 ---------ELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR---IQRLA----ARAPAWLAAQDALARlREQ 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1550 SLEHEEGkilRAQL-EFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAE-TRSRNEALRVKKKMEGDLNEmEI 1627
Cdd:PRK04863 619 SGEEFED---SQDVtEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEdPRLNALAERFGGVLLSEIYD-DV 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1628 QLSHANRMAA---------------EAQKQVKSLQSLLKDTQI------QLDDAVRANDDLKENIAIV------------ 1674
Cdd:PRK04863 695 SLEDAPYFSAlygparhaivvpdlsDAAEQLAGLEDCPEDLYLiegdpdSFDDSVFSVEELEKAVVVKiadrqwrysrfp 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1675 ----------ERRNNLLQAELEELravveqTERSRKLAEQelietSERVQLLHSQNTSLINQK-------------KKMD 1731
Cdd:PRK04863 775 evplfgraarEKRIEQLRAEREEL------AERYATLSFD-----VQKLQRLHQAFSRFIGSHlavafeadpeaelRQLN 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1732 ADLSQLQTEV---EEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSaHLERmkknmeqtIKDLQHRLDEAEQ----IA 1804
Cdd:PRK04863 844 RRRVELERALadhESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADET-LADR--------VEEIREQLDEAEEakrfVQ 914
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1805 LKGGK-KQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTE-------EDRKNLL-RLQDLVDKLQLKV 1875
Cdd:PRK04863 915 QHGNAlAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfsyEDAAEMLaKNSDLNEKLRQRL 994
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1034587182 1876 KAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIG 1928
Cdd:PRK04863 995 EQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLG 1047
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
869-1792 |
1.28e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.82 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 869 RRKELEEKMVSLLQEKNDlqlQVQAEQDNLADAEERCDQLIKNKIqlEAKVKEMNERLEDEEEMNAELTAKKRKLEDECS 948
Cdd:TIGR01612 501 RMKDFKDIIDFMELYKPD---EVPSKNIIGFDIDQNIKAKLYKEI--EAGLKESYELAKNWKKLIHEIKKELEEENEDSI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 949 ELKRDIDDLELTLAKVEKE-------KHATENKVKNLTEEmaglDEIIAKLTKEKKALqEAHQQALDDL-QAEEDKVNTL 1020
Cdd:TIGR01612 576 HLEKEIKDLFDKYLEIDDEiiyinklKLELKEKIKNISDK----NEYIKKAIDLKKII-ENNNAYIDELaKISPYQVPEH 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1021 TKAKVKLEQQVDDlegslEQEKKVRMDLERAKRKLEgdlKLTQESIMDLENDKQQLDERLKKKDFELNAL-NARIEDEQA 1099
Cdd:TIGR01612 651 LKNKDKIYSTIKS-----ELSKIYEDDIDALYNELS---SIVKENAIDNTEDKAKLDDLKSKIDKEYDKIqNMETATVEL 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1100 LGSQLQKKLKELQARIEELEeeleaertarakvEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLE 1179
Cdd:TIGR01612 723 HLSNIENKKNELLDIIVEIK-------------KHIHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKIS 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1180 EATLQHEATAAALRKKHADS---VAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIkakaNLEKMCRtlEDQM 1256
Cdd:TIGR01612 790 EIKNHYNDQINIDNIKDEDAkqnYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFI----NFENNCK--EKID 863
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1257 NEHRSKAEETQRSVNDLTSQRAKLQTENgelsrqLDEKEALISQLTRGKLTYTQQLEDLKRqLEEEVKAKNALAHALQSA 1336
Cdd:TIGR01612 864 SEHEQFAELTNKIKAEISDDKLNDYEKK------FNDSKSLINEINKSIEEEYQNINTLKK-VDEYIKICENTKESIEKF 936
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1337 RHDCDLLREQYEEETEakaelqrVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAE--EAVEAVNAKCSSL 1414
Cdd:TIGR01612 937 HNKQNILKEILNKNID-------TIKESNLIEKSYKDKFDNTLIDKINELDKAFKDASLNDYEAKnnELIKYFNDLKANL 1009
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1415 EKTKHRLQ----NEIEDLMVDVERSNAAAaaldkkQRNFDKI-LAEWKQKYEESQSELESSQKEARSLSTELFKLK---- 1485
Cdd:TIGR01612 1010 GKNKENMLyhqfDEKEKATNDIEQKIEDA------NKNIPNIeIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAeini 1083
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1486 ---NAYEESLEHL---ETFKRENKNLQEEISDLTEQLGSSG----KTIHELEKVRKQLEAEKMELQSAL----------- 1544
Cdd:TIGR01612 1084 tnfNEIKEKLKHYnfdDFGKEENIKYADEINKIKDDIKNLDqkidHHIKALEEIKKKSENYIDEIKAQIndledvadkai 1163
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1545 -----EEAEASLEHEEGKILRAQLEFNQIKAEI-ERKLAEKDE-EMEQAKRNHLRVVDSLQT----SLDAEtrsrnealr 1613
Cdd:TIGR01612 1164 snddpEEIEKKIENIVTKIDKKKNIYDEIKKLLnEIAEIEKDKtSLEEVKGINLSYGKNLGKlfleKIDEE--------- 1234
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1614 vKKKMEGDLNEMEIQLSHANRMAAEAQkQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVE 1693
Cdd:TIGR01612 1235 -KKKSEHMIKAMEAYIEDLDEIKEKSP-EIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIE 1312
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1694 QTERSRKLAEqelIETSERVQLLHSQ-NTSLINQKKKMDADLSQLQT-----EVEEAVQECRNAEEKAKKAITDAAMMAE 1767
Cdd:TIGR01612 1313 DFSEESDIND---IKKELQKNLLDAQkHNSDINLYLNEIANIYNILKlnkikKIIDEVKEYTKEIEENNKNIKDELDKSE 1389
|
970 980
....*....|....*....|....*
gi 1034587182 1768 ELKKEQDTSAHLERMKKNMEQTIKD 1792
Cdd:TIGR01612 1390 KLIKKIKDDINLEECKSKIESTLDD 1414
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1310-1906 |
1.33e-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: 50.34 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1310 QQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLR---------EQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAI 1380
Cdd:COG3096 306 YRLVEMARELEELSARESDLEQDYQAASDHLNLVQtalrqqekiERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1381 QRTEELEEAKKKLA--------------------QRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDL---MVDVER--- 1434
Cdd:COG3096 386 AAEEEVDSLKSQLAdyqqaldvqqtraiqyqqavQALEKARALCGLPDLTPENAEDYLAAFRAKEQQAteeVLELEQkls 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1435 -SNAAAAALDKKQRNFDKILAE------WKQkyeesqseLESSQKEARSLSTELFKLkNAYEESLEHLETFKRENKNLQE 1507
Cdd:COG3096 466 vADAARRQFEKAYELVCKIAGEversqaWQT--------ARELLRRYRSQQALAQRL-QQLRAQLAELEQRLRQQQNAER 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1508 EISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEA---SLEHEEGKiLRAQLEFNQIKAEIERKLAEK----D 1580
Cdd:COG3096 537 LLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEqrsELRQQLEQ-LRARIKELAARAPAWLAAQDAlerlR 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1581 EEMEQAKRNHLRVVDSLQTSLDAE---TRSRNEALRVKKKMEGDLNEmeiqLSHAN-----RMAAEAQKQVKSLQSLLKD 1652
Cdd:COG3096 616 EQSGEALADSQEVTAAMQQLLEREreaTVERDELAARKQALESQIER----LSQPGgaedpRLLALAERLGGVLLSEIYD 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1653 tQIQLDDA-------------------------VRANDDLKENIAIVERR-----NNLLQAELEELRAVVEQTERS---- 1698
Cdd:COG3096 692 -DVTLEDApyfsalygparhaivvpdlsavkeqLAGLEDCPEDLYLIEGDpdsfdDSVFDAEELEDAVVVKLSDRQwrys 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1699 ---------RKLAEQELIETSE-----------------RVQLLHSQNTSLINQKKKM--DAD-------LSQLQTEVEE 1743
Cdd:COG3096 771 rfpevplfgRAAREKRLEELRAerdelaeqyakasfdvqKLQRLHQAFSQFVGGHLAVafAPDpeaelaaLRQRRSELER 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1744 AVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmKKNMEQTIKDLQHRLDEAEQ----IALKGgkKQLQKLEARV 1819
Cdd:COG3096 851 ELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLA--DETLADRLEELREELDAAQEaqafIQQHG--KALAQLEPLV 926
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1820 RELEN-------------ELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRknLLRLQDLVDKLQLKVkaykRQAEEAE 1886
Cdd:COG3096 927 AVLQSdpeqfeqlqadylQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGL--LGENSDLNEKLRARL----EQAEEAR 1000
|
730 740
....*....|....*....|
gi 1034587182 1887 EQANTNLskfRKVQHELDEA 1906
Cdd:COG3096 1001 REAREQL---RQAQAQYSQY 1017
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1090-1364 |
1.46e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1090 LNARIEDEQALGSQLQKKLKELQARIeeleeeleaeRTARAKVEKLRS-----DLSRELEEISERLEEAggatsvqiemn 1164
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKEL----------EEAEAALEEFRQknglvDLSEEAKLLLQQLSEL----------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1165 kkrEAEFQKMRRDLEEAtlqhEATAAALRKKHADSVAELGEQIDN--LQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAK 1242
Cdd:COG3206 225 ---ESQLAEARAELAEA----EARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALR 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1243 ANLEkmcrTLEDQMnehrskAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRgkltYTQQLEDLKRQLEee 1322
Cdd:COG3206 298 AQIA----ALRAQL------QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVE-- 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1034587182 1323 vkaknalahalqsarhdcdLLREQYE------EETEAKAELQ----RVLSKA 1364
Cdd:COG3206 362 -------------------VARELYEsllqrlEEARLAEALTvgnvRVIDPA 394
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1048-1202 |
1.46e-05 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 50.14 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1048 LERAKRKLEGDLKLTQESIMDLENDKQQLDERLKkkdfELNALNARIEDEQAlgsQLQKKLKELQARieeleeELEAERT 1127
Cdd:COG1193 502 IERARELLGEESIDVEKLIEELERERRELEEERE----EAERLREELEKLRE---ELEEKLEELEEE------KEEILEK 568
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034587182 1128 ARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAE 1202
Cdd:COG1193 569 AREEAEEILREARKEAEELIRELREA-----------QAEEEELKEARKKLEELKQELEEKLEKPKKKAKPAKPP 632
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1485-1920 |
1.52e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.83 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1485 KNAYEEsLEHLETFKRE--NKNLQEEISDLtEQLGSSGKTIHELEKVRKQ----------------LEAEK-------ME 1539
Cdd:PRK04778 25 KRNYKR-IDELEERKQEleNLPVNDELEKV-KKLNLTGQSEEKFEEWRQKwdeivtnslpdieeqlFEAEElndkfrfRK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1540 LQSALEEAEASLEHEEGKILRAQLEFNQIKaEIERKLaekDEEMEQAKRNHlrvvDSLQTSLDAETRSRNEALrvkKKME 1619
Cdd:PRK04778 103 AKHEINEIESLLDLIEEDIEQILEELQELL-ESEEKN---REEVEQLKDLY----RELRKSLLANRFSFGPAL---DELE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1620 GDLNEMEIQLSHANRMAA-----EAQKQVKSLQSLLKDTQIQLDDavranddlkenI-AIVERRNNLLQAELEELRAVVE 1693
Cdd:PRK04778 172 KQLENLEEEFSQFVELTEsgdyvEAREILDQLEEELAALEQIMEE-----------IpELLKELQTELPDQLQELKAGYR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1694 Q-TERSRKLAEQELIETSERVQLLHSQNTSLINQ-------------KKKMDADLSQLQTEVEeavqeCRNAEEKAKKAI 1759
Cdd:PRK04778 241 ElVEEGYHLDHLDIEKEIQDLKEQIDENLALLEEldldeaeekneeiQERIDQLYDILEREVK-----ARKYVEKNSDTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1760 TDAAMMAEELKKEqdTSAHLERMKKN-------------MEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENEL 1826
Cdd:PRK04778 316 PDFLEHAKEQNKE--LKEEIDRVKQSytlneselesvrqLEKQLESLEKQYDEITE-RIAEQEIAYSELQEELEEILKQL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1827 ---EAEQKRNAESVKGMRKSERRIKEltyQTEEDRKNLLRLQDLVDKLQL-----KVKAYKRQAEEAEEQANTNLSKFR- 1897
Cdd:PRK04778 393 eeiEKEQEKLSEMLQGLRKDELEARE---KLERYRNKLHEIKRYLEKSNLpglpeDYLEMFFEVSDEIEALAEELEEKPi 469
|
490 500
....*....|....*....|....*.
gi 1034587182 1898 ---KVQHELDEAEERADIAESQVNKL 1920
Cdd:PRK04778 470 nmeAVNRLLEEATEDVETLEEETEEL 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1744-1927 |
1.53e-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: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1744 AVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELE 1823
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-ELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1824 NELEAEQKRNAESVKGMRKSERR---------------IKELTY----------QTEEDRKNLLRLQDLVDKLQLKVKAY 1878
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQpplalllspedfldaVRRLQYlkylaparreQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034587182 1879 KRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1927
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1381-1611 |
1.67e-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: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1381 QRTEELEEAKKKLAQ---RLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWK 1457
Cdd:COG4942 24 EAEAELEQLQQEIAElekELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1458 QKYeesQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLgssgktiHELEKVRKQLEAEK 1537
Cdd:COG4942 104 EEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-------AELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034587182 1538 MELQSALEEAEAslehEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQtSLDAETRSRNEA 1611
Cdd:COG4942 174 AELEALLAELEE----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA-RLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1432-1834 |
2.01e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1432 VERSNAAAAALDKKQRNFDKILAEwKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEhLETFKRENKNLQEEISD 1511
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1512 LTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHL 1591
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1592 RVVDSLQTSLDAETRSRNEAL------------RVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDD 1659
Cdd:COG4717 231 QLENELEAAALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1660 AVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQ--ELIETSERVQLLHSQNTSLINQKKKMDADLSQL 1737
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1738 QTEVEEAVQ---ECRNAEEKAKKAITDAAMMAEELKKEQ--DTSAHLERMKKNMEQTIKDLQHRLDEAE-QIALKGGKKQ 1811
Cdd:COG4717 391 LEQAEEYQElkeELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEELEEELEELREELAELEaELEQLEEDGE 470
|
410 420
....*....|....*....|...
gi 1034587182 1812 LQKLEARVRELENELEAEQKRNA 1834
Cdd:COG4717 471 LAELLQELEELKAELRELAEEWA 493
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1686-1935 |
2.41e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1686 EELRAVVEQT-------ERsRKLAEQELIETSE---RVQLLHSQntslinqkkkMDADLSQLQTEVEEAVqecRNAEEKA 1755
Cdd:COG1196 155 EERRAIIEEAagiskykER-KEEAERKLEATEEnleRLEDILGE----------LERQLEPLERQAEKAE---RYRELKE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1756 KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKRNAE 1835
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-ELEELRLELEELELELEEAQAEEYELLAELAR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1836 SVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAES 1915
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
250 260
....*....|....*....|
gi 1034587182 1916 QVNKLRAKSRDIGTKGLNEE 1935
Cdd:COG1196 380 ELEELAEELLEALRAAAELA 399
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1472-1930 |
2.43e-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: 49.33 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1472 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASL 1551
Cdd:pfam05483 120 KAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAF 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1552 EHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSH 1631
Cdd:pfam05483 200 EELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1632 ANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSE 1711
Cdd:pfam05483 280 QDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTC 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1712 RVQ-LLHSQNTSLIN---QKKKMDADLSQLQTEVEEAVQECRNAE---EKAKKAITDAAMMAEELKKEQDTSahlERMKK 1784
Cdd:pfam05483 360 SLEeLLRTEQQRLEKnedQLKIITMELQKKSSELEEMTKFKNNKEvelEELKKILAEDEKLLDEKKQFEKIA---EELKG 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1785 NMEQTIKDLQHRLDEAE--QIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLL 1862
Cdd:pfam05483 437 KEQELIFLLQAREKEIHdlEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELK 516
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034587182 1863 RLQDLVDKLQLKVKAYKRQAE---EAEEQANTNLSKFRK--------VQHELDEAEERADIAESQVNKLRAKSRDIGTK 1930
Cdd:pfam05483 517 KHQEDIINCKKQEERMLKQIEnleEKEMNLRDELESVREefiqkgdeVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
843-1014 |
2.51e-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: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 843 AEREKEMASMKEEFTRLKEALEKseaRRKELEEKMVSLLQEKNDLQ-LQVQAEQDNLADAEERCDQLikNKIqleakVKE 921
Cdd:COG3883 61 EALQAEIDKLQAEIAEAEAEIEE---RREELGERARALYRSGGSVSyLDVLLGSESFSDFLDRLSAL--SKI-----ADA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 922 MNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQE 1001
Cdd:COG3883 131 DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
170
....*....|...
gi 1034587182 1002 AHQQALDDLQAEE 1014
Cdd:COG3883 211 AAAAAAAAAAAAA 223
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
860-1681 |
2.87e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.66 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 860 KEALEK--SEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLA------------DAEERCDQLIKN----KIQLEAKVKE 921
Cdd:TIGR01612 976 INELDKafKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLyhqfdekekatnDIEQKIEDANKNipniEIAIHTSIYN 1055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 922 MNERLEDEEEMNAELTAKK--RKLEDECSELKRDIDDLEL----TLAKVEKEKHATE-NKVKNlteEMAGLDEIIAKLTK 994
Cdd:TIGR01612 1056 IIDEIEKEIGKNIELLNKEilEEAEINITNFNEIKEKLKHynfdDFGKEENIKYADEiNKIKD---DIKNLDQKIDHHIK 1132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 995 EKKALQEAHQQALDDLQAEEDKVNTLTKAKVkleqQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQEsIMDLENDK- 1073
Cdd:TIGR01612 1133 ALEEIKKKSENYIDEIKAQINDLEDVADKAI----SNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNE-IAEIEKDKt 1207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1074 ---------------------QQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAeRTARAKV 1132
Cdd:TIGR01612 1208 sleevkginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETF-NISHDDD 1286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1133 EKLRSDLSRELEEISERLEEaggatSVQIEMNKKREAEFQKMRRDLEEATLQHEataaalrkKHADSVAELGEQIDNLQR 1212
Cdd:TIGR01612 1287 KDHHIISKKHDENISDIREK-----SLKIIEDFSEESDINDIKKELQKNLLDAQ--------KHNSDINLYLNEIANIYN 1353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1213 VKQ--KLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMN--EHRSKAEETQ---------RSVNDLTSQRAK 1279
Cdd:TIGR01612 1354 ILKlnKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINleECKSKIESTLddkdideciKKIKELKNHILS 1433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1280 LQTENGELSRQLDEKEALISQLTRgkltyTQQLEDLKRQLEEEVKAKNAlahalqSARHDCDL--LREQYEEETEAKAEL 1357
Cdd:TIGR01612 1434 EESNIDTYFKNADENNENVLLLFK-----NIEMADNKSQHILKIKKDNA------TNDHDFNIneLKEHIDKSKGCKDEA 1502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1358 QR----------VLSKANSEVAQWRTKYETDAIQrtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNE--- 1424
Cdd:TIGR01612 1503 DKnakaieknkeLFEQYKKDVTELLNKYSALAIK--NKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEkfr 1580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1425 IEDLMVDVERSNAAAAALDKKQRNFDkilaewkqkyeesqselessqkearslsTELFKLKNAYEESLEHLetfkRENKN 1504
Cdd:TIGR01612 1581 IEDDAAKNDKSNKAAIDIQLSLENFE----------------------------NKFLKISDIKKKINDCL----KETES 1628
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1505 LQEEISDLT-----EQLGSSGKTIHELEKVRKQLEAEKMELqsalEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEK 1579
Cdd:TIGR01612 1629 IEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQKKNI----EDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEK 1704
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1580 DEEMEQAKRNHL------------RVVDSLQTSlDAETRSRNEALRVKKKMEGDLNEMEIQLSH--ANRMAAEAQKQVKS 1645
Cdd:TIGR01612 1705 IKEIAIANKEEIesikelieptieNLISSFNTN-DLEGIDPNEKLEEYNTEIGDIYEEFIELYNiiAGCLETVSKEPITY 1783
|
890 900 910
....*....|....*....|....*....|....*.
