|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-768 |
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: 1345.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAIGDrgKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSK--KKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd01377 159 IAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd01377 239 ILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd01377 319 EQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKP-MGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRniKGKQEAH 577
Cdd:cd01377 399 QEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEAH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 578 FSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTGDsgksKGGKKKGSSFQTVSALHRENL 657
Cdd:cd01377 477 FILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGG----GKKKKKGGSFRTVSQLHKEQL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 658 NKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIPEGQF 737
Cdd:cd01377 553 NKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD 632
|
650 660 670
....*....|....*....|....*....|.
gi 124376530 738 iDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01377 633 -DGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
99-768 |
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: 1336.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGKQEAHF 578
Cdd:cd14916 401 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 579 SLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTGDSGKSKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENLN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 659 KLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIPEGQFI 738
Cdd:cd14916 561 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 640
|
650 660 670
....*....|....*....|....*....|
gi 124376530 739 DSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14916 641 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
99-768 |
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: 1289.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANAnKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKM-KGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14913 240 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGKQEAHF 578
Cdd:cd14913 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 579 SLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADtGDSGKSKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14913 480 SLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATAD-ADSGKKKVAKKKGSSFQTVSALFRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 659 KLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIPEGQFI 738
Cdd:cd14913 559 KLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 124376530 739 DSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14913 639 DSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
99-768 |
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: 1260.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKDNAnANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQT-PGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14917 240 VLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGKQEAHF 578
Cdd:cd14917 400 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 579 SLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADtGDSGKSKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14917 480 SLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGAD-APIEKGKGKAKKGSSFQTVSALHRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 659 KLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIPEGQFI 738
Cdd:cd14917 559 KLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 124376530 739 DSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14917 639 DSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
100-768 |
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: 1213.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASIAAIGDR-GKKDNANANK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 256
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDGpGKKAQFLATKtgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 257 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSA 336
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 337 FDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 417 SVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 497 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPR-NIKGKQE 575
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRpDKKRKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 576 AHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTGD--SGKSKGGKKKGSSFQTVSALH 653
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEdpKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 654 RENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIP 733
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 124376530 734 EGQFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14927 642 DDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
99-768 |
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: 1159.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGKQEAHF 578
Cdd:cd14923 401 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 579 SLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTGDS-GKSKGGKKKGSSFQTVSALHRENL 657
Cdd:cd14923 481 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSgGSKKGGKKKGSSFQTVSAVFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 658 NKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIPEGQF 737
Cdd:cd14923 561 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 124376530 738 IDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14923 641 IDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
99-768 |
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: 1148.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAIGDRgKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEK-KKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14918 240 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14918 320 QQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGKQEAHF 578
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 579 SLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADtGDSGKSKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14918 480 SLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAE-ADSGAKKGAKKKGSSFQTVSALFRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 659 KLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIPEGQFI 738
Cdd:cd14918 559 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 124376530 739 DSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14918 639 DSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-768 |
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: 1136.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANAN-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAF 337
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 338 DVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 498 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGKQEAH 577
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 578 FSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTGDSGKSKGGKKKGSSFQTVSALHRENL 657
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 658 NKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIPEGQF 737
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 124376530 738 IDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14910 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
99-768 |
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: 1134.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAIGDRgKKDNANANK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 256
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEK-KKEEAASGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 257 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSA 336
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 337 FDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd14915 240 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 417 SVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 497 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGKQEA 576
Cdd:cd14915 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 577 HFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTGDSGKSKGGKKKGSSFQTVSALHREN 656