gi 1034587182 1646 LQslLKDTQIQlddavrANDDLKENIAIVERRNNLL 1681
Cdd:TIGR01612 1784 DE--IKNTRIN------AQNEFLKIIEIEKKSKSYL 1811
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1340-1552 |
2.94e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.16 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1340 CDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKH 1419
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1420 RLQNEIEDLM------VDVER----SNAAAAALDKKQRNFDKILAEWKQKYEESQSELESS-------QKEARSLSTELF 1482
Cdd:PRK05771 118 ELEQEIERLEpwgnfdLDLSLllgfKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvvLKELSDEVEEEL 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034587182 1483 KlKNAYEE-SLEHLETFKRENKNLQEEISDLTEQLGSsgkTIHELEKVRKQLEAEKM----ELQSALEEAEASLE 1552
Cdd:PRK05771 198 K-KLGFERlELEEEGTPSELIREIKEELEEIEKERES---LLEELKELAKKYLEELLalyeYLEIELERAEALSK 268
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
955-1339 |
3.37e-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: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 955 DDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDL-------QAEEDKVN-TLTKAKVK 1026
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLrrlfdekQSEKDKKNkALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1027 LEQQVDDLEGSLEQ-EKKVRMDLERAKRKLEGDLKLTQESIMDLENDkqqlderlkkKDFELNALNARIEDEQALGSQLQ 1105
Cdd:pfam12128 680 ANERLNSLEAQLKQlDKKHQAWLEEQKEQKREARTEKQAYWQVVEGA----------LDAQLALLKAAIAARRSGAKAEL 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1106 KKLKELQARieeleeeleaERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQH 1185
Cdd:pfam12128 750 KALETWYKR----------DLASLGVDPDVIAKLKREIRTLERKIERI-----------AVRRQEVLRYFDWYQETWLQR 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1186 EataaalrkkhadsvaelgeqiDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEE 1265
Cdd:pfam12128 809 R---------------------PRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC 867
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034587182 1266 TQRSVNDLTSQRAKLQTEnGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEevKAKNALAHALQSARHD 1339
Cdd:pfam12128 868 EMSKLATLKEDANSEQAQ-GSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIAD--HSGSGLAETWESLREE 938
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1535-1920 |
4.40e-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: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1535 AEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERK-LAEKDEEME-QAKRNHLRVVdslqtsldaetrsrNEAL 1612
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELsARESDLEQDyQAASDHLNLV--------------QTAL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1613 RVKKKME---GDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRN----NLLQAeL 1685
Cdd:COG3096 344 RQQEKIEryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyqQAVQA-L 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1686 EELRAVVEQTERSRKLAEQELIETSERVQLLHSqntSLINQKKKM-DADLSQLQTE-VEEAVQ------ECRNAEEKAKK 1757
Cdd:COG3096 423 EKARALCGLPDLTPENAEDYLAAFRAKEQQATE---EVLELEQKLsVADAARRQFEkAYELVCkiagevERSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1758 AITDAAMMAEELKKEQDTSAHLERMKKNMEQtikdlQHRLDE-AEQIALKGGKK--QLQKLEARVRELENELEAEQKRNA 1834
Cdd:COG3096 500 LLRRYRSQQALAQRLQQLRAQLAELEQRLRQ-----QQNAERlLEEFCQRIGQQldAAEELEELLAELEAQLEELEEQAA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1835 ESVKGMRKSERRIKELTYQTEEDRK---NLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERAD 1911
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAArapAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQ 654
|
....*....
gi 1034587182 1912 IAESQVNKL 1920
Cdd:COG3096 655 ALESQIERL 663
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
931-1221 |
5.00e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 931 EMNAELTAKKRkledecsELKRDIDDLELTLAKVEkEKHATENKVKNLTEEMAG--LDEIIAKLTKEKKALQEAHQQald 1008
Cdd:PHA02562 167 EMDKLNKDKIR-------ELNQQIQTLDMKIDHIQ-QQIKTYNKNIEEQRKKNGenIARKQNKYDELVEEAKTIKAE--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1009 dlqaeedkVNTLTKAKVKLEQQVDDLEGSLeqeKKVRMDLERAKRKLEgdlKLTQESIMDLEND-----KQQLDERlkkk 1083
Cdd:PHA02562 236 --------IEELTDELLNLVMDIEDPSAAL---NKLNTAAAKIKSKIE---QFQKVIKMYEKGGvcptcTQQISEG---- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1084 dfelnalNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiem 1163
Cdd:PHA02562 298 -------PDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKA---------- 360
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587182 1164 nKKREAEFQKmrrdleeatlqheatAAALRKKHADSVAELGEQIDNLQRVKQKLEKEK 1221
Cdd:PHA02562 361 -KKVKAAIEE---------------LQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1312-1887 |
5.23e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1312 LEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYE--TDAIQRTEELEEA 1389
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1390 KKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLqNEIEDLMVDVERSNAAAAALDKKQ-RNFDKILAEWK---QKYeesqs 1465
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYKELEERH-MKIINDPVYKNRNYINDYFKYKNDiENKKQILSNIDaeiNKY----- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1466 elessqKEARSLSTELFKLKNAYEESlehletfKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALE 1545
Cdd:PRK01156 325 ------HAIIKKLSVLQKDYNDYIKK-------KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1546 EAEASLEHEEGKilraQLEFNQIKAEIERKLAEKDEEmeqakrnhlrvVDSLQTSLDAETRSRNEALRVKKKMEG----- 1620
Cdd:PRK01156 392 FISEILKIQEID----PDAIKKELNEINVKLQDISSK-----------VSSLNQRIRALRENLDELSRNMEMLNGqsvcp 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1621 ----DLNEMEIqlshaNRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEniaiveRRNNLLQAELEELRAVVEQTE 1696
Cdd:PRK01156 457 vcgtTLGEEKS-----NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKK------RKEYLESEEINKSINEYNKIE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1697 RSRklAEQELIETSE-RVQLLHSQNTSLINQKKKMD-ADLSQLQTEVEEA--------VQECRNAEEKAKKAITDAAMMA 1766
Cdd:PRK01156 526 SAR--ADLEDIKIKInELKDKHDKYEEIKNRYKSLKlEDLDSKRTSWLNAlavislidIETNRSRSNEIKKQLNDLESRL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1767 EELKKE-QDTSAHLERMKKNMEQTIKDLQHRLDEAEqiALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSER 1845
Cdd:PRK01156 604 QEIEIGfPDDKSYIDKSIREIENEANNLNNKYNEIQ--ENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIED 681
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1034587182 1846 RIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEE 1887
Cdd:PRK01156 682 NLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1384-1919 |
5.78e-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: 48.10 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1384 EELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKhrlqNEIEDLMVDVERsnaaaAALDKKQRNFDKILAEWKQKyees 1463
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTK----RLIEELKLNLER-----AQTEEAQAKQDSELAKLRVE---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1464 QSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDL----------TEQLGSSGKtihELEKVRKQL 1533
Cdd:pfam05701 109 EMEQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLvserdiaikrAEEAVSASK---EIEKTVEEL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1534 EAEKMELQSALEEAEAS-LEHEEGKIlRAQLEFNQIKAEIERKLAEKDEEMEQAkRNHLRVVDSLQTSLDAetrsrNEAL 1612
Cdd:pfam05701 186 TIELIATKESLESAHAAhLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-----ASAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1613 RVKKK------MEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDdavRANDDLKENIAIVERrnnlLQAELE 1686
Cdd:pfam05701 259 LLDLKaelaayMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIE---KAKDEVNCLRVAAAS----LRSELE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1687 ELRAVVEQTERSRKLAEqelietservqllhsqntslinqkkkmdADLSQLQTEVEEAVQECRNAEEKAKKAitdAAMMA 1766
Cdd:pfam05701 332 KEKAELASLRQREGMAS----------------------------IAVSSLEAELNRTKSEIALVQAKEKEA---REKMV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1767 EELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkgGKKQLQKLEARVRELENELEA---EQKRNAESVKGMRKS 1843
Cdd:pfam05701 381 ELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQ-----AKAAASTVESRLEAVLKEIEAakaSEKLALAAIKALQES 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587182 1844 ERRiKELTYQTEEDRKNLLRLQDLvdklqlkvKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNK 1919
Cdd:pfam05701 456 ESS-AESTNQEDSPRGVTLSLEEY--------YELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNR 522
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1075-1555 |
5.81e-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: 48.20 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1075 QLDERLKKKdfELNALNARIEDEQALGSQLQ------KKLKELQARIeeleeeleaertarakveklrsdlsrelEEISE 1148
Cdd:pfam05557 13 QLQNEKKQM--ELEHKRARIELEKKASALKRqldresDRNQELQKRI----------------------------RLLEK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1149 RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQhEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEL 1228
Cdd:pfam05557 63 REAEAEEALREQAELNRLKKKYLEALNKKLNEKESQ-LADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1229 DDVTSNMEQIIKAKANLEKMCRTL---EDQMNE---HRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALiSQLT 1302
Cdd:pfam05557 142 DLLKAKASEAEQLRQNLEKQQSSLaeaEQRIKElefEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHL-NENI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1303 RGKLTYTQQLEDLKRQLeeevkaknalahalqsarhdcdllrEQYEEETEAKAELQRVLSKANSEVAQWRTKYETDA--I 1380
Cdd:pfam05557 221 ENKLLLKEEVEDLKRKL-------------------------EREEKYREEAATLELEKEKLEQELQSWVKLAQDTGlnL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1381 QRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNE-------IEDLMVDVERSNAAAAALDK------KQR 1447
Cdd:pfam05557 276 RSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQElaqylkkIEDLNKKLKRHKALVRRLQRrvllltKER 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1448 NFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEES-------LEHLETFKRENKNLQEEISDLTEQ----- 1515
Cdd:pfam05557 356 DGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMeaqlsvaEEELGGYKQQAQTLERELQALRQQeslad 435
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1034587182 1516 LGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEE 1555
Cdd:pfam05557 436 PSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRC 475
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1496-1851 |
6.20e-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: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1496 ETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQsalEEAEASLEHEEGKILRAQLEFNQIKAEIERK 1575
Cdd:pfam07888 69 EQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS---EEKDALLAQRAAHEARIRELEEDIKTLTQRV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1576 LaEKDEEMEQAKRNHLRVVDSLQtsldaETRSRNEALRVK-KKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQ 1654
Cdd:pfam07888 146 L-ERETELERMKERAKKAGAQRK-----EEEAERKQLQAKlQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1655 IQLDDAvranddlkeniaivERRNNLLQAELEELRAVveqtersrklaeQELIETSER-VQLLHSQNTSLINQKKKMDAD 1733
Cdd:pfam07888 220 QKLTTA--------------HRKEAENEALLEELRSL------------QERLNASERkVEGLGEELSSMAAQRDRTQAE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1734 LSQLQTEVEE----------AVQECRNAEEKAKKAITDAAMMAEElkKEQDTSAHLERMKKNMEQTIKDLQH------RL 1797
Cdd:pfam07888 274 LHQARLQAAQltlqladaslALREGRARWAQERETLQQSAEADKD--RIEKLSAELQRLEERLQEERMEREKlevelgRE 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1034587182 1798 DEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELT 1851
Cdd:pfam07888 352 KDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1048-1586 |
6.52e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1048 LERAKRKLEGDLKLTQESIMDLENdkqqLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERT 1127
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1128 A--------------RAKVEKLRSDLSRELEE---ISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1190
Cdd:PRK01156 240 AlnelssledmknryESEIKTAESDLSMELEKnnyYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1191 ALRKKHADSVAELGEQIDNLQRVKQKleKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSV 1270
Cdd:PRK01156 320 EINKYHAIIKKLSVLQKDYNDYIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1271 NDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLE---------------EEVKAKNALAH---A 1332
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlGEEKSNHIINHyneK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1333 LQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAqRLQEAEEAVEAVNAKCS 1412
Cdd:PRK01156 478 KSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKIN-ELKDKHDKYEEIKNRYK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1413 SLEKTKHRLQNEiEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESL 1492
Cdd:PRK01156 557 SLKLEDLDSKRT-SWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKY 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1493 EHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQL---EAEKMELQSALEEAEASLEHEEG--KILRAQL-EFN 1566
Cdd:PRK01156 636 NEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIndiEDNLKKSRKALDDAKANRARLEStiEILRTRInELS 715
|
570 580
....*....|....*....|
gi 1034587182 1567 QIKAEIERKLaEKDEEMEQA 1586
Cdd:PRK01156 716 DRINDINETL-ESMKKIKKA 734
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1020-1170 |
6.82e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1020 LTKAKVKLEQQVDDLEGSLEQEKK-----VRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARI 1094
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKealleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1095 EDEQALGSQLQKKLKELQARIEELEEEleaertARAKVEKLrSDLSRE------LEEISERLEEAGGATSVQIEMNKKRE 1168
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEE------QLQELERI-SGLTAEeakeilLEKVEEEARHEAAVLIKEIEEEAKEE 185
|
..
gi 1034587182 1169 AE 1170
Cdd:PRK12704 186 AD 187
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
765-1110 |
6.85e-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: 48.02 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 765 FKAGLLGLLEEMR---------DERLSRIITRIQaqsrgvlaRMEYKKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYF- 834
Cdd:pfam15818 5 FKTSLLEALEELRmrreaetqyEEQIGKIIVETQ--------ELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCAl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 835 ---KIKPLLKSAEREKEMASmkeeftrLKEALEKSEARRKELEEKmVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKN 911
Cdd:pfam15818 77 eeeKGKYQLATEIKEKEIEG-------LKETLKALQVSKYSLQKK-VSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 912 KIQLeakVKEMNERLE----DEEEMNAELTAKKRKLEDECSELKRDIDDL--ELTLAKVE-KEKHATEN--------KVK 976
Cdd:pfam15818 149 QFGL---VKENHGKLEqnvqEAIQLNKRLSALNKKQESEICSLKKELKKVtsDLIKSKVTcQYKMGEENinltikeqKFQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 977 NLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEgslEQEKKVRMDLERAKRKLe 1056
Cdd:pfam15818 226 ELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALK---ENNQTLERDNELQREKV- 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1034587182 1057 gdlKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKE 1110
Cdd:pfam15818 302 ---KENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1595-1807 |
7.14e-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: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1595 DSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIV 1674
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1675 ER------RNNLLQ--------AELEELRAVVEQTERSRKLAEQELIETSERvqlLHSQNTSLINQKKKMDADLSQLQTE 1740
Cdd:COG4942 110 LRalyrlgRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAE---LAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587182 1741 VEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKG 1807
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1226-1397 |
7.65e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1226 LELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGK 1305
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1306 ltytqQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEE 1385
Cdd:COG1579 90 -----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|..
gi 1034587182 1386 LEEAKKKLAQRL 1397
Cdd:COG1579 165 REELAAKIPPEL 176
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
871-1223 |
7.80e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 871 KELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSEL 950
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 951 KRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQ 1030
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1031 VDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKE 1110
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1111 LQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1190
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350
....*....|....*....|....*....|...
gi 1034587182 1191 ALRKKHADSVAELGEQIDNLQRVKQKLEKEKSE 1223
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
867-1334 |
8.23e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 47.82 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 867 EARRKELEEKMVSLLQEKNDLQLQVQAEQDNLadaeercdQLIKNKIQLEAkvKEMNERLEDEEEMNAELTAKKRKLede 946
Cdd:pfam07111 241 ELERQELLDTMQHLQEDRADLQATVELLQVRV--------QSLTHMLALQE--EELTRKIQPSDSLEPEFPKKCRSL--- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 947 cseLKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTL------ 1020
Cdd:pfam07111 308 ---LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLqmelsr 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1021 -TKAKVKLEQQVDDLEgslEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKkdfelnalnariedeqa 1099
Cdd:pfam07111 385 aQEARRRQQQQTASAE---EQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRK----------------- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1100 lgsqlQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISE---RL--EEAGGATSVQIEMNKKREaEFQKM 1174
Cdd:pfam07111 445 -----VHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREernRLdaELQLSAHLIQQEVGRARE-QGEAE 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1175 RRDLEEATLQHEATAaalrKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDV-----TSNMEQIIKAKANLEKMC 1249
Cdd:pfam07111 519 RQQLSEVAQQLEQEL----QRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQqeiygQALQEKVAEVETRLREQL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1250 RTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEalisqltrgkltyTQQLEDLKRQLEEEVKAKNAL 1329
Cdd:pfam07111 595 SDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEAR-------------KEEGQRLARRVQELERDKNLM 661
|
....*
gi 1034587182 1330 AHALQ 1334
Cdd:pfam07111 662 LATLQ 666
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1493-1932 |
8.75e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.59 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1493 EHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSAL--------EEAEASLEHEEGKILRAQLE 1564
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1565 FNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVK 1644
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1645 SLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLI 1724
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1725 NQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIA 1804
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1805 LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEE 1884
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1034587182 1885 AEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGL 1932
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAA 523
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1422-1922 |
9.51e-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: 47.43 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1422 QNEIEDLMVDVERSNAAAAALDKKQRNFDKILAewKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLEtfkRE 1501
Cdd:pfam05557 20 QMELEHKRARIELEKKASALKRQLDRESDRNQE--LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL---NE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1502 NKNLQEEISDLTEQLGSsgktihELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQlEFNQIKAEIERKLAEKDE 1581
Cdd:pfam05557 95 KESQLADAREVISCLKN------ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS-EAEQLRQNLEKQQSSLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1582 EMEQAKrnHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMaaeaqkqvKSLQSLLKDTQIQLDDAV 1661
Cdd:pfam05557 168 AEQRIK--ELEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNEN--------IENKLLLKEEVEDLKRKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1662 RANDDLKENIAIVERRNNLLQAELEELravvEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEV 1741
Cdd:pfam05557 238 EREEKYREEAATLELEKEKLEQELQSW----VKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1742 EEAVQECRNAEEKakkaITDAAMMAEELK--------------KEQD-TSAHLERMKK--NMEQTIKDLQHRLDEAEQIA 1804
Cdd:pfam05557 314 RELEQELAQYLKK----IEDLNKKLKRHKalvrrlqrrvllltKERDgYRAILESYDKelTMSNYSPQLLERIEEAEDMT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1805 LKGgKKQLQKLEARVRELENELEAEQKRNA--ESVKGMRKSERRIKELTYQTEED---RKNLLRLQDLVDKLQLKVKAYK 1879
Cdd:pfam05557 390 QKM-QAHNEEMEAQLSVAEEELGGYKQQAQtlERELQALRQQESLADPSYSKEEVdslRRKLETLELERQRLREQKNELE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1034587182 1880 RQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRA 1922
Cdd:pfam05557 469 MELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQA 511
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1071-1242 |
9.78e-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: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1071 NDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERL 1150
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1151 EEAGG-----ATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFK 1225
Cdd:COG1579 83 GNVRNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|....*..