Cdd:cd14915 480 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKGGKKKGSSFQTVSALFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 657 LNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIPEGQ 736
Cdd:cd14915 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 124376530 737 FIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14915 640 FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-768 |
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: 1122.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANAN-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAF 337
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 338 DVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 498 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGKQEAH 577
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 578 FSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATA--DTGDSGKSKGGKKKGSSFQTVSALHRE 655
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAegASAGGGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 656 NLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIPEG 735
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 124376530 736 QFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-768 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1096.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 87 IEDMAMLTFLHEPAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 167 TDRENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRGkkdnanaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFG 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAG-------NVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 247 KFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTnNPYDYAFVSQ-GEVSVASID 325
Cdd:pfam00063 154 KYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQsGCYTIDGID 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 326 DSEELMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRV 405
Cdd:pfam00063 233 DSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 406 KVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 484
Cdd:pfam00063 313 KTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVNE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 485 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLYDNHlGKSNN 563
Cdd:pfam00063 393 KLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 564 FQKPRNikgKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTGDSGKSKGGK--- 640
Cdd:pfam00063 471 FQKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTpkr 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 641 KKGSSFQTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 720
Cdd:pfam00063 548 TKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEF 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 124376530 721 RQRYRILNPVAIPEGqFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:pfam00063 628 VQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-768 |
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: 1064.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKdnananKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14929 155 LSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14929 234 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14929 314 EQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGKQEAHF 578
Cdd:cd14929 394 QEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHF 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 579 SLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTGdSGKSKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14929 474 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSA-IQFGEKKRKKGASFQTVASLHKENLN 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 659 KLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIPEGQFI 738
Cdd:cd14929 553 KLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFV 632
|
650 660 670
....*....|....*....|....*....|
gi 124376530 739 DSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14929 633 SSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-780 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1028.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 80 NPPKFDKIEDMAMLTFLHEPAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISD 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 160 NAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASIAAigdrgkkdnANANKGTLEDQIIQANPALEAFGNAKTVRN 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG---------SNTEVGSVEDQILESNPILEAFGNAKTLRN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 240 DNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNnPYDYAFVSQG-E 318
Cdd:smart00242 152 NNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGgC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 319 VSVASIDDSEELMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQA-EPDGTEDADKSAYLMGLNSADLL 397
Cdd:smart00242 231 LTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 398 KGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQL 477
Cdd:smart00242 311 KALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 478 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLYdN 556
Cdd:smart00242 391 CINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN-Q 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 557 HLGKSNNFQKPRNikgKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTGDsgks 636
Cdd:smart00242 469 HHKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSK---- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 637 kggkkkgSSFQTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRIL 716
Cdd:smart00242 542 -------KRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLP 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124376530 717 YGDFRQRYRILNPVAIPEGQFiDSRKGTEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRD 780
Cdd:smart00242 615 FDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
100-768 |
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: 1003.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASIAAIGDRgkkdnANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTGKQ-----SSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFDV 339
Cdd:cd14934 157 AGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 340 LGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 419
Cdd:cd14934 237 LGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNME 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 420 QVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14934 317 QCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 500 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGK-QEAHF 578
Cdd:cd14934 397 EEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAHF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 579 SLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLkLMATLFSSYATADTGdsgksKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14934 477 ELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSL-GLLALLFKEEEAPAG-----SKKQKRGSSFMTVSNFYREQLN 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 659 KLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIPEGqFI 738
Cdd:cd14934 551 KLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FV 629
|
650 660 670
....*....|....*....|....*....|
gi 124376530 739 DSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14934 630 DNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-768 |
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: 1001.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAigdRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGA---SKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14909 158 LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14909 238 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14909 318 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIK-GKQEAH 577
Cdd:cd14909 398 QEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAAH 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 578 FSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTGDSGKSKGGKKKGSSFQTVSALHRENL 657
Cdd:cd14909 478 FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 658 NKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIPEGQf 737
Cdd:cd14909 558 NSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE- 636
|
650 660 670
....*....|....*....|....*....|.