gi 1034587182 1226 LELDDVTSNMEQIIKAK 1242
Cdd:COG1579 163 AEREELAAKIPPELLAL 179
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
839-1083 |
9.92e-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: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 839 LLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQ---------EKNDLQLQVQAEQDNLADAEERCDQLI 909
Cdd:pfam15742 99 VLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQQKLEHAHKvcltdtcilEKKQLEERIKEASENEAKLKQQYQEEQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 910 KNKIQLEAKVKEMNERLEDeeemnaeLTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEemagLDEII 989
Cdd:pfam15742 179 QKRKLLDQNVNELQQQVRS-------LQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQE----LSEKL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 990 AKLTKEKKALQEAHQQALDDLQAEEDKVNtltkakvkleqqvddlegslEQEKKVRMDLERAKRKLEGDLKLTQESIMDL 1069
Cdd:pfam15742 248 SSLQQEKEALQEELQQVLKQLDVHVRKYN--------------------EKHHHHKAKLRRAKDRLVHEVEQRDERIKQL 307
|
250
....*....|....
gi 1034587182 1070 ENDKQQLDERLKKK 1083
Cdd:pfam15742 308 ENEIGILQQQSEKE 321
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1702-1889 |
1.07e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1702 AEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT-SAHLE 1780
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1781 RMKKNMEQT-----------IKDLQHRLDEAEQIAlKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKE 1849
Cdd:COG3883 94 ALYRSGGSVsyldvllgsesFSDFLDRLSALSKIA-DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034587182 1850 LTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQA 1889
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
830-1321 |
1.07e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.43 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 830 MKLYFKIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEkndLQLQVQ----------------- 892
Cdd:pfam05557 125 LELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFE---IQSQEQdseivknskselaripe 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 893 --AEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTA---KKRKLEDECSELKRDIDDLELTLAKVEke 967
Cdd:pfam05557 202 leKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPE-- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 968 khATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQalddlqaeedkvntltkakvkLEQQVDDLEGSLEQEKKVRMD 1047
Cdd:pfam05557 280 --DLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRE---------------------LEQELAQYLKKIEDLNKKLKR 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1048 LERAKRKLegdlkltQESIMDLENDKQQLDERLKKKDFELNALNAriedeqalGSQLQKKLKELqarieeleeeleaert 1127
Cdd:pfam05557 337 HKALVRRL-------QRRVLLLTKERDGYRAILESYDKELTMSNY--------SPQLLERIEEA---------------- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1128 arakvEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDleeatlqheaTAAALRKKHADSVAELGEQI 1207
Cdd:pfam05557 386 -----EDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQ----------ESLADPSYSKEEVDSLRRKL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1208 DNLQRVKQKLEKEKSEFKLELddvtsnMEQIIKAKANLEKmCRTLEDQMNehrSKAEETQRSVNDLTsqraKLQTENGEL 1287
Cdd:pfam05557 451 ETLELERQRLREQKNELEMEL------ERRCLQGDYDPKK-TKVLHLSMN---PAAEAYQQRKNQLE----KLQAEIERL 516
|
490 500 510
....*....|....*....|....*....|....*...
gi 1034587182 1288 SRQL----DEKEALISQLTRGKLTYTQQLEDLKRQLEE 1321
Cdd:pfam05557 517 KRLLkkleDDLEQVLRLPETTSTMNFKEVLDLRKELES 554
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
981-1159 |
1.15e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 981 EMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEgSLEQEKKVRMDLERAKRKLEGdlk 1060
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-ARIKKYEEQLGNVRNNKEYEA--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1061 LTQEsIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTA-RAKVEKLRSDL 1139
Cdd:COG1579 94 LQKE-IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEElEAEREELAAKI 172
|
170 180
....*....|....*....|
gi 1034587182 1140 SRELEEISERLEEAGGATSV 1159
Cdd:COG1579 173 PPELLALYERIRKRKNGLAV 192
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1477-1656 |
1.20e-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: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1477 LSTELFKLKNAYEESLEHLETFKRENKnlqeeISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEG 1556
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1557 KI--LRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVV------DSLQTSLDAET--------------RSRNEALR- 1613
Cdd:COG3206 255 ALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIalraqiAALRAQLQQEAqrilasleaelealQAREASLQa 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034587182 1614 ----VKKKMEgDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQ 1656
Cdd:COG3206 335 qlaqLEARLA-ELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
859-995 |
1.32e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 859 LKEALEKSEARRKELEEKmvsllqeknDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTA 938
Cdd:COG2433 378 IEEALEELIEKELPEEEP---------EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034587182 939 KKRKL----------EDECSELKRDIDDLELTLAKVEKEKHATENKVKNLtEEMAGLDE--------IIAKLTKE 995
Cdd:COG2433 449 ELSEArseerreirkDREISRLDREIERLERELEEERERIEELKRKLERL-KELWKLEHsgelvpvkVVEKFTKE 522
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
873-1111 |
1.46e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 873 LEEKMVSLLQEKNDLQLqVQAEQDNLADAEERcdqlIKNKIQLEAKVKEMNERLEDEeeMNAELTAKKRKLEDECSELKR 952
Cdd:PRK05771 14 LKSYKDEVLEALHELGV-VHIEDLKEELSNER----LRKLRSLLTKLSEALDKLRSY--LPKLNPLREEKKKVSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 953 DIDDLELTLAKVEKEkhatenkVKNLTEEMAGLDEIIAKLTKEKKALQ--EAHQQALDDLQAEED---KVNTLTKAKVKL 1027
Cdd:PRK05771 87 LIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvFVGTVPEDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1028 EQQVDDLEGSLEQEKK------VRMDLERAKRKLEGDLKLTQESIMDLENDKqQLDERLKKKDFELNALNARIEDeqalg 1101
Cdd:PRK05771 160 LKLESDVENVEYISTDkgyvyvVVVVLKELSDEVEEELKKLGFERLELEEEG-TPSELIREIKEELEEIEKERES----- 233
|
250
....*....|
gi 1034587182 1102 sqLQKKLKEL 1111
Cdd:PRK05771 234 --LLEELKEL 241
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
859-1399 |
1.57e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 46.67 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 859 LKEALEKSEARRKELEEKMVSLLQE-----KNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAK----VKEM------- 922
Cdd:pfam07111 120 LRAALAGAEMVRKNLEEGSQRELEEiqrlhQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKrageAKQLaeaqkea 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 923 ----NERLEDEEEMNAELT-----------------------AKKRKLEDECSELKRDIDDL----ELTLAKVEKEKHAT 971
Cdd:pfam07111 200 ellrKQLSKTQEELEAQVTlveslrkyvgeqvppevhsqtweLERQELLDTMQHLQEDRADLqatvELLQVRVQSLTHML 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 972 ENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQA----LDDLQAEE----DKVNTLTKAKVKLEQQVDD-------LEG 1036
Cdd:pfam07111 280 ALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKvfalMVQLKAQDlehrDSVKQLRGQVAELQEQVTSqsqeqaiLQR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1037 SLeQEKKVRMDLERAKRK-LEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARI 1115
Cdd:pfam07111 360 AL-QDKAAEVEVERMSAKgLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRL 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1116 EEleeeleaertARAKVEKLRSDLSRELEEISERLEEAGGATSV-QIEMNKKREAEFQKMRRDLEEATLQheaTAAALRK 1194
Cdd:pfam07111 439 SY----------AVRKVHTIKGLMARKVALAQLRQESCPPPPPApPVDADLSLELEQLREERNRLDAELQ---LSAHLIQ 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1195 KHADSVAELGE-QIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKanlekmcrtledqmnehrskaeetQRSVNDL 1273
Cdd:pfam07111 506 QEVGRAREQGEaERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQ------------------------QESTEEA 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1274 TSQRAKLQTENGELSRQLDEKEALISQLTRgkltytQQLEDLKRQLEEevkAKNALAHALQSARHdcdlLREQYEEETEA 1353
Cdd:pfam07111 562 ASLRQELTQQQEIYGQALQEKVAEVETRLR------EQLSDTKRRLNE---ARREQAKAVVSLRQ----IQHRATQEKER 628
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1034587182 1354 KAELQRVLSKANSEVAQWRTKyetdaiqRTEELEEAKKKLAQRLQE 1399
Cdd:pfam07111 629 NQELRRLQDEARKEEGQRLAR-------RVQELERDKNLMLATLQQ 667
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1378-1923 |
1.58e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1378 DAIQRTEELEEAKKKLaqrlqeaEEAVEAVNAKCSSLEKTKHRLQNEIEDlmvdVERSNAAAAALDKKQRNFDKILAEWK 1457
Cdd:PRK01156 156 DEILEINSLERNYDKL-------KDVIDMLRAEISNIDYLEEKLKSSNLE----LENIKKQIADDEKSHSITLKEIERLS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1458 QKYEESQSELESSQKEARSLSTeLFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLG--------SSGKTIHELEKV 1529
Cdd:PRK01156 225 IEYNNAMDDYNNLKSALNELSS-LEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMkiindpvyKNRNYINDYFKY 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1530 RKQLEAEKMELQSAleEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRN 1609
Cdd:PRK01156 304 KNDIENKKQILSNI--DAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1610 EALRVKK---KMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRN-------- 1678
Cdd:PRK01156 382 YSKNIERmsaFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgtt 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1679 ----------NLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTS-LINQKKKMDADLSQLqTEVEEAVQE 1747
Cdd:PRK01156 462 lgeeksnhiiNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADL-EDIKIKINE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1748 CRNAEEKAKKAITDAAMMAEELKKEQDTSaHLERMKKNMEQTIKDLQHRLDEAeqialkggKKQLQKLEARVRELENELE 1827
Cdd:PRK01156 541 LKDKHDKYEEIKNRYKSLKLEDLDSKRTS-WLNALAVISLIDIETNRSRSNEI--------KKQLNDLESRLQEIEIGFP 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1828 AEQKRNAESVkgmrkseRRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQA---EEAEEQANTNLSKFRKVQHELD 1904
Cdd:PRK01156 612 DDKSYIDKSI-------REIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIaeiDSIIPDLKEITSRINDIEDNLK 684
|
570
....*....|....*....
gi 1034587182 1905 EAEERADIAESQVNKLRAK 1923
Cdd:PRK01156 685 KSRKALDDAKANRARLEST 703
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1539-1920 |
1.61e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1539 ELQSALEEAeASLEHEEGKILRAQLEFNQIKAEIERKLA-----EKDEEME-QAKRNHLRVVdslqtsldaetrsrNEAL 1612
Cdd:PRK04863 280 ERRVHLEEA-LELRRELYTSRRQLAAEQYRLVEMARELAelneaESDLEQDyQAASDHLNLV--------------QTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1613 RVKKKME---GDLNEMEIQLSHANRMAAEAQKQ--------------VKSLQSLLKDTQIQLDDAVRANDDLKENIAIVE 1675
Cdd:PRK04863 345 RQQEKIEryqADLEELEERLEEQNEVVEEADEQqeenearaeaaeeeVDELKSQLADYQQALDVQQTRAIQYQQAVQALE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1676 RRNNLLQA---ELEELRAVVEQTERSRKLAEQELIETSERVQLlhSQNTSliNQKKKMDADLSQLQTEVEEAVqecrnAE 1752
Cdd:PRK04863 425 RAKQLCGLpdlTADNAEDWLEEFQAKEQEATEELLSLEQKLSV--AQAAH--SQFEQAYQLVRKIAGEVSRSE-----AW 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1753 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTiKDLQHRLDEAEQIALKG--GKKQLQKLEARVRELENELEAEQ 1830
Cdd:PRK04863 496 DVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQ-QRAERLLAEFCKRLGKNldDEDELEQLQEELEARLESLSESV 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1831 KRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERA 1910
Cdd:PRK04863 575 SEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARK 654
|
410
....*....|
gi 1034587182 1911 DIAESQVNKL 1920
Cdd:PRK04863 655 QALDEEIERL 664
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
911-1180 |
1.70e-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: 46.66 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 911 NKIQLEAKVKEM-NERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDeiI 989
Cdd:pfam17380 285 SERQQQEKFEKMeQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRE--L 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 990 AKLTKEKKALQEAHQQALDDLQAEEDKVN--------TLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAK----RKLEG 1057
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELERLQMERQQKNervrqeleAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARqrevRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1058 DLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQalgsQLQKKLKELQARIEELEEEleAERTARAKVEKLRS 1137
Cdd:pfam17380 443 ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK----RDRKRAEEQRRKILEKELE--ERKQAMIEEERKRK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1034587182 1138 DLSRELEEIS------ERLEEAGGATSVQIEMNKKREAEfQKMRRDLEE 1180
Cdd:pfam17380 517 LLEKEMEERQkaiyeeERRREAEEERRKQQEMEERRRIQ-EQMRKATEE 564
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1534-1763 |
1.72e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1534 EAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQakrnhlrvVDSLQTSLDaetrsrnealr 1613
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE--------IDKLQAEIA----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1614 vkkKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIqlDDAVRANDDLKeniAIVERRNNLLQaELEELRAVVE 1693
Cdd:COG3883 76 ---EAEAEIEERREELGERARALYRSGGSVSYLDVLLGSESF--SDFLDRLSALS---KIADADADLLE-ELKADKAELE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1694 QTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAA 1763
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1374-1888 |
1.76e-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: 46.89 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1374 KYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRnfdkiL 1453
Cdd:TIGR00618 177 QYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE-----A 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1454 AEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEES------LEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELE 1527
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRArkaaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1528 KVRKQ---LEAEKMELQSAL-EEAEASLEHEEGKILRAQLEfnQIKAEIERKLA-----EKDEEMEQAKRNHLRVVDSLQ 1598
Cdd:TIGR00618 332 AHVKQqssIEEQRRLLQTLHsQEIHIRDAHEVATSIREISC--QQHTLTQHIHTlqqqkTTLTQKLQSLCKELDILQREQ 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1599 TSLDAETRSRNEALRVKKKMEGdlnEMEIQLSHANRMAAEAQKQVKSLqsllKDTQIQLDDAVRANDDLKENIAIVErrn 1678
Cdd:TIGR00618 410 ATIDTRTSAFRDLQGQLAHAKK---QQELQQRYAELCAAAITCTAQCE----KLEKIHLQESAQSLKEREQQLQTKE--- 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1679 NLLQAELE----ELRAVVEQTERSRKLAEQELIETSERVQLLHSQ-NTSLINQKKKMDADLSQLQTEVEEAVQECRNAEE 1753
Cdd:TIGR00618 480 QIHLQETRkkavVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1754 KAKKAITDAamMAEELKKEQDTSAHLERMKK--NMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQK 1831
Cdd:TIGR00618 560 SLKEQMQEI--QQSFSILTQCDNRSKEDIPNlqNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQC 637
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587182 1832 RNAESVKGMRKsERRIKELTYQTEEDRKNLLRLQDlvdklqlKVKAYKRQAEEAEEQ 1888
Cdd:TIGR00618 638 SQELALKLTAL-HALQLTLTQERVREHALSIRVLP-------KELLASRQLALQKMQ 686
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1321-1623 |
1.90e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.61 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1321 EEVKAKNALAHALQSARHDCDLLREQYEEETEAKAE--LQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLaQRLQ 1398
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEvlIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQL-QELK 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1399 EAEEAVEAVNAKCSSLEKTKHRLQNEIE-DLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKeaRSL 1477
Cdd:COG5022 889 IDVKSISSLKLVNLELESEIIELKKSLSsDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVE--SKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1478 STELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGkTIHELEKVRKQLEAEKMELQSAleEAEASLEHEEGK 1557
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYG-ALQESTKQLKELPVEVAELQSA--SKIISSESTELS 1043
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587182 1558 ILR--AQLEFNQIKAeiERKLAEKDEEMEQAKRNHLRvvDSLQTSLDAETRSRNEALRVKKKMEGDLN 1623
Cdd:COG5022 1044 ILKplQKLKGLLLLE--NNQLQARYKALKLRRENSLL--DDKQLYQLESTENLLKTINVKDLEVTNRN 1107
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
777-1326 |
2.01e-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: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 777 RDERLSRIITRIQAQSRGVLARMEYKKLLER------------RDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAE 844
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYFPNKKQLEDwlhskskeinqtRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 845 REKEMASMKEEFTRLKEALEKSEARRKELeekmvSLLQEKNDLQLQVQAEqdnLADAEERCDQLIKNKIQLEakvKEMNE 924
Cdd:TIGR00606 627 KLFDVCGSQDEESDLERLKEEIEKSSKQR-----AMLAGATAVYSQFITQ---LTDENQSCCPVCQRVFQTE---AELQE 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 925 RLEDEEEMNAELTAKKRKLEDECSELKRDIDDL-------ELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKK 997
Cdd:TIGR00606 696 FISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG 775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 998 AL---QEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEG-----SLEQEKKVRMDLERAKRKLEGDLKLTQESImdl 1069
Cdd:TIGR00606 776 TImpeEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGsdldrTVQQVNQEKQEKQHELDTVVSKIELNRKLI--- 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1070 eNDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISER 1149
Cdd:TIGR00606 853 -QDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISS 931
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1150 LEEAGGATSVQIEMNKKREAEFQKMRRDLEEATlqhEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKeksEFKLELD 1229
Cdd:TIGR00606 932 KETSNKKAQDKVNDIKEKVKNIHGYMKDIENKI---QDGKDDYLKQKETELNTVNAQLEECEKHQEKINE---DMRLMRQ 1005
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1230 DVTSNMEQIIKAKANLEKMCRtledqmnehRSKAEETQRSVNDLTSQRAKLQ-TENGELSRQLDEKEALISQLTRGKLTY 1308
Cdd:TIGR00606 1006 DIDTQKIQERWLQDNLTLRKR---------ENELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLIKRNHVLALGR 1076
|
570
....*....|....*...
gi 1034587182 1309 TQQLEDLKRQLEEEVKAK 1326
Cdd:TIGR00606 1077 QKGYEKEIKHFKKELREP 1094
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
859-1085 |
2.07e-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: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 859 LKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDnladaEERCDQLIKNKIQLEAKVKEMNERLEdeeemnaeltA 938
Cdd:pfam18971 619 LEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQ-----KDEIFALINKEANRDARAIAYTQNLK----------G 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 939 KKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAkLTKEKKALQEAHQQALDDLQAEEDK-V 1017
Cdd:pfam18971 684 IKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLG-INPEWISKVENLNAALNEFKNGKNKdF 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 1018 NTLTKAKVKLEQQVDDLEGSLEQEKKV-RMDLERAKRKLEGDLKLTQESIMDLEN-DKQQLDERLKK-KDF 1085
Cdd:pfam18971 763 SKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfSKEQLAQQAQKnEDF 833
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
843-967 |
2.08e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 843 AEREKEMASMKEEFTRLKEALEKSEARRKELEEKM--VSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVK 920
Cdd:COG1579 48 EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELA 127
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034587182 921 EMNERLEDEEEmnaELTAKKRKLEDECSELKRDIDDLELTLAKVEKE 967
Cdd:COG1579 128 ELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1258-1905 |
2.08e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.58 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1258 EHRSKAEETQRSVNDLTSQRAKLQTENGE--LSRQLDEKEALISQLTR-GKLTYTQQLEDLKRQLEEEVKAKNALAHALQ 1334
Cdd:TIGR01612 693 EDKAKLDDLKSKIDKEYDKIQNMETATVElhLSNIENKKNELLDIIVEiKKHIHGEINKDLNKILEDFKNKEKELSNKIN 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1335 SarhdcdllreqYEEETEAkaelqrvLSKANSEVAQWRTKY-ETDAIQRTEElEEAKkklaQRLQEAEEAVEAVNAKCSS 1413
Cdd:TIGR01612 773 D-----------YAKEKDE-------LNKYKSKISEIKNHYnDQINIDNIKD-EDAK----QNYDKSKEYIKTISIKEDE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1414 LEKTKHRLQNEIEDLMVDVER----SNAAAAALDKKQRNFDKILAEWKQKYEESQSEL-ESSQKEARSLSTELfklKNAY 1488
Cdd:TIGR01612 830 IFKIINEMKFMKDDFLNKVDKfinfENNCKEKIDSEHEQFAELTNKIKAEISDDKLNDyEKKFNDSKSLINEI---NKSI 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1489 EESLEHLETFKREN------KNLQEEISD-------LTEQLGSSGKTIHELEKVRK----QLEAEKMELQSALEEA--EA 1549
Cdd:TIGR01612 907 EEEYQNINTLKKVDeyikicENTKESIEKfhnkqniLKEILNKNIDTIKESNLIEKsykdKFDNTLIDKINELDKAfkDA 986
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1550 SLEHEEGKILRAQLEFNQIKAEI----ERKLAEKDEEMEQAKRNHL-RVVDSLQTSLDAETRSRNEALRVKKKMEGD--- 1621
Cdd:TIGR01612 987 SLNDYEAKNNELIKYFNDLKANLgknkENMLYHQFDEKEKATNDIEqKIEDANKNIPNIEIAIHTSIYNIIDEIEKEigk 1066
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1622 ---------LNEMEIQLSHANRMaaEAQKQVKSLQSLLKDTQIQLDDAV-RANDDLK-------ENIAIVERRNNLLQAE 1684
Cdd:TIGR01612 1067 niellnkeiLEEAEINITNFNEI--KEKLKHYNFDDFGKEENIKYADEInKIKDDIKnldqkidHHIKALEEIKKKSENY 1144
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1685 LEELRAVVEQTER-SRKLAEQELIETSERVQllhsQN-TSLINQKKKMDADLSQLQTEVEE------AVQECRNAEEKAK 1756
Cdd:TIGR01612 1145 IDEIKAQINDLEDvADKAISNDDPEEIEKKI----ENiVTKIDKKKNIYDEIKKLLNEIAEiekdktSLEEVKGINLSYG 1220
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1757 KAItdAAMMAEELKKEQDTSAHlerMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAE----QKR 1832
Cdd:TIGR01612 1221 KNL--GKLFLEKIDEEKKKSEH---MIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDhhiiSKK 1295
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1833 NAESVKGMRKSERRI--------------KEL-TYQTEEDRKN------LLRLQDLVDKLQL--------KVKAYKRQAE 1883
Cdd:TIGR01612 1296 HDENISDIREKSLKIiedfseesdindikKELqKNLLDAQKHNsdinlyLNEIANIYNILKLnkikkiidEVKEYTKEIE 1375
|
730 740
....*....|....*....|..
gi 1034587182 1884 EAEEQANTNLSKFRKVQHELDE 1905
Cdd:TIGR01612 1376 ENNKNIKDELDKSEKLIKKIKD 1397
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
868-1022 |
2.12e-04 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 44.95 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 868 ARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQL---------------IKNKI--------QLEAKVKEMNE 924
Cdd:pfam15934 41 ENKNEQEQQLKEFTVQNQRLACQIDNLHETLKDRDHQIKQLqsmitgysdisennrLKEEIhdlkqkncVQARVVRKMGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 925 RLEDEEEMNAELTAKKRKL----EDECSELK---RDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLdeiiakltKEKK 997
Cdd:pfam15934 121 ELKGQEEQRVELCDKYESLlgsfEEQCQELKranRRVQSLQTRLSQVEKLQEELRTERKILREEVIAL--------KEKD 192
|
170 180
....*....|....*....|....*....
gi 1034587182 998 ALQEAHQQALDD----LQAEEDKVNTLTK 1022
Cdd:pfam15934 193 AKSNGRERALQDqlkcCQTEIEKSRTLIR 221
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
843-1113 |
2.30e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 843 AEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM 922
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 923 NER-------LEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAK---L 992
Cdd:pfam07888 156 KERakkagaqRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEneaL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 993 TKEKKALQE---AHQQA-------LDDLQAEEDKVNT-LTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKL 1061
Cdd:pfam07888 236 LEELRSLQErlnASERKveglgeeLSSMAAQRDRTQAeLHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEA 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587182 1062 TQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQ----ALGSQLQKKLKELQA 1113
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKdcnrVQLSESRRELQELKA 371
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
962-1703 |
2.35e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.33 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 962 AKVEKEK-HATENKVKNLTEE-MAGLDEIIAKLTKEKKAL---QEAHQQAL------DDLQAEEDKVNT-LTKAKVKLEQ 1029
Cdd:PRK10246 196 ARTELEKlQAQASGVALLTPEqVQSLTASLQVLTDEEKQLltaQQQQQQSLnwltrlDELQQEASRRQQaLQQALAAEEK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1030 QVDDLegsleqekkVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDErlkkkdfelnaLNARIEDEQALgsqlqkklk 1109
Cdd:PRK10246 276 AQPQL---------AALSLAQPARQLRPHWERIQEQSAALAHTRQQIEE-----------VNTRLQSTMAL--------- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1110 elQARIEELEEELEAERTARakveklRSDLSRELEEiSERL----EEAGGATSVQIEMNKKReAEFQKMRRDLEEATLQH 1185
Cdd:PRK10246 327 --RARIRHHAAKQSAELQAQ------QQSLNTWLAE-HDRFrqwnNELAGWRAQFSQQTSDR-EQLRQWQQQLTHAEQKL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1186 EATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEE 1265
Cdd:PRK10246 397 NALPAITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQ 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1266 TQR---------SVNDLTSQRAKLQTENGELSRQLDEKEAlISQLTRGKLTYTQQLEDlkrQLEEEVKaknALAHALQSA 1336
Cdd:PRK10246 477 LADvkticeqeaRIKDLEAQRAQLQAGQPCPLCGSTSHPA-VEAYQALEPGVNQSRLD---ALEKEVK---KLGEEGAAL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1337 RHDCDLLREQYEEETEakaELQRVLSKANSEVAQWRTKYETDAIQRTEELEeakkkLAQRLQEAEEAVEAVNakcssLEK 1416
Cdd:PRK10246 550 RGQLDALTKQLQRDES---EAQSLRQEEQALTQQWQAVCASLNITLQPQDD-----IQPWLDAQEEHERQLR-----LLS 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1417 TKHRLQNEIedlmvdversnaaaAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELfklkNAYEESLEHLE 1496
Cdd:PRK10246 617 QRHELQGQI--------------AAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWL----ATRQQEAQSWQ 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1497 TFKRENKNLQEEISDLT---EQLGSSGKTIHELEKVR----KQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFnqik 1569
Cdd:PRK10246 679 QRQNELTALQNRIQQLTpllETLPQSDDLPHSEETVAldnwRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQF---- 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1570 aeiERKLAEKDEEMEQAkrnhlrvvdSLQTSLDAETRSRNEALrvKKKMEGDLNEMEIQLSHANR-MAAEAQKQVKSLQS 1648
Cdd:PRK10246 755 ---DTALQASVFDDQQA---------FLAALLDEETLTQLEQL--KQNLENQRQQAQTLVTQTAQaLAQHQQHRPDGLDL 820
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587182 1649 LLKDTQIQLDDAVRAnDDLKENIAIV-ERRNNLLQAE--LEELRAVVEQTERSRKLAE 1703
Cdd:PRK10246 821 TVTVEQIQQELAQLA-QQLRENTTRQgEIRQQLKQDAdnRQQQQALMQQIAQATQQVE 877
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1489-1628 |
2.38e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1489 EESLEHLeTFKRENKNLQEEISDLTEQ---LGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEF 1565
Cdd:COG2433 379 EEALEEL-IEKELPEEEPEAEREKEHEereLTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE 457
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034587182 1566 NQiKAEIERKLAEKDEEmeqakrnhlrvVDSLQTSLDaETRSRNEALRVKKKMEGDLNEMEIQ 1628
Cdd:COG2433 458 RR-EIRKDREISRLDRE-----------IERLERELE-EERERIEELKRKLERLKELWKLEHS 507
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1138-1850 |
2.45e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1138 DLSRELEEISER---LEEAGGATS--VQIEMNKKREAE-FQKMRRDLEEATLQHEATAAAlrkkhadsVAELGEQIDNLQ 1211
Cdd:COG3096 310 EMARELEELSAResdLEQDYQAASdhLNLVQTALRQQEkIERYQEDLEELTERLEEQEEV--------VEEAAEQLAEAE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1212 RVKQKLEKEKSEFKLELDDVTSNME----------QIIKAKANLEKMCR-------TLEDQMNEHRSKAEETQRSVNDL- 1273
Cdd:COG3096 382 ARLEAAEEEVDSLKSQLADYQQALDvqqtraiqyqQAVQALEKARALCGlpdltpeNAEDYLAAFRAKEQQATEEVLELe 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1274 ----TSQRAKLQTENG---------------------ELSRQLDEKEALISQLTrgklTYTQQLEDLKRQLEEEVKAK-- 1326
Cdd:COG3096 462 qklsVADAARRQFEKAyelvckiageversqawqtarELLRRYRSQQALAQRLQ----QLRAQLAELEQRLRQQQNAErl 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1327 -NALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRtkyetdaiQRTEELEEAKKKLAQR---LQEAEE 1402
Cdd:COG3096 538 lEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELR--------QQLEQLRARIKELAARapaWLAAQD 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1403 AVEAVNAKC-----SSLEKTKHR---LQNEIEdlmVDVERSNAAAA--ALDKKQRN-------FDKILAEWKQKYeesqs 1465
Cdd:COG3096 610 ALERLREQSgealaDSQEVTAAMqqlLERERE---ATVERDELAARkqALESQIERlsqpggaEDPRLLALAERL----- 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1466 elessqkeARSLSTELFK---LKNA-YEESL----------EHLETFKRENKNLQEEISDL-----TEQLGS-SGKTIHE 1525
Cdd:COG3096 682 --------GGVLLSEIYDdvtLEDApYFSALygparhaivvPDLSAVKEQLAGLEDCPEDLyliegDPDSFDdSVFDAEE 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1526 LEK----------VR----------------KQLEAEKMELQsALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEK 1579
Cdd:COG3096 754 LEDavvvklsdrqWRysrfpevplfgraareKRLEELRAERD-ELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAP 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1580 DEEME-QAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMeiqLSHANRMAAEaqkqvkSLQSLLKDTQIQLD 1658
Cdd:COG3096 833 DPEAElAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL---LPQANLLADE------TLADRLEELREELD 903
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1659 DAVRANDDLKEN---IAIVERRNNLLQ---AELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDA 1732
Cdd:COG3096 904 AAQEAQAFIQQHgkaLAQLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENS 983
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1733 DLS-QLQTEVEEAVQECRNAEEKAKKA---ITDAAMMAEELKKEQDTSAhleRMKKNMEQTIKDLQHRLD-EAEQIAlkg 1807
Cdd:COG3096 984 DLNeKLRARLEQAEEARREAREQLRQAqaqYSQYNQVLASLKSSRDAKQ---QTLQELEQELEELGVQADaEAEERA--- 1057
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1034587182 1808 gkkqlqklEARVRELENELEAEQKRNAESVKGMRKSERRIKEL 1850
Cdd:COG3096 1058 --------RIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSL 1092
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1325-1459 |
2.48e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1325 AKNALAHALQSARHDCDLLREqyEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAV 1404
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034587182 1405 EAVNAKCSSLEKTKHRLQNEIEDlmvdversnaaaaaLDKKQRNFDKILAEWKQK 1459
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQE--------------LEKKEEELEELIEEQLQE 143
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
853-1406 |
2.68e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.20 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 853 KEEFTRLKEALEKSEARRKELEEKM---VSLLQE-KNDLQLQVQAEQDNLADAEERCDQLIKNK--IQLEAKVKEMNERL 926
Cdd:TIGR01612 1103 KEENIKYADEINKIKDDIKNLDQKIdhhIKALEEiKKKSENYIDEIKAQINDLEDVADKAISNDdpEEIEKKIENIVTKI 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 927 EDEEEMNAELtakkRKLEDECSELKRDIDDLE---------------LTLAKVEKEKHATENKVKNLTEEMAGLDEIiak 991
Cdd:TIGR01612 1183 DKKKNIYDEI----KKLLNEIAEIEKDKTSLEevkginlsygknlgkLFLEKIDEEKKKSEHMIKAMEAYIEDLDEI--- 1255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 992 ltKEKKALQEAHQQALDDLQAEEDKVNT--------LTKAKVKLEQQVDDLEGSLE--QEKKVRMDLERAKRKLEGDLKL 1061
Cdd:TIGR01612 1256 --KEKSPEIENEMGIEMDIKAEMETFNIshdddkdhHIISKKHDENISDIREKSLKiiEDFSEESDINDIKKELQKNLLD 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1062 TQE----------------SIMDLENDKQQLDErLKKKDFELNALNARIEDEQALGSQLQKK------LKELQARIEELE 1119
Cdd:TIGR01612 1334 AQKhnsdinlylneianiyNILKLNKIKKIIDE-VKEYTKEIEENNKNIKDELDKSEKLIKKikddinLEECKSKIESTL 1412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1120 EELEAERTARaKVEKLRSDLSRELEEISERLEEAGGATS------VQIEMNKKREAEFQKMRRDleEATLQHEATAAALr 1193
Cdd:TIGR01612 1413 DDKDIDECIK-KIKELKNHILSEESNIDTYFKNADENNEnvlllfKNIEMADNKSQHILKIKKD--NATNDHDFNINEL- 1488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1194 KKHADSVAELGEQIDnlqRVKQKLEKEKSEFKLELDDVTSNMEQ---------IIKAKANLEKMCRTLEDQMNEHRSKAE 1264
Cdd:TIGR01612 1489 KEHIDKSKGCKDEAD---KNAKAIEKNKELFEQYKKDVTELLNKysalaiknkFAKTKKDSEIIIKEIKDAHKKFILEAE 1565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1265 ETQRSVNDLTSQRAKLQTENGELSRQ-------------LDEKEALISQLTRGKLTYTQQLEDLKRQL--------EEEV 1323
Cdd:TIGR01612 1566 KSEQKIKEIKKEKFRIEDDAAKNDKSnkaaidiqlslenFENKFLKISDIKKKINDCLKETESIEKKIssfsidsqDTEL 1645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1324 KAKNALAHALQSArhdCDLLREQYEEETEAKAELQRVLSKANS---EVAQWRTKYETDAIQRTEELEEAKKklaQRLQEA 1400
Cdd:TIGR01612 1646 KENGDNLNSLQEF---LESLKDQKKNIEDKKKELDELDSEIEKieiDVDQHKKNYEIGIIEKIKEIAIANK---EEIESI 1719
|
....*.