gi 124376530 738 iDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14909 637 -DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
31-1086 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 851.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 31 FDIRTECFVPDDKEEFVKAKILSRE--GGKVIAE--TENGKTVTVKEDQVLQ--QNPPKFDKIEDMAMLTFLHEPAVLFN 104
Cdd:COG5022 6 AEVGSGCWIPDEEKGWIWAEIIKEAfnKGKVTEEgkKEDGESVSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPAVLHN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 105 LKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGK 184
Cdd:COG5022 86 LEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 185 TVNTKRVIQYFASIAAigdrgkkdNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADI 264
Cdd:COG5022 166 TENAKRIMQYLASVTS--------SSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 265 ETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNnPYDYAFVSQGEV-SVASIDDSEELMATDSAFDVLGFT 343
Cdd:COG5022 238 ETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQN-PKDYIYLSQGGCdKIDGIDDAKEFKITLDALKTIGID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 344 SEEKAGVYKLTGAIMHYGNMKFKqKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYY 423
Cdd:COG5022 317 EEEQDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 424 SIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYK 503
Cdd:COG5022 396 IRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 504 KEGIEWTFIDFgMDLQACIDLIEK--PMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGKQeahFSLI 581
Cdd:COG5022 476 KEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRLNKNSNPKFKKSRFRDNK---FVVK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 582 HYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTgdsgkskggkkkGSSFQTVSALHRENLNKLM 661
Cdd:COG5022 552 HYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIES------------KGRFPTLGSRFKESLNSLM 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 662 TNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIPEGQFI--- 738
Cdd:COG5022 620 STLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwke 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 739 DSRKGTEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRMQAQARGQLMRIEFKKIVERRDALLVIQW 818
Cdd:COG5022 700 DTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQH 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 819 NIRAFMGVKNWPWMKLYFKIKPLLKSAETEKEM---------------------ATMKEEFGR----IKETLEKSEARRK 873
Cdd:COG5022 780 GFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYrsylaciiklqktikrekklrETEEVEFSLkaevLIQKFGRSLKAKK 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 874 --ELEEKMVSLLQEKNDLQL---QVQAEQD-----------NLNDAEE--------RCDQLIKNKIQLE--AKVKEMNE- 926
Cdd:COG5022 860 rfSLLKKETIYLQSAQRVELaerQLQELKIdvksisslklvNLELESEiielkkslSSDLIENLEFKTEliARLKKLLNn 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 927 -RLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLakveKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAH 1005
Cdd:COG5022 940 iDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLL----KKSTILVREGNKANSELKNFKKELAELSKQYGALQEST 1015
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1006 QQ------ALDDLQVEEDKVNSLSKSKvKLEQQVDDLEGSLEQEKK------VRMDLERAKRKLEGDLKLTQESIMDLEN 1073
Cdd:COG5022 1016 KQlkelpvEVAELQSASKIISSESTEL-SILKPLQKLKGLLLLENNqlqaryKALKLRRENSLLDDKQLYQLESTENLLK 1094
|
1130
....*....|...
gi 124376530 1074 DKLQLEEKLKKKE 1086
Cdd:COG5022 1095 TINVKDLEVTNRN 1107
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-768 |
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: 843.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKR-SEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 178 GESGAGKTVNTKRVIQYFASIAAigdrGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSG----SGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDML----LVTNNPYDYAFVSQGEVSVASIDDSEELMAT 333
Cdd:cd00124 157 RLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELklelLLSYYYLNDYLNSSGCDRIDGVDDAEEFQEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 334 DSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREE--QAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEY 411
Cdd:cd00124 237 LDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGET 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 412 VTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATL--ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 489
Cdd:cd00124 317 ITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 490 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPR 568
Cdd:cd00124 397 FNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 569 nikgKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSlklmatlfssyatadtgdsgkskggkkkgssfqt 648
Cdd:cd00124 476 ----KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS---------------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 649 vsaLHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 728
Cdd:cd00124 518 ---QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILA 594
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 124376530 729 PvAIPEGQFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd00124 595 P-GATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-768 |
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: 801.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASIAAIGDRG------KKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF 253
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASKPKGsgavphPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 254 GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGEVSVASIDDSEELMAT 333
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 334 DSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 412
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNTV-AQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 413 TKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 491
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 492 HHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLgksnnfQKPRNIK 571
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 572 G--KQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLF---SSYATADTGDSGKSKGGKKKGSSF 646
Cdd:cd14911 474 TdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWkdaEIVGMAQQALTDTQFGARTRKGMF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 647 QTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 124376530 727 LNPVAIPEGqFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14911 634 LTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-768 |
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: 768.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASIAAiGDRGKKDnaNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVAS-SHKGRKD--HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPEL-LDMLLVTNNpyDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14920 159 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14920 237 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENTV-AQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQpRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14920 316 KEQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 496 VLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLyDNHLGKSNNFQKPRNIKG 572
Cdd:cd14920 395 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 573 kqEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFS-------SYATADTGDSGKSKGGKKKGSS 645
Cdd:cd14920 474 --KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdvdrivgLDQVTGMTETAFGSAYKTKKGM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 646 FQTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 725
Cdd:cd14920 552 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 124376530 726 ILNPVAIPEGqFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14920 632 ILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
100-768 |
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: 717.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASIAAiGDRGKKDNANA--NKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVAS-SFKTKKDQSSIalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPyDYAFVSQGEVSVASIDDSEELMATDSAF 337
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYS-KYRFLSNGNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 338 DVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDTA-AQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 417 SVQQVYYSIGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 496 VLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLYdNHLGKSNNFQKPRNIkg 572
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPKKL-- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 573 KQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSY-------ATADTGDsGKSKGGKKKGSS 645
Cdd:cd14932 476 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdrivgldKVAGMGE-SLHGAFKTRKGM 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 646 FQTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 725
Cdd:cd14932 555 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 634
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 124376530 726 ILNPVAIPEGqFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14932 635 ILTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
99-768 |
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: 697.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 178 GESGAGKTVNTKRVIQYFASIAAigdrgkkdnANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGG---------SSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAF 337
Cdd:cd01380 152 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 338 DVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd01380 232 TLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQP--RQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd01380 312 LQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 496 VLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNN-FQKPRNIKGKq 574
Cdd:cd01380 392 KLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFSNTA- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 575 eahFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMatlfssyatadtgdsgkskggkkkgssfqTVSALHR 654
Cdd:cd01380 470 ---FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRKK-----------------------------TVGSQFR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 655 ENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAipE 734
Cdd:cd01380 518 DSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK--E 595
|
650 660 670
....*....|....*....|....*....|....
gi 124376530 735 GQFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01380 596 WLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
100-768 |
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: 693.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASIAAiGDRGKKDNANAnkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVAS-SHKGKKDTSIT--GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELL-DMLLVTNNpyDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14921 159 VGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNTA-AQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14921 316 KEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 497 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRNIKGK 573
Cdd:cd14921 396 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 574 QEahFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSY-------ATADTGDSGKSKGGKKKGSSF 646
Cdd:cd14921 475 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldQMAKMTESSLPSASKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 647 QTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 124376530 727 LNPVAIPEGqFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14921 633 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-768 |
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: 681.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASIAAiGDRGKKDnananKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVAS-SHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtnNPYD-YAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14919 156 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14919 234 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNTA-AQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 497 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRNIKGK 573
Cdd:cd14919 393 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 574 qeAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSY-------ATADTGDSGKSKGGKKKGSSF 646
Cdd:cd14919 472 --ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldQVAGMSETALPGAFKTRKGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 647 QTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14919 550 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 124376530 727 LNPVAIPEGqFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14919 630 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
100-768 |
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: 678.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASIAAiGDRGKKDNAN--ANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVAS-SHKTKKDQNSlaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPyDYAFVSQGEVSVASIDDSEELMATDSAF 337
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYN-NYRFLSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 338 DVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASmPDNTA-AQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 417 SVQQVYYSIGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd15896 319 TQEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 496 VLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRNIkg 572
Cdd:cd15896 399 ILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPKKL-- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 573 KQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYAT-----ADTGDSGKSKGGKKKGSSFQ 647
Cdd:cd15896 476 KDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRivgldKVSGMSEMPGAFKTRKGMFR 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 648 TVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 727
Cdd:cd15896 556 TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 635
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 124376530 728 NPVAIPEGqFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd15896 636 TPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-768 |
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: 666.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASIAAiGDRGKKDNANAnkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVAS-SPKGRKEPGVP--GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYdYAFVSQGEVSVASiDDSEELMATDSAFDV 339
Cdd:cd14930 159 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 340 LGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14930 237 LGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNTA-AQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14930 316 EQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 497 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRNIkgK 573
Cdd:cd14930 395 LEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHL--R 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 574 QEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSY-------ATADTGDsgKSKGGKKKGSSF 646
Cdd:cd14930 472 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVegivgleQVSSLGD--GPPGGRPRRGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 647 QTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14930 550 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 124376530 727 LNPVAIPEGqFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14930 630 LTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-768 |
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: 641.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASIAAigdrgkkdNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSG--------GSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFDV 339
Cdd:cd01378 154 VGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 340 LGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEY---VTKGQ 416
Cdd:cd01378 234 IGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISDTSV-LDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 417 SVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQ-YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHhmF 495
Cdd:cd01378 313 NVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--L 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 496 VL--EQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFP-KATDMTFKAKLyDNHLGKSNNFQKPRNIK 571
Cdd:cd01378 391 TLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 572 GKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSsyATADTGDSGKSKggkkkgssfqTVSA 651
Cdd:cd01378 469 ELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFP--EGVDLDSKKRPP----------TAGT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 652 LHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVA 731
Cdd:cd01378 537 KFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKT 616
|
650 660 670
....*....|....*....|....*....|....*..