gi 1034587182 1401 EEAVEA 1406
Cdd:TIGR01612 1720 KELIEP 1725
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1253-1446 |
2.78e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1253 EDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHA 1332
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1333 LQSARHDCDLL---------------REQYEEETEAKAELQRVLSKANSEVAQwrtkYETDAIQRTEELEEAKKKLAQRL 1397
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEA----KKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034587182 1398 QEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQ 1446
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1669-1917 |
2.81e-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: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1669 ENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQEC 1748
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1749 RNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNMEQTIKDLQHRLDE--AEQIALKGGKKQLQKLEARVREL 1822
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1823 ENELEAEQKRnaesvkgmrkserrikeltyqteedrknllrLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHE 1902
Cdd:COG4942 180 LAELEEERAA-------------------------------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|....*
gi 1034587182 1903 LDEAEERADIAESQV 1917
Cdd:COG4942 229 IARLEAEAAAAAERT 243
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
885-1097 |
3.98e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.07 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 885 NDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKemnerleDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKV 964
Cdd:PRK11637 43 SDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLK-------KQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 965 EKEKHATEnkvKNLTEEM---------AGLDEIIAKLTKEKKALQEAHQQALDdlQAEEDKVNTLTKAKVKLEQQVDDLE 1035
Cdd:PRK11637 116 EQQQAAQE---RLLAAQLdaafrqgehTGLQLILSGEESQRGERILAYFGYLN--QARQETIAELKQTREELAAQKAELE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587182 1036 GSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLEN----DKQQLDErLKKKDFELNALNARIEDE 1097
Cdd:PRK11637 191 EKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESslqkDQQQLSE-LRANESRLRDSIARAERE 255
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1673-1811 |
4.03e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1673 IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDAdlsQLQTEVEEAVQECRNAE 1752
Cdd:PRK00409 503 IIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQE---EEDKLLEEAEKEAQQAI 579
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034587182 1753 EKAKKAITDAAMMAEELKKEQDTSAHLermkKNMEQTIKDLQHRLDEAEQIALKGGKKQ 1811
Cdd:PRK00409 580 KEAKKEADEIIKELRQLQKGGYASVKA----HELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1203-1447 |
4.28e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1203 LGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEqiikAKANLEKMcRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQT 1282
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVDLSEE----AKLLLQQL-SELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1283 ENGELSRQldekeALISQLTrgkltytQQLEDLKRQLEEEvkaknalahalqSARhdcdlLREQYEEETEAKAELQRVLS 1362
Cdd:COG3206 255 ALPELLQS-----PVIQQLR-------AQLAELEAELAEL------------SAR-----YTPNHPDVIALRAQIAALRA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1363 KANSEVAQWRTKYETDAiqrtEELEEAKKKLAQRLQEAEEAVEAVNAKcsslektkhrlQNEIEDLMVDVERSNAAAAAL 1442
Cdd:COG3206 306 QLQQEAQRILASLEAEL----EALQAREASLQAQLAQLEARLAELPEL-----------EAELRRLEREVEVARELYESL 370
|
....*
gi 1034587182 1443 DKKQR 1447
Cdd:COG3206 371 LQRLE 375
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
898-1013 |
4.29e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 898 LADAEERCDQLIKN----------KIQLEAKVKEMNERLEDEEE---MNAELTAKKRKLEDECSELKRDIDDLELTLAKV 964
Cdd:PRK12704 33 IKEAEEEAKRILEEakkeaeaikkEALLEAKEEIHKLRNEFEKElreRRNELQKLEKRLLQKEENLDRKLELLEKREEEL 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034587182 965 EKEKHATENKVKNLTEEMAGLDEIIAK----------LTKEkkalqEAHQQALDDLQAE 1013
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEqlqelerisgLTAE-----EAKEILLEKVEEE 166
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
834-998 |
4.83e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 834 FKIKPLLKSAEREKEMAS------MKEEFTRLKEALEK-SEARRKELEEKMVSLLQEKNDLqlqvqaeqdnladaEERCD 906
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKkealleAKEEIHKLRNEFEKeLRERRNELQKLEKRLLQKEENL--------------DRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 907 QLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDE---CSELKRDiDDLELTLAKVEKE-KHATENKVKNLTEEm 982
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerISGLTAE-EAKEILLEKVEEEaRHEAAVLIKEIEEE- 181
|
170
....*....|....*.
gi 1034587182 983 agldeiiAKLTKEKKA 998
Cdd:PRK12704 182 -------AKEEADKKA 190
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1687-1871 |
4.97e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1687 ELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKK---AITDAA 1763
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1764 MMAEELKKE--------------QDTSAHLERMKKNMEQtIKDLQHRLDEAE--QIALKGGKKQLQKLEARVRELENELE 1827
Cdd:PHA02562 269 SKIEQFQKVikmyekggvcptctQQISEGPDRITKIKDK-LKELQHSLEKLDtaIDELEEIMDEFNEQSKKLLELKNKIS 347
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034587182 1828 AEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKL 1871
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
852-1576 |
5.21e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.21 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 852 MKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMN-------- 923
Cdd:PTZ00440 726 YTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISndinilke 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 924 ----------------ERLEDEEEMNAE-------------LTAKKRKLEDECSELKRDID----DLEL------TLAKV 964
Cdd:PTZ00440 806 nkknnqdllnsyniliQKLEAHTEKNDEelkqllqkfptedENLNLKELEKEFNENNQIVDniikDIENmnkninIIKTL 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 965 EKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQ-------EAHQQALDDLQAEEDKVNT------LTKAKVKLEQQV 1031
Cdd:PTZ00440 886 NIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINtdniiqkNEKLNLLNNLNKEKEKIEKqlsdtkINNLKMQIEKTL 965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1032 D-----------DLEGSLEQEKKVRMDLERAKRKLEG---DLKLTQESIMDLENDKQQ-----LDERLKKKDfelNALNA 1092
Cdd:PTZ00440 966 EyydkskeningNDGTHLEKLDKEKDEWEHFKSEIDKlnvNYNILNKKIDDLIKKQHDdiielIDKLIKEKG---KEIEE 1042
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1093 RIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEE-----AGGATSVQIEMNKKR 1167
Cdd:PTZ00440 1043 KVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEiknksHEHVVNADKEKNKQT 1122
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1168 EAeFQKMRRDLEEATLQHEATAAALRKKH-----ADSVAELGEQIDNL--QRVKQKLEKEKSEFKLELDDVTSNMEQIIK 1240
Cdd:PTZ00440 1123 EH-YNKKKKSLEKIYKQMEKTLKELENMNleditLNEVNEIEIEYERIliDHIVEQINNEAKKSKTIMEEIESYKKDIDQ 1201
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1241 AKANL--EKMCRTLEDQMNEHRSKAEETQRSVNDLTsQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQ 1318
Cdd:PTZ00440 1202 VKKNMskERNDHLTTFEYNAYYDKATASYENIEELT-TEAKGLKGEANRSTNVDELKEIKLQVFSYLQQVIKENNKMENA 1280
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1319 LeEEVKAKNALAHALQSARHDCDLLREQYEEET---EAKAELQ---RVLSKANSEVAQWRT-KYETDAIQRTEELEEAKK 1391
Cdd:PTZ00440 1281 L-HEIKNMYEFLISIDSEKILKEILNSTKKAEEfsnDAKKELEktdNLIKQVEAKIEQAKEhKNKIYGSLEDKQIDDEIK 1359
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1392 KLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEdlmvDVERSNAAAAALDKKQRNFDKILAEWK-QKYEESQSELESS 1470
Cdd:PTZ00440 1360 KIEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVR----NASRGKDKIDFLNKHEAIEPSNSKEVNiIKITDNINKCKQY 1435
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1471 QKEARSLSTELFKLKNA---YEESLEH-------------LETFKRENKNLQEEI----SDLTEQLGSSGKTIHELEKVR 1530
Cdd:PTZ00440 1436 SNEAMETENKADENNDSiikYEKEITNilnnssilgkktkLEKKKKEATNIMDDIngehSIIKTKLTKSSEKLNQLNEQP 1515
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1034587182 1531 KQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKL 1576
Cdd:PTZ00440 1516 NIKREGDVLNNDKSTIAYETIQYNLGRVKHNLLNILNIKDEIETIL 1561
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1141-1410 |
5.37e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1141 RELEEISERLEEAggatsvqiemnKKR-EAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELgeqidnLQRVKQKLEK 1219
Cdd:PRK05035 439 RAIEQEKKKAEEA-----------KARfEARQARLEREKAAREARHKKAAEARAAKDKDAVAAA------LARVKAKKAA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1220 EKSEFKLELDDVTSNMEQIIKAKAnlekmcrtledqmnehrSKAEETQRSVNDLTSQRAklqtengelsrqlDEKEALIS 1299
Cdd:PRK05035 502 ATQPIVIKAGARPDNSAVIAAREA-----------------RKAQARARQAEKQAAAAA-------------DPKKAAVA 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1300 Q-LTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALqsARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETD 1378
Cdd:PRK05035 552 AaIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAI--ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKA 629
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034587182 1379 AIQRTEELEE---------------AKKKLAQRLQEAEEAVEAVNAK 1410
Cdd:PRK05035 630 EQQANAEPEEpvdprkaavaaaiarAKARKAAQQQANAEPEEAEDPK 676
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
960-1191 |
5.50e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 960 TLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLE 1039
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1040 qekkvrmdlERAKRKLEG-------DLKLTQESIMDL-----------ENDKQQLDERLKKKDfELNALNARIEDEQAlg 1101
Cdd:COG3883 90 ---------ERARALYRSggsvsylDVLLGSESFSDFldrlsalskiaDADADLLEELKADKA-ELEAKKAELEAKLA-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1102 sQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEA 1181
Cdd:COG3883 158 -ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250
....*....|
gi 1034587182 1182 TLQHEATAAA 1191
Cdd:COG3883 237 AAAAAAAASA 246
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1024-1573 |
5.71e-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: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1024 KVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDfelNALNARIEDEQALGSQ 1103
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAE---EALREQAELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1104 LQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSvQIEMNKKREAEFQKMRRDLEEAtl 1183
Cdd:pfam05557 85 LEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQE-RLDLLKAKASEAEQLRQNLEKQ-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1184 QHEATAAALRKKhadsvaELGEQIDNLQRVKQKLEKEKSEFkLELDDVTSNMEQIIKAKANLEKMCRT---LEDQMNEHR 1260
Cdd:pfam05557 162 QSSLAEAEQRIK------ELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKELERLREHNKHLNENIENkllLKEEVEDLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1261 SKAEETQRSVNDLtsqrAKLQTENGELSRQLDEKEAL-----------------ISQLTRGKLTYTQQLEDLKRQLEEEV 1323
Cdd:pfam05557 235 RKLEREEKYREEA----ATLELEKEKLEQELQSWVKLaqdtglnlrspedlsrrIEQLQQREIVLKEENSSLTSSARQLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1324 KAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEelEEAKKKLAQRLQEAEEA 1403
Cdd:pfam05557 311 KARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTM--SNYSPQLLERIEEAEDM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1404 VEAVNAKCSSLEktkHRLQNEIEDLMVDVERSNAAAAALDKKQRNfdkilaewkqkyeesqseleSSQKEARSLSTELFK 1483
Cdd:pfam05557 389 TQKMQAHNEEME---AQLSVAEEELGGYKQQAQTLERELQALRQQ--------------------ESLADPSYSKEEVDS 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1484 LKNAYEESLEHLETFKRENKNLQEEISDLTEQLG---SSGKTIH---------------ELEKVRKQLEAEKMELQSALE 1545
Cdd:pfam05557 446 LRRKLETLELERQRLREQKNELEMELERRCLQGDydpKKTKVLHlsmnpaaeayqqrknQLEKLQAEIERLKRLLKKLED 525
|
570 580
....*....|....*....|....*...
gi 1034587182 1546 EAEASLEHEEGKILRAQLEFNQIKAEIE 1573
Cdd:pfam05557 526 DLEQVLRLPETTSTMNFKEVLDLRKELE 553
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1628-1833 |
7.35e-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: 43.09 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1628 QLSHANRMAAEAQKQVKSLQSLLKDTQIQLDdavRANDDLKENiaiverrnnllQAELEELRAVVEQTERSRKLAEQELI 1707
Cdd:pfam00261 23 KLEEAEKRAEKAEAEVAALNRRIQLLEEELE---RTEERLAEA-----------LEKLEEAEKAADESERGRKVLENRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1708 ETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLE------- 1780
Cdd:pfam00261 89 KDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEaseekas 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034587182 1781 RMKKNMEQTIKDLQHRLDEAEQIALKGgKKQLQKLEARVRELENELEAEQKRN 1833
Cdd:pfam00261 169 EREDKYEEQIRFLTEKLKEAETRAEFA-ERSVQKLEKEVDRLEDELEAEKEKY 220
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
800-1064 |
7.60e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 800 EYKKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAEREKEMASMKeeftrlKEALEKSEARRKELEEKMVS 879
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK------AEELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 880 LLQEKNDLQLQVQAEQDNLADAEErcdqlIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRdiddlel 959
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAE-----EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK------- 1709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 960 tlaKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQalddlQAEEDKVNTLTKAKVKLEQQVDDL----- 1034
Cdd:PTZ00121 1710 ---KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-----EEEKKKIAHLKKEEEKKAEEIRKEkeavi 1781
|
250 260 270
....*....|....*....|....*....|.
gi 1034587182 1035 -EGSLEQEKKVRMDLERAKRKLEGDLKLTQE 1064
Cdd:PTZ00121 1782 eEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
873-1151 |
7.78e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.76 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 873 LEEKMVSLLQEKNDLQLQVQAEQDN--------LADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLE 944
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAEPSRlyslyekeIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 945 DECSELKRDIDdlELTLAKVEkekhaTENKVKNLTEEMAGLDEIiakLTKEKKALQEAHQQalDDLQAEEDKVNT--LTK 1022
Cdd:pfam00038 103 NDLVGLRKDLD--EATLARVD-----LEAKIESLKEELAFLKKN---HEEEVRELQAQVSD--TQVNVEMDAARKldLTS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1023 AKVKLEQQVDdlegslEQEKKVRMDLERA-KRKLEgdlKLTQESIMDLEnDKQQLDERLKKKDFELNALNARIEDEQALG 1101
Cdd:pfam00038 171 ALAEIRAQYE------EIAAKNREEAEEWyQSKLE---ELQQAAARNGD-ALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1102 SQLQKKLKELQARIEEleeeleaertARAKVEKLRSDLSRELEEISERLE 1151
Cdd:pfam00038 241 ASLERQLAETEERYEL----------QLADYQELISELEAELQETRQEMA 280
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1572-1926 |
8.27e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.51 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1572 IERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEAlrvkkKMEGDLNEMEIQLSHANRMAAEAQK---QVKSLQS 1648
Cdd:PLN02939 61 SNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRA-----SMQRDEAIAAIDNEQQTNSKDGEQLsdfQLEDLVG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1649 LLKDTQ---IQLDDA-VRANDDLKEniaiVERRNNLLQAELEELRAVVEQTERSRKLAEQELIetseRVQLLHSQntsLI 1724
Cdd:PLN02939 136 MIQNAEkniLLLNQArLQALEDLEK----ILTEKEALQGKINILEMRLSETDARIKLAAQEKI----HVEILEEQ---LE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1725 NQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTS---AHLERMKKNMEQTIKDLQHRLDEAE 1801
Cdd:PLN02939 205 KLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1802 QIALKGGKKQLQKLEARVRELENELEAEQKRNAESV---KGMRKSERRIKELTYQTEEDRKNLLRLQdLVDKLQLKVKAY 1878
Cdd:PLN02939 285 EDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAAlvlDQNQDLRDKVDKLEASLKEANVSKFSSY-KVELLQQKLKLL 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1034587182 1879 KRQAEEAEEQANTnlskfrKVQHELDEAEERADIAESQVNKLRAKSRD 1926
Cdd:PLN02939 364 EERLQASDHEIHS------YIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
850-1173 |
8.63e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 850 ASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDE 929
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 930 EEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAH-QQALD 1008
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1009 DLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELN 1088
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1089 ALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKRE 1168
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
....*
gi 1034587182 1169 AEFQK 1173
Cdd:COG4372 347 LVGLL 351
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1475-1910 |
1.04e-03 |
|
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: 44.19 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1475 RSLSTELFKLKNAYEESLEHLEtfkrenKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHE 1554
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLT------LRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1555 EGKiLRAQLEFNQIKAEIERKLA-EKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEiQLSHAN 1633
Cdd:TIGR00618 253 EEQ-LKKQQLLKQLRARIEELRAqEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRA-KLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1634 RMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQ----------AELEELRAVVEQTERSRKLAE 1703
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhihtlqqqktTLTQKLQSLCKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1704 QELIETSE----RVQLLHSQNTSLINQKKKMD-----ADLSQLQTEVEEAVQECRNA-EEKAKKAITDAAMMAEELKKEQ 1773
Cdd:TIGR00618 411 TIDTRTSAfrdlQGQLAHAKKQQELQQRYAELcaaaiTCTAQCEKLEKIHLQESAQSlKEREQQLQTKEQIHLQETRKKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1774 DTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGG-----------KKQLQKLEARVRELENELEAEQKRNAESVKGMRK 1842
Cdd:TIGR00618 491 VVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPltrrmqrgeqtYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ 570
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034587182 1843 SERRIKELTYQTEEDRKNLL----RLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERA 1910
Cdd:TIGR00618 571 SFSILTQCDNRSKEDIPNLQnitvRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA 642
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1622-1763 |
1.10e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1622 LNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQA---------ELEELRAVV 1692
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 1693 EQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAA 1763
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1766-1917 |
1.12e-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: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1766 AEELKKEQDTSAHLERMKKNMEQTIKDLQhrldeaeqialkggkKQLQKLEARVRELENELEAEQKRNAES---VKGMRK 1842
Cdd:COG2433 391 PEEEPEAEREKEHEERELTEEEEEIRRLE---------------EQVERLEAEVEELEAELEEKDERIERLereLSEARS 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1843 SERR-------IKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRqAEEAEEQANT----NLSKFRKvqHELDEAEERAD 1911
Cdd:COG2433 456 EERReirkdreISRLDREIERLERELEEERERIEELKRKLERLKE-LWKLEHSGELvpvkVVEKFTK--EAIRRLEEEYG 532
|
....*.
gi 1034587182 1912 IAESQV 1917
Cdd:COG2433 533 LKEGDV 538
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1076-1238 |
1.22e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1076 LDERLKKKDFELNALNARIED-------EQALGSQLQKKLKELQARIEELEEEleaertaRAKVEKLRSDLSRELEEISE 1148
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAEladllslERQGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1149 RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAAL---RKKHADS---VAELGEQIDN--LQRVKQkLEKE 1220
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALdasEKRDRESqakIADLGRRLNValAQRVQE-LNRY 195
|
170
....*....|....*...
gi 1034587182 1221 KSEFKLELDDVTSNMEQI 1238
Cdd:PRK09039 196 RSEFFGRLREILGDREGI 213
|
|
| 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 1034587182 914 QLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 993
Cdd:PRK15374 103 QLESRLAVWQAMIESQKEMGIQVSKEFQTALGEAQEATDLYEASIKKTDTAKSVYDAAEKKLTQAQNKLQSLDPADPGYA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 994 KEKKALQEAHQQALDDLQAEEDK----VNTLTKAKVKLEQQvDDLEGSLEQEKKVRMDLERAK---RKLEGDLKLTQESI 1066
Cdd:PRK15374 183 QAEAAVEQAGKEATEAKEALDKAtdatVKAGTDAKAKAEKA-DNILTKFQGTANAASQNQVSQgeqDNLSNVARLTMLMA 261
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034587182 1067 MDLENDKQQLDERLKKkdfELNALNARIEDEQAlgsQLQKKLKELQARI 1115
Cdd:PRK15374 262 MFIEIVGKNTEESLQN---DLALFNALQEGRQA---EMEKKSAEFQEET 304
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1578-1922 |
1.40e-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: 43.35 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1578 EKDEEMEQAKRNHLRVVDS---LQTSLDAETRSRNEALR----VKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLL 1650
Cdd:pfam07888 10 EEESHGEEGGTDMLLVVPRaelLQNRLEECLQERAELLQaqeaANRQREKEKERYKRDREQWERQRRELESRVAELKEEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1651 KDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKM 1730
Cdd:pfam07888 90 RQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1731 DADLSQLQTEVEEAVQECRNaeekakkaitdaamMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQ--IALKGG 1808
Cdd:pfam07888 170 EAERKQLQAKLQQTEEELRS--------------LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeAENEAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1809 KKQLQKLEARVRELENELEAeQKRNAESVKGMRksERRIKELTYQTEEDRKNLLRLQDLvdKLQLKVKAYKRQAEEAEEQ 1888
Cdd:pfam07888 236 LEELRSLQERLNASERKVEG-LGEELSSMAAQR--DRTQAELHQARLQAAQLTLQLADA--SLALREGRARWAQERETLQ 310
|
330 340 350
....*....|....*....|....*....|....*.