gi 124376530 732 IPEGQFIDsRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01378 617 WPAWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
100-768 |
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: 636.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASIAaigdrGKKDnanankgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd01381 82 SGAGKTESTKLILQYLAAIS-----GQHS-------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTnNPYDYAFVSQGE-VSVASIDDSEELMATDSAFD 338
Cdd:cd01381 150 EGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-DASDYYYLTQGNcLTCEGRDDAAEFADIRSAMK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQRE--EQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd01381 229 VLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 417 SVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYF---IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 493
Cdd:cd01381 309 SAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRH 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 494 MFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRNikg 572
Cdd:cd01381 389 IFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKPKS--- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 573 KQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSY--ATADTgdsgkskggkkkGSSFQTVS 650
Cdd:cd01381 464 DLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDisMGSET------------RKKSPTLS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 651 ALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPv 730
Cdd:cd01381 532 SQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP- 610
|
650 660 670
....*....|....*....|....*....|....*...
gi 124376530 731 AIPEGQFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01381 611 GIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
99-768 |
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: 632.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRgkKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAiGDRGkkdnanankgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd01383 79 ESGAGKTETAKIAMQYLAALGG-GSSG-----------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTnNPYDYAFVSQGE-VSVASIDDSEELMATDSAF 337
Cdd:cd01383 147 ICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLK-SASEYKYLNQSNcLTIDGVDDAKKFHELKEAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 338 DVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd01383 226 DTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLET-KQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd01383 306 LQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 497 LEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLyDNHLgKSNnfqkpRNIKGKQE 575
Cdd:cd01383 386 LEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHL-KSN-----SCFKGERG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 576 AHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLmATLFSSYATADTGDSGKSKGGKKKGSSFQTVSALHRE 655
Cdd:cd01383 458 GAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQL-PQLFASKMLDASRKALPLTKASGSDSQKQSVATKFKG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 656 NLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIPEG 735
Cdd:cd01383 537 QLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSAS 616
|
650 660 670
....*....|....*....|....*....|...
gi 124376530 736 QfiDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01383 617 Q--DPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-768 |
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: 615.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASiaaigdrgkkdnANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCA------------VTNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKK--PELLDMLLVtNNPYDYAFVSQ-GEVSVASIDDSEELMATDSA 336
Cdd:cd14883 150 KGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKL-GEPEDYHYLNQsGCIRIDNINDKKDFDHLRLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 337 FDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKG 415
Cdd:cd14883 229 MNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 416 QSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14883 309 LKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 496 VLEQEEYKKEGIEWTFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRNIKGKQ 574
Cdd:cd14883 389 KLEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPDRRRWKT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 575 EahFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFS----SYATADTGDSGKSKGGKKKGSSFQTVS 650
Cdd:cd14883 467 E--FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTypdlLALTGLSISLGGDTTSRGTSKGKPTVG 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 651 ALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPV 730
Cdd:cd14883 545 DTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPR 624
|
650 660 670
....*....|....*....|....*....|....*...
gi 124376530 731 AIPEGQFIDsRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14883 625 ARSADHKET-CGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-768 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 583.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 178 GESGAGKTVNTKRVIQYFAsiaaigDRGKKDNANANkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLA------YMGGRAVTEGR--SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGE-VSVASIDDSEELMATDSA 336
Cdd:cd01384 153 RISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKL-KDPKQFHYLNQSKcFELDGVDDAEEYRATRRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 337 FDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEP--DGTEDADK-SAYLMGLNSADLLKGLCHPRVKVGNEYVT 413
Cdd:cd01384 232 MDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPkdEKSEFHLKaAAELLMCDEKALEDALCKRVIVTPDGIIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 414 KGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 493
Cdd:cd01384 312 KPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 494 MFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLYDNhLGKSNNFQKPrniKG 572
Cdd:cd01384 392 VFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKP---KL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 573 KQEAhFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTGdsgkskggkkKGSSFQTVSAL 652
Cdd:cd01384 467 SRTD-FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGTS----------SSSKFSSIGSR 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 653 HRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPvAI 732
Cdd:cd01384 536 FKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAP-EV 614
|
650 660 670
....*....|....*....|....*....|....*.