gi 1034587182 1889 ANTNLSKFR--KVQHELDEAEERADIAESQVNKLRA 1922
Cdd:pfam07888 311 QSAEADKDRieKLSAELQRLEERLQEERMEREKLEV 346
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
852-1106 |
1.45e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.69 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 852 MKEEFTRLKEALEKSEARRK----ELEEKMVSLLQEKN------------DLQLQVQAEQDNLADAEERCDQLIKNKIQL 915
Cdd:PLN03229 484 LQERLENLREEFSKANSQDQlmhpVLMEKIEKLKDEFNkrlsrapnylslKYKLDMLNEFSRAKALSEKKSKAEKLKAEI 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 916 EAKVKEMNERLEDEEEMNAeltakkRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMaGLDEIIAKltke 995
Cdd:PLN03229 564 NKKFKEVMDRPEIKEKMEA------LKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSM-GLEVIGVT---- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 996 KKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKkvrmdLERAKRKLEGDLKlTQESIMDLEND-KQ 1074
Cdd:PLN03229 633 KKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSKIELLK-----LEVAKASKTPDVT-EKEKIEALEQQiKQ 706
|
250 260 270
....*....|....*....|....*....|....*...
gi 1034587182 1075 QLDE-----RLKKKDFELNA-LNARIEDEQALGSQLQK 1106
Cdd:PLN03229 707 KIAEalnssELKEKFEELEAeLAAARETAAESNGSLKN 744
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1649-1923 |
1.50e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.77 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1649 LLKDTQIQLDDAVRANDDLKEniaiverrnnlLQAELEELRAVVEQTERSRKLAE-QELietseRVQLLHSQNTSLINQK 1727
Cdd:PLN03188 951 LLKEKYENHPEVLRTKIELKR-----------VQDELEHYRNFYDMGEREVLLEEiQDL-----RSQLQYYIDSSLPSAR 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1728 KK---------MDADLSQLQTEVEEAVQECrnAEEKAKK-------AITDAAMMAEELKKEQDTSAHLERMKKNMEQTIK 1791
Cdd:PLN03188 1015 KRnsllkltysCEPSQAPPLNTIPESTDES--PEKKLEQerlrwteAESKWISLAEELRTELDASRALAEKQKHELDTEK 1092
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1792 DLQHRLDEAEQIALKGGKKQLQK----------LEARVRELENELEAEQKrnAESVKGMRKSERR--------IKELTYQ 1853
Cdd:PLN03188 1093 RCAEELKEAMQMAMEGHARMLEQyadleekhiqLLARHRRIQEGIDDVKK--AAARAGVRGAESKfinalaaeISALKVE 1170
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587182 1854 TEEDRKnllRLQDLVDKLQLKVkaykRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAE-------SQVNKLRAK 1923
Cdd:PLN03188 1171 REKERR---YLRDENKSLQAQL----RDTAEAVQAAGELLVRLKEAEEALTVAQKRAMDAEqeaaeayKQIDKLKRK 1240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1388-1619 |
1.54e-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: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1388 EAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSEL 1467
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1468 ESSQKEARSLSTELFKLKNAYEESL----EHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSA 1543
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587182 1544 LEEAEASleheegkilraqlefnqiKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKME 1619
Cdd:COG4942 180 LAELEEE------------------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
846-1115 |
1.62e-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: 43.21 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 846 EKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDN--LADAEERCDQLIKNKIQLEAKVKEmN 923
Cdd:pfam09731 160 KAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPplLDAAPETPPKLPEHLDNVEEKVEK-A 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 924 ERLEDEEEMNAELTAKKRklEDECSELKRDIDDLELTLAKVEKEKHATENKVknLTEEMAGLDEIIAKLTKEKKALQEAH 1003
Cdd:pfam09731 239 QSLAKLVDQYKELVASER--IVFQQELVSIFPDIIPVLKEDNLLSNDDLNSL--IAHAHREIDQLSKKLAELKKREEKHI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1004 QQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMD-----LENDKQQLDE 1078
Cdd:pfam09731 315 ERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEhlkdvLVEQEIELQR 394
|
250 260 270
....*....|....*....|....*....|....*..
gi 1034587182 1079 RLKKKdfelnaLNARIEDEQALgsqLQKKLKELQARI 1115
Cdd:pfam09731 395 EFLQD------IKEKVEEERAG---RLLKLNELLANL 422
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
852-998 |
1.72e-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: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 852 MKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAeercdQLIKNKI-QLEAKVKEMNERLEdee 930
Cdd:pfam10186 17 ARNRLYELRVDLARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKL-----RLLKSEVaISNERLNEIKDKLD--- 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587182 931 EMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 998
Cdd:pfam10186 89 QLRREIAEKKKKIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRS 156
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1562-1836 |
1.77e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.50 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1562 QLEFNQIKAEIERklAEKDEEMEQAKrnhlrVVDSLQTSLDAetrsrnealrvkkkmegdLNEMEIqlshANRMAAEAQK 1641
Cdd:PRK10929 22 APDEKQITQELEQ--AKAAKTPAQAE-----IVEALQSALNW------------------LEERKG----SLERAKQYQQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1642 QVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAE---LEELRAVVEQTERSRKLAE-------------QE 1705
Cdd:PRK10929 73 VIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSsqlLEKSRQAQQEQDRAREISDslsqlpqqqtearRQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1706 LIETSERVQLLHSQNTSLiNQkkkmdADLSQLQteveeavqecrnAEEKAKKAITDaammaeELKkeqdtsahLERMKKN 1785
Cdd:PRK10929 153 LNEIERRLQTLGTPNTPL-AQ-----AQLTALQ------------AESAALKALVD------ELE--------LAQLSAN 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 1786 MEQTIKDLQHRLdeaeqialkgGKKQLQKLEARVRELENELEAEQKRNAES 1836
Cdd:PRK10929 201 NRQELARLRSEL----------AKKRSQQLDAYLQALRNQLNSQRQREAER 241
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1273-1909 |
1.78e-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: 43.27 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1273 LTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTY--------------------------------TQQLEDLKRQLE 1320
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKTFwspelkkeralrkeeaarisvlkeqyrvtqeeNQHLQLTIQALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1321 EEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSevaqwRTKYETDAIQRT-EELE------------ 1387
Cdd:pfam10174 81 DELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHE-----RQAKELFLLRKTlEEMElrietqkqtlga 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1388 --EAKKKLAQRLQ------EAEEAVEAVNAKCSSLEKTKHRL-----QNEIEDLMVDVE-RSNAAAAALDKKQRNFDKIL 1453
Cdd:pfam10174 156 rdESIKKLLEMLQskglpkKSGEEDWERTRRIAEAEMQLGHLevlldQKEKENIHLREElHRRNQLQPDPAKTKALQTVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1454 AEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQL 1533
Cdd:pfam10174 236 EMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1534 EAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKlaekdEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALR 1613
Cdd:pfam10174 316 TNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEK-----ESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1614 VKKK----MEGDLNEMEIQLSHANRMAAEAQKQVKSLQ-------SLLKDTQIQLDDAVRANDDLKENIaivERRNNLLQ 1682
Cdd:pfam10174 391 VKERkinvLQKKIENLQEQLRDKDKQLAGLKERVKSLQtdssntdTALTTLEEALSEKERIIERLKEQR---EREDRERL 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1683 AELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAitda 1762
Cdd:pfam10174 468 EELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKA---- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1763 ammaeelkkeqDTSAHLERMKKNMEQTIKDLQHrldEAEQIALKGGKKQ--LQKLEARVRELENELEAEQKRNAE----- 1835
Cdd:pfam10174 544 -----------HNAEEAVRTNPEINDRIRLLEQ---EVARYKEESGKAQaeVERLLGILREVENEKNDKDKKIAEleslt 609
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587182 1836 --SVKGMRKSERRIKELtyQTEEDRKNLLRLQD-LVDKLQLKVKAYKRQAEEAeeqantnLSKFRKVQHELDEAEER 1909
Cdd:pfam10174 610 lrQMKEQNKKVANIKHG--QQEMKKKGAQLLEEaRRREDNLADNSQQLQLEEL-------MGALEKTRQELDATKAR 677
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
923-1319 |
2.00e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 923 NERLEDEEEMNAEL-TAKKRKLEDEcsELKRDIDDLELTL---AKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 998
Cdd:PRK11281 32 NGDLPTEADVQAQLdALNKQKLLEA--EDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 999 LQEAHQQALDDLQAEEdkvntltkakvkLEQQVDDLEGSLEQekkVRMDL--------------ERAKRKLEGDLKLTQE 1064
Cdd:PRK11281 110 NDEETRETLSTLSLRQ------------LESRLAQTLDQLQN---AQNDLaeynsqlvslqtqpERAQAALYANSQRLQQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1065 ----SIMDLENDKQQLDERLKKKDFELNALNARIEDEQAL---GSQLQ----KKLKELQARIEELEEELEAERTArakVE 1133
Cdd:PRK11281 175 irnlLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSlegNTQLQdllqKQRDYLTARIQRLEHQLQLLQEA---IN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1134 KLRSDLSRELEEISERLEEAGgatsvQIEMNK--KREAEF-QKMRRDLEEATLQ-HEATAAALRKKHA-DSVAE----LG 1204
Cdd:PRK11281 252 SKRLTLSEKTVQEAQSQDEAA-----RIQANPlvAQELEInLQLSQRLLKATEKlNTLTQQNLRVKNWlDRLTQsernIK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1205 EQIDNLQ------RV--KQKLekeksefKLELDDVTSNM-EQIikakANLekmcRTLEDQMNEHRSKAEETQRSVNDLts 1275
Cdd:PRK11281 327 EQISVLKgslllsRIlyQQQQ-------ALPSADLIEGLaDRI----ADL----RLEQFEINQQRDALFQPDAYIDKL-- 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1034587182 1276 qrakLQTENGELSRQldEKEALISQL-TRGKLtytqqLEDLKRQL 1319
Cdd:PRK11281 390 ----EAGHKSEVTDE--VRDALLQLLdERREL-----LDQLNKQL 423
|
|
| F-BAR_PSTPIP2 |
cd07672 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
1232-1424 |
2.09e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 2; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 2 (PSTPIP2), also known as Macrophage Actin-associated tYrosine Phosphorylated protein (MAYP), is mostly expressed in hematopoietic cells but is also expressed in the brain. It is involved in regulating cell adhesion and motility. Mutations in the gene encoding murine PSTPIP2 can cause autoinflammatory disorders such as chronic multifocal osteomyelitis and macrophage autoinflammatory disease. PSTPIP2 contains an N-terminal F-BAR domain and lacks the PEST motifs and SH3 domain that are found in PSTPIP1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153356 [Multi-domain] Cd Length: 240 Bit Score: 41.86 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1232 TSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQ 1311
Cdd:cd07672 4 TGGYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKKPCGQTEINTLKRSLDVFKQQIDNVGQSHIQLAQT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1312 LEDLKRQLE---EEVKAKNALAHALQSARHDCDLLreQYEEETEAKAEL-QRVLSKANSEVAQWRTKYETDAIQRteelE 1387
Cdd:cd07672 84 LRDEAKKMEdfrERQKLARKKIELIMDAIHKQRAM--QFKKTMESKKNYeQKCRDKDEAEQAVNRNANLVNVKQQ----E 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034587182 1388 EAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNE 1424
Cdd:cd07672 158 KLFAKLAQSKQNAEDADRLYMQNISVLDKIREDWQKE 194
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
846-1036 |
2.23e-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: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 846 EKEMASMKEEFTR-LKEALEKSEARRKELEE----KMVSLLQEKNDLQLQVQAEQDNLAdaEERCDQLIK------NKIQ 914
Cdd:pfam12128 695 DKKHQAWLEEQKEqKREARTEKQAYWQVVEGaldaQLALLKAAIAARRSGAKAELKALE--TWYKRDLASlgvdpdVIAK 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 915 LEAKVKEMNERLEDEEEMNAE------------------LTAKKRKLEDECSELK----RDIDDLELTLAKVEKEKHATE 972
Cdd:pfam12128 773 LKREIRTLERKIERIAVRRQEvlryfdwyqetwlqrrprLATQLSNIERAISELQqqlaRLIADTKLRRAKLEMERKASE 852
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587182 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 |
2.62e-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: 42.57 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVK 920
Cdd:pfam07888 144 RVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 921 EMNERLEDEEEMNAELTAKKRKLE--DECSE-LKRDIDDLELTLAKVEKEKHATENKVKNLTEEMA----GLDEIIAKLT 993
Cdd:pfam07888 224 TAHRKEAENEALLEELRSLQERLNasERKVEgLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLAdaslALREGRARWA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 994 KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKV-RMDLERAKRKLE---GDLKLTQESIMDL 1069
Cdd:pfam07888 304 QERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCnRVQLSESRRELQelkASLRVAQKEKEQL 383
|
250
....*....|...
gi 1034587182 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 ... |
1585-1859 |
2.65e-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: 42.11 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1585 QAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSllkdtqiQLDDAVRAN 1664
Cdd:pfam15905 66 QKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEK-------QLLELTRVN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1665 DDLKENIAI--VERRNNLLQAELEELRAVVEQTERSrKLAEQELIEtserVQLLHSQNTslINQKKKMDADLSQLQTEVE 1742
Cdd:pfam15905 139 ELLKAKFSEdgTQKKMSSLSMELMKLRNKLEAKMKE-VMAKQEGME----GKLQVTQKN--LEHSKGKVAQLEEKLVSTE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1743 EAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlkggKKQLQKLEARVREL 1822
Cdd:pfam15905 212 KEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL----SKQIKDLNEKCKLL 287
|
250 260 270
....*....|....*....|....*....|....*...
gi 1034587182 1823 ENELEAEQKRNAESVKGMRKSERRIKE-LTYQTEEDRK 1859
Cdd:pfam15905 288 ESEKEELLREYEEKEQTLNAELEELKEkLTLEEQEHQK 325
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1001-1263 |
2.68e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1001 EAHQQALD---DLQAEEDKVNTLTKAKVKLEQQVDDLEGSlEQEKKVRMD-LERAKRKLEgDLKLTQESIMDLENDKQQL 1076
Cdd:COG0497 141 DAQRELLDafaGLEELLEEYREAYRAWRALKKELEELRAD-EAERARELDlLRFQLEELE-AAALQPGEEEELEEERRRL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1077 D--ERLKKKDFE-LNALNariEDEQALGSQLQKklkelqarieeleeeleaertARAKVEKLrSDLSRELEEISERLEEA 1153
Cdd:COG0497 219 SnaEKLREALQEaLEALS---GGEGGALDLLGQ---------------------ALRALERL-AEYDPSLAELAERLESA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1154 ggatSVQIEmnkkrEA--EFQKMRRDLE------EATLQHEATAAALRKKHADSVAELgeqIDNLQRVKQKLEkeksefk 1225
Cdd:COG0497 274 ----LIELE-----EAasELRRYLDSLEfdperlEEVEERLALLRRLARKYGVTVEEL---LAYAEELRAELA------- 334
|
250 260 270
....*....|....*....|....*....|....*...
gi 1034587182 1226 lELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKA 1263
Cdd:COG0497 335 -ELENSDERLEELEAELAEAEAELLEAAEKLSAARKKA 371
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
847-1043 |
2.75e-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: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 847 KEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM---- 922
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESergr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 923 ----NERLEDEEEMN---AELTAKKRKLED---ECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKL 992
Cdd:pfam00261 81 kvleNRALKDEEKMEileAQLKEAKEIAEEadrKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587182 993 -TKEKKALQ------EAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKK 1043
Cdd:pfam00261 161 eASEEKASEredkyeEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
949-1754 |
2.80e-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: 43.02 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 949 ELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAgldeiiaKLTKEKKALQEAHQQALDDLQaeedKVNTLTKAKVKLE 1028
Cdd:COG3096 282 ELSERALELRRELFGARRQLAEEQYRLVEMARELE-------ELSARESDLEQDYQAASDHLN----LVQTALRQQEKIE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1029 QQVDDLEG---SLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLEN---DKQQ-LDERLKKKDFELNALNARIEDEQALG 1101
Cdd:COG3096 351 RYQEDLEElteRLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSqlaDYQQaLDVQQTRAIQYQQAVQALEKARALCG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1102 ------SQLQKKLKELQARieeLEEELEAERTARAKVEkLRSDLSRELEEISERLEEAGGATSvqiemnkkREAEFQKMR 1175
Cdd:COG3096 431 lpdltpENAEDYLAAFRAK---EQQATEEVLELEQKLS-VADAARRQFEKAYELVCKIAGEVE--------RSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1176 RDLEEA-TLQHEA-TAAALRKKHADSVAELGEQidnlqrvkQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLE 1253
Cdd:COG3096 499 ELLRRYrSQQALAqRLQQLRAQLAELEQRLRQQ--------QNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELE 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1254 DQMNEHRSKAEETQRSVNDLTSQRAKLqTENGELSRQLDEKEALISQLTRGKLTYTQQLED-LKRQLEEEVKAKNALAHA 1332
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKEL-AARAPAWLAAQDALERLREQSGEALADSQEVTAaMQQLLEREREATVERDEL 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1333 LQSARHdcdlLREQYEEETEAK-AELQRVLSKAN-------SEVaqwrtkYETDAIQR----------------TEELEE 1388
Cdd:COG3096 650 AARKQA----LESQIERLSQPGgAEDPRLLALAErlggvllSEI------YDDVTLEDapyfsalygparhaivVPDLSA 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1389 AKKKLAQR-----------------------LQEAEEAVEAVNAK---------------CSSLEKTKHRLQNEIEDLmv 1430
Cdd:COG3096 720 VKEQLAGLedcpedlyliegdpdsfddsvfdAEELEDAVVVKLSDrqwrysrfpevplfgRAAREKRLEELRAERDEL-- 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1431 dVERSNAAAAALDKKQR---NFDKILAEWKQkyeesqsELESSQKEArslstELFKLKNAYEESLEHLETFKRENKNLQE 1507
Cdd:COG3096 798 -AEQYAKASFDVQKLQRlhqAFSQFVGGHLA-------VAFAPDPEA-----ELAALRQRRSELERELAQHRAQEQQLRQ 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1508 EISDLTEQLGSSGKTIHEL-----EKVRKQLEAEKMELQSAlEEAEASLEhEEGKILRaQLE------------FNQIKA 1570
Cdd:COG3096 865 QLDQLKEQLQLLNKLLPQAnlladETLADRLEELREELDAA-QEAQAFIQ-QHGKALA-QLEplvavlqsdpeqFEQLQA 941
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1571 EIERKLAEKDEEMEQ--------AKRNHLRVVDSLQtsLDAETRSRNEALRVKkkmegdLNEMEIQLSHANRMAAEAQKQ 1642
Cdd:COG3096 942 DYLQAKEQQRRLKQQifalsevvQRRPHFSYEDAVG--LLGENSDLNEKLRAR------LEQAEEARREAREQLRQAQAQ 1013
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1643 VKSLQSLLKDtqiqLDDAVRA-NDDLKEniaiverrnnlLQAELEEL--RAVVEQTERSRklaeqelietsERVQLLHSQ 1719
Cdd:COG3096 1014 YSQYNQVLAS----LKSSRDAkQQTLQE-----------LEQELEELgvQADAEAEERAR-----------IRRDELHEE 1067
|
890 900 910
....*....|....*....|....*....|....*
gi 1034587182 1720 NTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEK 1754
Cdd:COG3096 1068 LSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERD 1102
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
1762-1931 |
2.96e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 42.28 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1762 AAMMAEELKKEQDTSAHLERMKKNMEQTikdlQHRLDEAEQI--ALKGGKKQLQKLEARVRELENELEAEQKRNAESVKG 1839
Cdd:PRK10361 28 AQQKAEQLAEREEMVAELSAAKQQITQS----EHWRAECELLnnEVRSLQSINTSLEADLREVTTRMEAAQQHADDKIRQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1840 MRKSERRIKE----LTYQTEE------DRKNLLRLQDLVDKLQLKVKAYKRQAEEA---EEQANTNLSkfrkvqHELDEA 1906
Cdd:PRK10361 104 MINSEQRLSEqfenLANRIFEhsnrrvDEQNRQSLNSLLSPLREQLDGFRRQVQDSfgkEAQERHTLA------HEIRNL 177
|
170 180
....*....|....*....|....*.
gi 1034587182 1907 EE-RADIAESQVNKLRAKSRDIGTKG 1931
Cdd:PRK10361 178 QQlNAQMAQEAINLTRALKGDNKTQG 203
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
839-1112 |
2.97e-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: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 839 LLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEekmvsllQEKNDLqlqvqaeQDNLADAEERCDQLIKNKIQLEAK 918
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQ-------QERDEL-------ADEIASGASGKSALQDEKRRLEAR 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 919 VKEMNERLEdEEEMNAELTAKK-RKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEmagldeiiakltkekk 997
Cdd:pfam01576 891 IAQLEEELE-EEQSNTELLNDRlRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAK---------------- 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 998 alqeahqqalddLQAEEDKVNTLTKAKVK-LEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQL 1076
Cdd:pfam01576 954 ------------LQEMEGTVKSKFKSSIAaLEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQY 1021
|
250 260 270
....*....|....*....|....*....|....*.
gi 1034587182 1077 DERLKKKDFELNALNARIEDEQALGSQLQKKLKELQ 1112
Cdd:pfam01576 1022 KDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQ 1057
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1640-1886 |
2.98e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1640 QKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHsQ 1719
Cdd:pfam02029 69 AKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWS-T 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1720 NTSLINQKKKMDADLSQLQTEVE------EAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDL 1793
Cdd:pfam02029 148 EVRQAEEEGEEEEDKSEEAEEVPtenfakEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1794 ----QHRLDEAEQIALKGGKKQLQKLEARVRELENElEAEQKRNA--------ESVKGMRKSERRIKELTYQTEEDRKNL 1861
Cdd:pfam02029 228 gglsQSQEREEEAEVFLEAEQKLEELRRRRQEKESE-EFEKLRQKqqeaelelEELKKKREERRKLLEEEEQRRKQEEAE 306
|
250 260
....*....|....*....|....*
gi 1034587182 1862 LRLQDLVDKLQLKVKAYKRQAEEAE 1886
Cdd:pfam02029 307 RKLREEEEKRRMKEEIERRRAEAAE 331
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
948-1248 |
3.13e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 948 SELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKL 1027
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1028 EQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKK 1107
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1108 LKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEA 1187
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 1188 TAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKM 1248
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
902-1043 |
3.14e-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: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 902 EERCDQLIKNKIQLEAKVKEMNErleDEEEMNAELTakkrkledECSELKRDIDDLELTL-AKVEKEKHATENKVKNLTE 980
Cdd:smart00787 136 EWRMKLLEGLKEGLDENLEGLKE---DYKLLMKELE--------LLNSIKPKLRDRKDALeEELRQLKQLEDELEDCDPT 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034587182 981 EMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKK 1043
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1749-1914 |
3.33e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1749 RNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQTIKDLQHRLdeaeqialkggkkqLQKLEARVRELENELEA 1828
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKE------AEAIKKEALLEAKEEIHKL--------------RNEFEKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1829 EQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQAnTNLSKFRKVQHELDEAEE 1908
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI-SGLTAEEAKEILLEKVEE 165
|
....*...
gi 1034587182 1909 --RADIAE 1914
Cdd:PRK12704 166 eaRHEAAV 173
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1165-1320 |
3.49e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 42.35 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1165 KKREAEFQKMRRDLEEATLQheATAAALRKKHADS-VAELGEQIDNLqrvkqkleKEKSEFKLElddvtsnmEQIIKAKA 1243
Cdd:pfam05911 20 EKAEAEALALKQQLESVTLQ--KLTAEERAAHLDGaLKECMQQLRNV--------KEEQEQKIH--------DVVLKKTK 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587182 1244 NLEKMCRTLEDQMNEhrskaeetqrsvndlTSQR-AKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLE 1320
Cdd:pfam05911 82 EWEKIKAELEAKLVE---------------TEQElLRAAAENDALSRSLQERENLLMKLSEEKSQAEAEIEALKSRLE 144
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
1645-1754 |
3.58e-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: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1645 SLQSLLKDT-QIQLDDAVRANDDLKENIAIVE-----------RRNNLL---------QAELEELRAVVEQTERSRKLAE 1703
Cdd:pfam05266 50 SFAGLLEKVkKLQVDDSRSVFESLMESFAELEkhgfdvkapqsRINKLLslkdrqtklLEELKKLEKKIAEEESEKRKLE 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 1704 QELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEK 1754
Cdd:pfam05266 130 EEIDELEKKILELERQLALAKEKKEAADKEIARLKSEAEKLEQEIQDVELE 180
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
843-1097 |
3.91e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 843 AEREKEMASMKE---EFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIknkiqlEAKV 919
Cdd:COG4913 671 AELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE------DLAR 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 920 KEMNERLED--EEEMNAELTAKKRK-LEDECSELKRDIDDLELTLAKVEKE-KHATENKVKNLTEEMAGLDEIIAKLT-- 993
Cdd:COG4913 745 LELRALLEErfAAALGDAVERELREnLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLDrl 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 994 ----------KEKKALQEAHQQALDDLQAEedkvntLTKAKVKLEQQVDDLEGSLEQ-----EKKVRMDLERAKRKlegD 1058
Cdd:COG4913 825 eedglpeyeeRFKELLNENSIEFVADLLSK------LRRAIREIKERIDPLNDSLKRipfgpGRYLRLEARPRPDP---E 895
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1034587182 1059 LKLTQESIMDLENDKQQLDERLKKKDFE-LNALNARIEDE 1097
Cdd:COG4913 896 VREFRQELRAVTSGASLFDEELSEARFAaLKRLIERLRSE 935
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1275-1795 |
4.02e-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: 42.25 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1275 SQRAKLQTENGELSRQLDEKEALI--SQLTRGKLTYTQQLEDLKRQLEEEvkAKNALAHALQSARHDCDLLREQyeeETE 1352
Cdd:COG3096 215 SLRDYLLPENSGVRKAFQDMEAALreNRMTLEAIRVTQSDRDLFKHLITE--ATNYVAADYMRHANERRELSER---ALE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1353 AKAELQRVLSKANSEvaQWRTKYETDAIqrtEELEEAKKKLAQRLQEAEEAVEAVnakcssleKTKHRLQNEIEDLMVDV 1432
Cdd:COG3096 290 LRRELFGARRQLAEE--QYRLVEMAREL---EELSARESDLEQDYQAASDHLNLV--------QTALRQQEKIERYQEDL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1433 ErsnAAAAALDKKQrnfdKILAEWKQKYEESQSELESSQKEARSLSTELFKlknaYEESLEHLETfkrenKNLQEEisdl 1512
Cdd:COG3096 357 E---ELTERLEEQE----EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD----YQQALDVQQT-----RAIQYQ---- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1513 teqlgssgKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEgkilraqlEFNQIKAEIERKLAEKDEemeqAKRNHLR 1592
Cdd:COG3096 417 --------QAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQ--------QATEEVLELEQKLSVADA----ARRQFEK 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1593 VVDSLQTSLDAETRSR-----NEALRV---KKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAvran 1664
Cdd:COG3096 477 AYELVCKIAGEVERSQawqtaRELLRRyrsQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA---- 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1665 DDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHsqntslinqkkKMDADLSQLQTEVEEA 1744
Cdd:COG3096 553 EELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL-----------AAQDALERLREQSGEA 621
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1034587182 1745 VQECRnaeekakkAITDAamMAEELKKEQDTSA---HLERMKKNMEQTIKDLQH 1795
Cdd:COG3096 622 LADSQ--------EVTAA--MQQLLEREREATVerdELAARKQALESQIERLSQ 665
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
840-1017 |
4.04e-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: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 840 LKSAEREKEmaSMKEEFTRLK-----------EALEKSEARRKELEEKMVSLlQEKNDLQ-------LQVQAEQDNLADA 901
Cdd:NF033838 206 IKQAKAKVE--SKKAEATRLEkiktdrekaeeEAKRRADAKLKEAVEKNVAT-SEQDKPKrrakrgvLGEPATPDKKEND 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 902 EERCDQLI-------------KNKIQLEAKVKEMNERLED--EEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEK 966
Cdd:NF033838 283 AKSSDSSVgeetlpspslkpeKKVAEAEKKVEEAKKKAKDqkEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEA 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034587182 967 EKHATENKVKNLTEEMAGLDEIIAKLTK----EKKALQEAHQQAlddlqAEEDKV 1017
Cdd:NF033838 363 KEPRNEEKIKQAKAKVESKKAEATRLEKiktdRKKAEEEAKRKA-----AEEDKV 412
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1771-1923 |
4.10e-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: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1771 KEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGK------KQLQKLEARVRELENELEAEQKRNAESVKGMRKSE 1844
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRqldresDRNQELQKRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034587182 1845 RRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1923
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQ 161
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1254-1447 |
4.12e-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: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1254 DQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEkealISQlTRGKLTYTQQledlkrqleeevkakNALAHAL 1333
Cdd:NF012221 1545 DAVSKHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAA----ISG-SQSQLESTDQ---------------NALETNG 1604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1334 QSARhdcDLLREQYEEETEAKAELQRVLSKANSEVA-------QWRTKYET---DAIQR---------TEELEEAKKKLA 1394
Cdd:NF012221 1605 QAQR---DAILEESRAVTKELTTLAQGLDALDSQATyagesgdQWRNPFAGgllDRVQEqlddakkisGKQLADAKQRHV 1681
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034587182 1395 QRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNaaAAALDKKQR 1447
Cdd:NF012221 1682 DNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRK--DDALAKQNE 1732
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1734-1920 |
4.24e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.78 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1734 LSQLQTEVEEAVQECRNAEEK---AKKAITDAAMMAEELKKE-QDTSAHLERMKKNMEQTikdlQHRLDEAEQIA----- 1804
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKleeAEKRAEKAEAEVAALNRRiQLLEEELERTEERLAEA----LEKLEEAEKAAdeser 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1805 -LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTE--EDRKNLL--RLQDLVDKLQL---KVK 1876
Cdd:pfam00261 79 gRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraEERAELAesKIVELEEELKVvgnNLK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034587182 1877 AYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKL 1920
Cdd:pfam00261 159 SLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL 202
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
841-1098 |
4.51e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVK 920
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 921 EMNERLedeEEMNAELTAKKRKLeDECSELKRDIDDLELTLAKVEKEKhatENKVKNLTEEMAGLDEiIAKLTKEKKALQ 1000
Cdd:COG1340 82 ELNEKL---NELREELDELRKEL-AELNKAGGSIDKLRKEIERLEWRQ---QTEVLSPEEEKELVEK-IKELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1001 EAHQQ------ALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQ 1074
Cdd:COG1340 154 KALEKneklkeLRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEII 233
|
250 260
....*....|....*....|....
gi 1034587182 1075 QLDERLKKKDFELNALNARIEDEQ 1098
Cdd:COG1340 234 ELQKELRELRKELKKLRKKQRALK 257
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1788-1927 |
4.55e-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: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1788 QTIKDLQHRLDEAEQIA--LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQ 1865
Cdd:COG1579 7 RALLDLQELDSELDRLEhrLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034587182 1866 DL--VDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1927
Cdd:COG1579 87 NNkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1128-1361 |
4.61e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1128 ARAKVEKLRSDLSRELEEISERLEEaggatsvqiEMNKKR--EAEFQKMRRDLEEATLQH---EATA-------AALRKK 1195
Cdd:pfam00038 69 ERARLQLELDNLRLAAEDFRQKYED---------ELNLRTsaENDLVGLRKDLDEATLARvdlEAKIeslkeelAFLKKN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1196 HADSVAELGEQIDNLQRVkqklekeksefkLELDDVTS-NMEQIIK-AKANLEKMC-RTLEDQMNEHRSKAEETQRSVND 1272
Cdd:pfam00038 140 HEEEVRELQAQVSDTQVN------------VEMDAARKlDLTSALAeIRAQYEEIAaKNREEAEEWYQSKLEELQQAAAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1273 LTSQRAKLQTENGELSRQLDEKEALISQLTRgkltytqQLEDLKRQLEEevkAKNALAHALQSARhdcDLLREQYEEETE 1352
Cdd:pfam00038 208 NGDALRSAKEEITELRRTIQSLEIELQSLKK-------QKASLERQLAE---TEERYELQLADYQ---ELISELEAELQE 274
|
....*....
gi 1034587182 1353 AKAELQRVL 1361
Cdd:pfam00038 275 TRQEMARQL 283
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1483-1662 |
5.05e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1483 KLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQ----------------SALEE 1546
Cdd:PHA02562 217 RKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkvikmyekggvcptctQQISE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1547 AEASLEHEEGKILRAQLEFNQIKAEIErKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEgdlnemE 1626
Cdd:PHA02562 297 GPDRITKIKDKLKELQHSLEKLDTAID-ELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIE------E 369
|
170 180 190
....*....|....*....|....*....|....*.
gi 1034587182 1627 IQLSHANRmaaeaQKQVKSLQSLLKDTQIQLDDAVR 1662
Cdd:PHA02562 370 LQAEFVDN-----AEELAKLQDELDKIVKTKSELVK 400
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
950-1111 |
5.19e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.27 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 950 LKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKAlQEAHQQALDDLQAeedKVNTLTKAKVKLEQ 1029
Cdd:pfam13851 31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN-YEKDKQSLKNLKA---RLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1030 QVDDLEgslEQEKKVRMDLERAKRKLEGDLKLTQESI----MDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQ 1105
Cdd:pfam13851 107 EHEVLE---QRFEKVERERDELYDKFEAAIQDVQQKTglknLLLEKKLQALGETLEKKEAQLNEVLAAANLDPDALQAVT 183
|
....*.