gi 124376530 733 PEGQFiDSRKGTEKLLSSLDIdhNQYKFGHTKVFFK 768
Cdd:cd01384 615 LKGSD-DEKAACKKILEKAGL--KGYQIGKTKVFLR 647
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-768 |
1.11e-170 |
|
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: 534.74 E-value: 1.11e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAigdrgkkdnanaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAG------------STNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPElldMLLVTNNPYDYAFVSQGE-VSVASIDDSEELMATDSAF 337
Cdd:cd14872 149 ICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPA---SRGGWGSSAAYGYLSLSGcIEVEGVDDVADFEEVVLAM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 338 DVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKS---AYLMGLNSADLLKGLCHPRVKVgneyvtK 414
Cdd:cd14872 226 EQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLkevATLLGVDAATLEEALTSRLMEI------K 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 415 GQ-------SVQQVYYSIGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 486
Cdd:cd14872 300 GCdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 487 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSnnFQ 565
Cdd:cd14872 380 QQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS--TF 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 566 KPRNIKGKqEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYatadTGDSGKSKGgkkkgss 645
Cdd:cd14872 457 VYAEVRTS-RTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPS----EGDQKTSKV------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 646 fqTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 725
Cdd:cd14872 525 --TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYR 602
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 124376530 726 ILnPVAIPEGQFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14872 603 FL-VKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-768 |
2.36e-170 |
|
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: 534.74 E-value: 2.36e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 178 GESGAGKTVNTKRVIQYFASIAAigdrgkkdnaNANKGTLEdQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG----------GLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLlvtnnPYDYAFVSQGEVSVASID---DSEELMATD 334
Cdd:cd14903 150 TLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFL-----DSANECAYTGANKTIKIEgmsDRKHFARTK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 335 SAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE--PDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 412
Cdd:cd14903 225 EALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 413 TKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 492
Cdd:cd14903 305 TVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 493 HMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKg 572
Cdd:cd14903 385 DVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 573 kqeAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLF----SSYATADTGDSGKSKGGKKKGSSFQT 648
Cdd:cd14903 463 ---TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFkekvESPAAASTSLARGARRRRGGALTTTT 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 649 VSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 728
Cdd:cd14903 540 VGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFL 619
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 124376530 729 PVAipEGQFIDSRKGTEKLLSSLDIDH-NQYKFGHTKVFFK 768
Cdd:cd14903 620 PEG--RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
94-768 |
4.89e-169 |
|
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: 530.67 E-value: 4.89e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 94 TFLHepavlfNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQ 172
Cdd:cd01382 2 TLLN------NIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 173 SILITGESGAGKTVNTKRVIQYFAsiaaigdrgkkDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIH 252
Cdd:cd01382 76 SIIVSGESGAGKTESTKYILRYLT-----------ESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 253 FGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLvtnnpydyafvsqgevSVASIDDSEELMA 332
Cdd:cd01382 145 FNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 333 TDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKS----AYLMGLNSADLLKGLCHpRVKVG 408
Cdd:cd01382 209 MDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSEQSleyaAELLGLDQDELRVSLTT-RVMQT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 409 NEYVTKGQS------VQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQpRQYFIGVLDIAGFEIFDFNSFEQLCINFT 482
Cdd:cd01382 288 TRGGAKGTVikvplkVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYC 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 483 NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLYDNHLgks 561
Cdd:cd01382 367 NEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK--- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 562 NNF--QKPRniKGKQEAH--------FSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTG 631
Cdd:cd01382 443 NHFrlSIPR--KSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKD 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 632 dsgksKGGKKKGSSFQTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGF 711
Cdd:cd01382 521 -----SKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGF 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 124376530 712 PNRILYGDFRQRYRILNPvaiPEGQFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01382 596 PSRTSFHDLYNMYKKYLP---PKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
105-768 |
2.51e-168 |
|
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: 528.00 E-value: 2.51e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 105 LKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGK 184
Cdd:cd01379 7 LQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGESGAGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 185 TVNTKRVIQYFASIaaigdrGKkdnanANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADI 264
Cdd:cd01379 87 TESANLLVQQLTVL------GK-----ANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 265 ETYLLEKSRVIFQLKAERNYHIFYQIL----SNKKpeLLDMLLVTNNPYDYAFVSQGEVSVASIDDS--EELMATDSAFD 338
Cdd:cd01379 156 SEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKPPRYLQNDGLTVQDIVNNSGnrEKFEEIEQCFK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQ----AEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 414
Cdd:cd01379 234 VIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 415 GQSVQQVYYSIGALAKAVYEKMFNWMVTRINATL---ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 491
Cdd:cd01379 314 NNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpdRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 492 HHMFVLEQEEYKKEGIEWTFIDFGmDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHlgKSNNFQKPRni 570
Cdd:cd01379 394 QHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYWRPK-- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 571 kgKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMAtlfssyatadtgdsgkskggkkkgssfQTVS 650