gi 1034587182 1106 KKLKEL 1111
Cdd:pfam13851 184 EKLEDV 189
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
841-1105 |
5.23e-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: 41.75 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKND--LQLQVQAEQDNLADAEERCDQLIKNKIQLEAK 918
Cdd:pfam12128 662 KQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEqkREARTEKQAYWQVVEGALDAQLALLKAAIAAR 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 919 VKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHA-------------------------TEN 973
Cdd:pfam12128 742 RSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEvlryfdwyqetwlqrrprlatqlsnIER 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 974 KVKNLTEEMAGLDE----IIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLtkAKVKLEQQVDDLEGSLEQEKKVRMDLE 1049
Cdd:pfam12128 822 AISELQQQLARLIAdtklRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL--ATLKEDANSEQAQGSIGERLAQLEDLK 899
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 1050 RAKRKLEGDLKLTQESIMDLENDKQQLD-----ERLKKKDFELNALNARIEDEQALGSQLQ 1105
Cdd:pfam12128 900 LKRDYLSESVKKYVEHFKNVIADHSGSGlaetwESLREEDHYQNDKGIRLLDYRKLVPYLE 960
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
841-1046 |
5.52e-03 |
|
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: 41.98 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 841 KSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLqlqvqaeQDNLADAEERCDQLIKNKIQLEAKVK 920
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL-------ESRLGDLKKERDELEAQLRELERKIE 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 921 EMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDL------ELTLAKVEKEKHAtenkvknLTEEMAGLDEIiakltk 994
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipeeELSLEDVQAELQR-------VEEEIRALEPV------ 973
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034587182 995 EKKALQEaHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEgslEQEKKVRM 1046
Cdd:TIGR02169 974 NMLAIQE-YEEVLKRLDELKEKRAKLEEERKAILERIEEYE---KKKREVFM 1021
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1103-1575 |
5.54e-03 |
|
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: 41.55 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1103 QLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvQIE-MNKKREAEFQKMRRDLEEA 1181
Cdd:pfam05701 39 LVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERA------QTEeAQAKQDSELAKLRVEEMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1182 TLQHEATAAA------LRKKHADSVAELG---EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQI-----------IKA 1241
Cdd:pfam05701 113 GIADEASVAAkaqlevAKARHAAAVAELKsvkEELESLRKEYASLVSERDIAIKRAEEAVSASKEIektveeltielIAT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1242 KANLEkMCRTLEDQMNEHRSKA-------------------EETQR------SVNDLTSQ----RAKLQTENGELS---- 1288
Cdd:pfam05701 193 KESLE-SAHAAHLEAEEHRIGAalareqdklnwekelkqaeEELQRlnqqllSAKDLKSKletaSALLLDLKAELAayme 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1289 ------RQLDEKEALISQLTRGKLTYTQ-QLEDLKRQLE---EEVKAKNALAHALQS----ARHDCDLLREQYEEETEAK 1354
Cdd:pfam05701 272 sklkeeADGEGNEKKTSTSIQAALASAKkELEEVKANIEkakDEVNCLRVAAASLRSelekEKAELASLRQREGMASIAV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1355 AELQRVLSKANSEVAQWRTKyETDAiqrTEELEEAKKKLAQRLQEAEEA-----------------VEAVNAKCSSLEKT 1417
Cdd:pfam05701 352 SSLEAELNRTKSEIALVQAK-EKEA---REKMVELPKQLQQAAQEAEEAkslaqaareelrkakeeAEQAKAAASTVESR 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1418 KHRLQNEIEDLMVDVERSNAAAAALDKKQrnfdkilaewkqkyeesqSELESSQKEARSLSTELfKLKNAYEESLEHLET 1497
Cdd:pfam05701 428 LEAVLKEIEAAKASEKLALAAIKALQESE------------------SSAESTNQEDSPRGVTL-SLEEYYELSKRAHEA 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587182 1498 FKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEaslEHEEGKiLRAQLEFNQIKAEIERK 1575
Cdd:pfam05701 489 EELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIALEKAE---KAKEGK-LAAEQELRKWRAEHEQR 562
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1440-1587 |
5.59e-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: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1440 AALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQE---------EIS 1510
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587182 1511 DLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAK 1587
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1100-1429 |
5.75e-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: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1100 LGSQLQKKLKEL-------QARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQ 1172
Cdd:pfam07888 32 LQNRLEECLQERaellqaqEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1173 KMRRDLEEATLQHEATAAALRKKHADSVAELGEQID---NLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMC 1249
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLEretELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1250 RTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENgelsRQLDEKEALISQL--TRGKLTYTQQ-LEDLKRQLEEEVKAK 1326
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH----RKEAENEALLEELrsLQERLNASERkVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1327 NALAHALQSARHDCDLLREQYEE------ETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTE-------------ELE 1387
Cdd:pfam07888 268 DRTQAELHQARLQAAQLTLQLADaslalrEGRARWAQERETLQQSAEADKDRIEKLSAELQRLEerlqeermereklEVE 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1034587182 1388 EAKKKLAQRLQEAEEAVEAVNAKCS--SLEKTKHRLQNEIEDLM 1429
Cdd:pfam07888 348 LGREKDCNRVQLSESRRELQELKASlrVAQKEKEQLQAEKQELL 391
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1131-1856 |
5.91e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1131 KVEKLRSDLSRELEEISERLEEAGGATSVQIEmNKKREAEFQ--KMRRDLEEATLQHEATAAALRKKHADSVAEL----- 1203
Cdd:NF041483 44 QVEVLRAKLHEARRSLASRPAYDGADIGYQAE-QLLRNAQIQadQLRADAERELRDARAQTQRILQEHAEHQARLqaelh 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1204 GEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIikaKANLEKMCRTLedqMNEHRSKAE--------ETQRsVNDLTS 1275
Cdd:NF041483 123 TEAVQRRQQLDQELAERRQTVESHVNENVAWAEQL---RARTESQARRL---LDESRAEAEqalaaaraEAER-LAEEAR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1276 QRAKLQTEN--GELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKN--ALAHALQSARHDCDLLREQYEEET 1351
Cdd:NF041483 196 QRLGSEAESarAEAEAILRRARKDAERLLNAASTQAQEATDHAEQLRSSTAAESdqARRQAAELSRAAEQRMQEAEEALR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1352 EAKAELQRVLSKANSEVAQWRTKYETDAIQRTeelEEAKKKLAQRLQEAEEAVEAVNAKCsslEKTKHRLQNEIEDLMVD 1431
Cdd:NF041483 276 EARAEAEKVVAEAKEAAAKQLASAESANEQRT---RTAKEEIARLVGEATKEAEALKAEA---EQALADARAEAEKLVAE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1432 VE---RSNAA---AAALDKKQRNFDKILAEwkqkyeesqselesSQKEARSLStelfklKNAYEESLEHLETFKRENKNL 1505
Cdd:NF041483 350 AAekaRTVAAedtAAQLAKAARTAEEVLTK--------------ASEDAKATT------RAAAEEAERIRREAEAEADRL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1506 QEEISDLTEQLGSSGKtiheleKVRKQLEAEKMELQSaleeaEASLEHEEGKILRAQL--EFNQIKAEIERKLAEKDEEM 1583
Cdd:NF041483 410 RGEAADQAEQLKGAAK------DDTKEYRAKTVELQE-----EARRLRGEAEQLRAEAvaEGERIRGEARREAVQQIEEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1584 EQAKRNHLRV----VDSLQTSLDAET-RSRNEALRVKKKMEGDLNE-MEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQL 1657
Cdd:NF041483 479 ARTAEELLTKakadADELRSTATAESeRVRTEAIERATTLRRQAEEtLERTRAEAERLRAEAEEQAEEVRAAAERAAREL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1658 -DDAVRANDDLKENIAIVERRnnlLQAELEELRAVVEQT--------ERSRKLAEQEL----IETSERVQLLHSQntsli 1724
Cdd:NF041483 559 rEETERAIAARQAEAAEELTR---LHTEAEERLTAAEEAladaraeaERIRREAAEETerlrTEAAERIRTLQAQ----- 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1725 nqkkkMDADLSQLQTE-VEEAVQECRNAEEKAKKAITDAAMMAEELKKE-QDTS--------AHLERMKKNMEQTIKDLQ 1794
Cdd:NF041483 631 -----AEQEAERLRTEaAADASAARAEGENVAVRLRSEAAAEAERLKSEaQESAdrvraeaaAAAERVGTEAAEALAAAQ 705
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587182 1795 H----RLDEAEQIaLKGGKKQLQKLEARVRELENELEAEQKR-----NAESVKGMRKSERRIKELTYQTEE 1856
Cdd:NF041483 706 EeaarRRREAEET-LGSARAEADQERERAREQSEELLASARKrveeaQAEAQRLVEEADRRATELVSAAEQ 775
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1432-1705 |
5.92e-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: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1432 VERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARslstelFKLKNAYEESLEHLETfkrENKNLQEEISD 1511
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAA------AEAEQELEESKRETET---GIQNLTAEIEQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1512 LTEQLGSSGKTIHElekvrkqlEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHL 1591
Cdd:COG5185 348 GQESLTENLEAIKE--------EIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1592 RVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEiQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENI 1671
Cdd:COG5185 420 RQIEELQRQIEQATSSNEEVSKLLNELISELNKVM-READEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLK 498
|
250 260 270
....*....|....*....|....*....|....
gi 1034587182 1672 AIVERRNNLLQAELEELRAVVEQTERSRKLAEQE 1705
Cdd:COG5185 499 ATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1525-1796 |
6.00e-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: 41.65 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1525 ELEKVRkqLEAEKMELQSALEEaEASLEHEEGKIL-RAQLEFNQ----IKAEIERKLAEKDEEMEQAKRNHLRVVDSLQT 1599
Cdd:pfam17380 349 ELERIR--QEERKRELERIRQE-EIAMEISRMRELeRLQMERQQknerVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1600 SLDAETRSRNEALRVKKKMEgdlNEMEiqlshanRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNN 1679
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERA---REME-------RVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1680 LLQAELEELRAVVEQTERSRKLAEQELIEtservqllhSQNTSLINQKKKMDADLSQLQTEVEEavqecrnaeekaKKAI 1759
Cdd:pfam17380 496 ILEKELEERKQAMIEEERKRKLLEKEMEE---------RQKAIYEEERRREAEEERRKQQEMEE------------RRRI 554
|
250 260 270
....*....|....*....|....*....|....*..
gi 1034587182 1760 TDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHR 1796
Cdd:pfam17380 555 QEQMRKATEERSRLEA---MEREREMMRQIVESEKAR 588
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1396-1589 |
6.23e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1396 RLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKyeesqselessqkeAR 1475
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR--------------IK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1476 SLSTELFKLKNAYE-ESLEH-LETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEh 1553
Cdd:COG1579 77 KYEEQLGNVRNNKEyEALQKeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE- 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1034587182 1554 EEGKILRAQLEfnQIKAEIERKLAEKDEEMEQAKRN 1589
Cdd:COG1579 156 AELEELEAERE--ELAAKIPPELLALYERIRKRKNG 189
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1071-1428 |
6.28e-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: 41.86 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1071 NDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAE-------RTARAKVEKLRSdLSREL 1143
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnlvQTALRQQEKIER-YQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1144 EEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQ------------------HEATAAALRKKHADSVAELGe 1205
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQladyqqaldvqqtraiqyQQAVQALEKARALCGLPDLT- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1206 qIDNlqrvkqkLEKEKSEFKLELDDVTSNMEQiIKAKANLEKMCRTLEDQMNE---------HRSKAEETQRSV-NDLTS 1275
Cdd:COG3096 436 -PEN-------AEDYLAAFRAKEQQATEEVLE-LEQKLSVADAARRQFEKAYElvckiagevERSQAWQTARELlRRYRS 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1276 QRAKLQTENGeLSRQLDEKEALISQLTRGKltytQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKA 1355
Cdd:COG3096 507 QQALAQRLQQ-LRAQLAELEQRLRQQQNAE----RLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1356 ELQRVLSKANSEVAQ-------WRT---KYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKcSSLEKTKHRLQNEI 1425
Cdd:COG3096 582 ELRQQLEQLRARIKElaarapaWLAaqdALERLREQSGEALADSQEVTAAMQQLLEREREATVER-DELAARKQALESQI 660
|
...
gi 1034587182 1426 EDL 1428
Cdd:COG3096 661 ERL 663
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
896-1166 |
6.39e-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: 41.09 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 896 DNLADAEercdqLIKNKIQLEAKVKEMNERLEDEEEMnaeltakkrkledecselkrDIDDLELTLAKVEKEKHATENKV 975
Cdd:pfam10498 107 DDLADEA-----LKRKNFKWKKPKYPPEEEFEEEDVV--------------------EEDDAELTLEKVEEEMLIEGDDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 976 KNLTEEmaglDEIIAKLTKEKKALQEAHQQALD------DLQAEEDKVntLTKAKVKLEQQVDDLEGSLEQ----EKKVR 1045
Cdd:pfam10498 162 KEDDED----EDLYNESTKGEEAESSKPREIIEsnvdaaEWKLELERV--LPQLKVTIKADAKDWRAHLEQmkqhKKSIE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1046 MDLERAK---RKLEGDLKLTQESIMDLE---NdkQQLDERLKkkdfELNALNARIedeqalgSQLQKKLKELQARIeele 1119
Cdd:pfam10498 236 ESLPDTKsqlDKLHTDISKTLEKIESREkyiN--SQLEPLIQ----EYREAQDEL-------SEVQEKYKQLSEGV---- 298
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034587182 1120 eeleaertarakveklrSDLSRELEEISERLEeaggatSVQIEMNKK 1166
Cdd:pfam10498 299 -----------------TERTRELAEITEELE------KVKQEMEER 322
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
846-989 |
6.43e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 846 EKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQleaKVKEMNER 925
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVK---KLEELEEE 233
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034587182 926 LEDEEEMNAELTAKKRKLEDECSELKR-----------DIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEII 989
Cdd:smart00787 234 LQELESKIEDLTNKKSELNTEIAEAEKkleqcrgftfkEIEKLKEQLKLLQSLTGWKITKLSGNTLSMTYDREIN 308
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
843-1151 |
6.48e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 843 AEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM 922
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 923 NERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKE------K 996
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaeqalD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 997 KALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQL 1076
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034587182 1077 DERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLE 1151
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1368-1507 |
6.77e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1368 VAQWRTKYETDA------IQRTEELEeakKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERsnAAAAA 1441
Cdd:PRK00409 504 IEEAKKLIGEDKeklnelIASLEELE---RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK--EAQQA 578
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587182 1442 LDKKQRNFDKILAEWKQKYEESQSELES-SQKEARSlstelfKLKNAYEESLEHLETFKRENKNLQE 1507
Cdd:PRK00409 579 IKEAKKEADEIIKELRQLQKGGYASVKAhELIEARK------RLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
864-1001 |
7.23e-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: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 864 EKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDqliKNKIQLEAKVKEMNERLEDEEEMN-----AELTA 938
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTE---KDQTALETLEKALKDLLTDEGGAIarkeiKDLQK 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034587182 939 KKRKLEDEC-SELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQE 1001
Cdd:cd22656 187 ELEKLNEEYaAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEK 250
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
924-1152 |
7.58e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 924 ERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL----DEIIAKLTKEKKAL 999
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELrekrDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1000 QEAHQQA------LDDLQAEEDKVNTLTKAKVKLEQQVDDLEG-------SLEQEKKVRMDLERAKRKLEgdlklTQESI 1066
Cdd:COG1340 81 DELNEKLnelreeLDELRKELAELNKAGGSIDKLRKEIERLEWrqqtevlSPEEEKELVEKIKELEKELE-----KAKKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1067 MDLENDKQQLDERLKKKDFELNALNARIedeQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEI 1146
Cdd:COG1340 156 LEKNEKLKELRAELKELRKEAEEIHKKI---KELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEI 232
|
....*.
gi 1034587182 1147 SERLEE 1152
Cdd:COG1340 233 IELQKE 238
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
835-1083 |
7.75e-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: 40.56 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 835 KIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAeERCDQLIKNKIQ 914
Cdd:pfam15905 68 NLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLEL-TRVNELLKAKFS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 915 LEAKVKEMN----ERLEDEEEMNA---ELTAKKRKLEDECSELKRD-------IDDLELTLAKVEKEKHATENKVKNLTE 980
Cdd:pfam15905 147 EDGTQKKMSslsmELMKLRNKLEAkmkEVMAKQEGMEGKLQVTQKNlehskgkVAQLEEKLVSTEKEKIEEKSETEKLLE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 981 EMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLK 1060
Cdd:pfam15905 227 YITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLN 306
|
250 260
....*....|....*....|...
gi 1034587182 1061 LTQESIMDLENDKQQLDERLKKK 1083
Cdd:pfam15905 307 AELEELKEKLTLEEQEHQKLQQK 329
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1524-1793 |
8.47e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1524 HELEKVRKQLEaekmELQSALEEAEASLEheegkILRAQLEfnqikaEIErKLAEKDEEMEQ--AKRNHLRVVDSLQTSL 1601
Cdd:COG0497 165 RAWRALKKELE----ELRADEAERARELD-----LLRFQLE------ELE-AAALQPGEEEEleEERRRLSNAEKLREAL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1602 daetrsrNEALRVkkkmegdLNEMEI----QLSHANRM---AAEAQKQVKSLQSLLKDTQIQLDDAVRanddlkeniaiv 1674
Cdd:COG0497 229 -------QEALEA-------LSGGEGgaldLLGQALRAlerLAEYDPSLAELAERLESALIELEEAAS------------ 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1675 errnnllqaeleELRAVVEQTErsrkLAEQELIETSERVQLLHS-------QNTSLINQKKKMDADLSQLQtEVEEAVQE 1747
Cdd:COG0497 283 ------------ELRRYLDSLE----FDPERLEEVEERLALLRRlarkygvTVEELLAYAEELRAELAELE-NSDERLEE 345
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034587182 1748 CRNAEEKAKKAITDAammAEEL-KKEQDTSAHLErmkKNMEQTIKDL 1793
Cdd:COG0497 346 LEAELAEAEAELLEA---AEKLsAARKKAAKKLE---KAVTAELADL 386
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
953-1066 |
8.48e-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: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 953 DIDDLELTLAKVEKEKHATENkvknltEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVD 1032
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100 110
....*....|....*....|....*....|....
gi 1034587182 1033 DLEgSLEQEkkvrmdLERAKRKLEGDLKLTQESI 1066
Cdd:COG0542 486 KIP-ELEKE------LAELEEELAELAPLLREEV 512
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1525-1788 |
8.57e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1525 ELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQL------EFNQIKAEIERKLAEKDEEMEQAKRNhlRVVDSL- 1597
Cdd:PRK10929 31 ELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQyqqvidNFPKLSAELRQQLNNERDEPRSVPPN--MSTDALe 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1598 ----QTS--LDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSllkdtqiqlddavranddlkENI 1671
Cdd:PRK10929 109 qeilQVSsqLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGT--------------------PNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1672 AIVERRNNLLQAELEELRAVVEQTERSRKLA--EQELIETseRVQLLHSQNTSLINQKKKMDADL-SQLQTEVEEAVQec 1748
Cdd:PRK10929 169 PLAQAQLTALQAESAALKALVDELELAQLSAnnRQELARL--RSELAKKRSQQLDAYLQALRNQLnSQRQREAERALE-- 244
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1034587182 1749 rNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 1788
Cdd:PRK10929 245 -STELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDL 283
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1528-1652 |
8.75e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 1528 KVRKQLEAEKMELQSALEEAEASLE-HEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETR 1606
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEaIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1034587182 1607 SRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKD 1652
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
835-1112 |
8.83e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 835 KIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNdlQLQVQAEQDNLADAEERCDQLIKNKIQ 914
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEE--QLAAAEAEQELEESKRETETGIQNLTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 915 --------LEAKVKEMNERLE--DEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENK-VKNLTEEMA 983
Cdd:COG5185 344 eieqgqesLTENLEAIKEEIEniVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDtLKAADRQIE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 984 GLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRmDLERAKRKLEGDLKLTQ 1063
Cdd:COG5185 424 ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNE-ELTQIESRVSTLKATLE 502
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1034587182 1064 ESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQ 1112
Cdd:COG5185 503 KLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELI 551
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
882-1058 |
9.03e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.01 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 882 QEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNA---ELTAKKRKLEDECSELKRDIDDLE 958
Cdd:PRK00106 42 QEAVNLRGKAERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSerqELKQIESRLTERATSLDRKDENLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 959 LTLAKVEKEKHATENKVKNLTEEmaglDEIIAKLTKEKkalqEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSL 1038
Cdd:PRK00106 122 SKEKTLESKEQSLTDKSKHIDER----EEQVEKLEEQK----KAELERVAALSQAEAREIILAETENKLTHEIATRIREA 193
|
170 180
....*....|....*....|....*.
gi 1034587182 1039 EQEKKVRMD------LERAKRKLEGD 1058
Cdd:PRK00106 194 EREVKDRSDkmakdlLAQAMQRLAGE 219
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
844-1152 |
9.73e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 844 EREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMN 923
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 924 ERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLE-----LTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 998
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEqelqaLSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587182 999 LQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDE 1078
Cdd:COG4372 216 LAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALEL 295
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034587182 1079 RLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEE 1152
Cdd:COG4372 296 KLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| |