Cdd:cd01379 469 --SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR---------------------------QTVA 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 651 ALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL--- 727
Cdd:cd01379 520 TYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLafk 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 124376530 728 ---NPVAipegqfidSRKGTEKLLSSLDIDHnqYKFGHTKVFFK 768
Cdd:cd01379 600 wneEVVA--------NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
100-768 |
4.09e-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: 525.88 E-value: 4.09e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYML----TDRENQSI 174
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIqsgvLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 175 LITGESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANK-------GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGK 247
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASeaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 248 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNnPYDYAFVSQGEVSVASIDDS 327
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 328 EELMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGT-EDADKSAYLMGLNSADLLKGLCHPRVK 406
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 407 VGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 486
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 487 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILE--EEC--MFPKATDMTFKAKLYDNHLGKS 561
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgKVNGKPGIFItlDDCwrFKGEEANKKFVSQLHASFGRKS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 562 NNFQKPRN-------IKGKQEA--HFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATlfssyatadtgd 632
Cdd:cd14890 480 GSGGTRRGssqhphfVHPKFDAdkQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIREV------------ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 633 sgkskggkkkgssfqTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFP 712
Cdd:cd14890 548 ---------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFA 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 124376530 713 NRILYGDFRQRYRILNPVAipegqfiDSRKGTEKLLSS-LDIDHNQYKFGHTKVFFK 768
Cdd:cd14890 613 LREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKmLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
100-768 |
1.38e-166 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 524.32 E-value: 1.38e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASIAaigdrgKKDNAnankgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGKL 259
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVN------QRRNN-----LVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKkPELLDMLLVTNNPYDYAFVSQG-EVSVASIDDSEELMATDSAFD 338
Cdd:cd01387 150 VGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGL-PAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQRE---EQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKG 415
Cdd:cd01387 229 VLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 416 QSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd01387 309 LTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 496 VLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRniKGKQ 574
Cdd:cd01387 389 KLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR--MPLP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 575 EahFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYA--TADTGDSGKSKGGKKKGSSFQTVSAL 652
Cdd:cd01387 465 E--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRaqTDKAPPRLGKGRFVTMKPRTPTVAAR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 653 HRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAI 732
Cdd:cd01387 543 FQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKL 622
|
650 660 670
....*....|....*....|....*....|....*...
gi 124376530 733 PEGQFIDSRkgtEKLLSSLD--IDHNQYKFGHTKVFFK 768
Cdd:cd01387 623 PRPAPGDMC---VSLLSRLCtvTPKDMYRLGATKVFLR 657
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1925 |
1.11e-164 |
|
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: 533.60 E-value: 1.11e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 848 EKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNER 927
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 928 LEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQ 1007
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1008 ALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEF 1087
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1088 DINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNK 1167
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1168 KREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANL 1247
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1248 EKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKA 1327
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1328 KNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDAEEAVE 1407
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1408 AVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLK 1487
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1488 NAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEF 1567
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1568 NQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKS 1647
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1648 LQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLIN 1727
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1728 QKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAL 1807
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1808 KGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEA 1887
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 124376530 1888 EEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1925
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-768 |
3.93e-164 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 518.09 E-value: 3.93e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRgKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 178 GESGAGKTVNTKRVIQYFASiAAIGDRGKKDnanankgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF---- 253
Cdd:cd14888 80 GESGAGKTESTKYVMKFLAC-AGSEDIKKRS-------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklk 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 254 -----GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILS-----------------------NKKPELLDMLL-V 304
Cdd:cd14888 152 skrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSfE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 305 TNNPYDYAFVSqGEVSVASIDDSEELMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQA---EPDGTED 381
Cdd:cd14888 232 PHLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 382 ADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGV 460
Cdd:cd14888 311 LEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 461 LDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLI-EKPMGIMSILEEEC 539
Cdd:cd14888 391 LDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEEC 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 540 MFPKATDMTFKAKLYDNHLGkSNNFQKprnIKGKQEAhFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMA 619
Cdd:cd14888 470 FVPGGKDQGLCNKLCQKHKG-HKRFDV---VKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFIS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 620 TLFSSYATADTGdsgkskgGKKKGSSFQTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNG 699
Cdd:cd14888 545 NLFSAYLRRGTD-------GNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGG 617
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124376530 700 VLEGIRICRKGFPNRILYGDFRQRYRILNPvaiPEGQfidsrkgtekllssldIDHNQYKFGHTKVFFK 768
Cdd:cd14888 618 VLQAVQVSRAGYPVRLSHAEFYNDYRILLN---GEGK----------------KQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-766 |
9.41e-164 |
|
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: 516.65 E-value: 9.41e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY------RGKKRSEAPPHIFSISDNAYQYMLTDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 171 --NQSILITGESGAGKTVNTKRVIQYFASIAAigdRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS---ATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 249 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNP-YDYAFVSQGEVSVASIDDS 327
Cdd:cd14901 158 IRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEeYKYLNSSQCYDRRDGVDDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 328 EELMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTE-DADKSAYLMGLNSADLLKGLCHPRVK 406
Cdd:cd14901 238 VQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLaNVRAACDLLGLDMDVLEKTLCTREIR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 407 VGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQP--RQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 484
Cdd:cd14901 318 AGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFANE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 485 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLYDNhLGKSNN 563
Cdd:cd14901 398 KLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHAS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 564 FQKPRNIKGKQEahFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATlfssyatadtgdsgkskggkkkg 643
Cdd:cd14901 476 FSVSKLQQGKRQ--FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 644 ssfqTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 723
Cdd:cd14901 531 ----TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHT 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 124376530 724 YRILNP------VAIPEGQFIDSRKGTEKLLSSLDIDHNQykFGHTKVF 766
Cdd:cd14901 607 YSCLAPdgasdtWKVNELAERLMSQLQHSELNIEHLPPFQ--VGKTKVF 653
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
105-768 |
8.61e-160 |
|
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: 505.83 E-value: 8.61e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 105 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRG--KKRSEAPPHIFSISDNAYQYMLTDR----ENQSILIT 177
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTPQSIVVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 178 GESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANKGT-LEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 256
Cdd:cd14892 87 GESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHEsIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 257 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpELLDMLLVTNNPYDYAFVSQGE-VSVASIDDSEELMATDS 335
Cdd:cd14892 167 GRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGNcVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 336 AFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQ--KQREEQAEPDGTEDADKSAYLMGLNSADLLKGLC-----HPRVKVG 408
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVtqttsTARGSVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 409 NEYVTKGQSVQqvyySIGALAKAVYEKMFNWMVTRINAtlETKQ------------PRQYFIGVLDIAGFEIFDFNSFEQ 476
Cdd:cd14892 326 EIKLTAREAKN----ALDALCKYLYGELFDWLISRINA--CHKQqtsgvtggaaspTFSPFIGILDIFGFEIMPTNSFEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 477 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEK-PMGIMSILEEECMFP-KATDMTFKAKLY 554
Cdd:cd14892 400 LCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTIYH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 555 DNHLGKSNNFQKPRNikgkQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSlklmatlfssyatadtgdsg 634
Cdd:cd14892 479 QTHLDKHPHYAKPRF----ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS-------------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 635 kskggkkkgsSFqtvsalhRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNR 714
Cdd:cd14892 535 ----------KF-------RTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIR 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 124376530 715 ILYGDFRQRYRIL-NPVAIPEGQFIDSRKGTEKLL----SSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14892 598 RQFEEFYEKFWPLaRNKAGVAASPDACDATTARKKceeiVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
102-768 |
1.14e-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: 503.83 E-value: 1.14e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 102 LFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESG 181
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 182 AGKTVNTKRVIQYFASIAAIGdrgkkdnanANKGTlEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 261
Cdd:cd01385 84 SGKTESTNFLLHHLTALSQKG---------YGSGV-EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 262 ADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTnNPYDYAFVSQGE-VSVASIDDSEELMATDSAFDVL 340
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLK-QPEDYHYLNQSDcYTLEGEDEKYEFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 341 GFTSEEKAGVYKLTGAIMHYGNMKFKQK--QREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQ----PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 494
Cdd:cd01385 313 PEAIATRDAMAKCLYSALFDWIVLRINHALLNKKdleeAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 495 FVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKlYDNHLGKSNNFQKPRnikgK 573
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ----V 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 574 QEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLM------------------ATLFSSYATADTGDSGK 635
Cdd:cd01385 467 MEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVreligidpvavfrwavlrAFFRAMAAFREAGRRRA 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 636 SKGGKKKGSSFQ----------------TVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNG 699
Cdd:cd01385 547 QRTAGHSLTLHDrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTG 626
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124376530 700 VLEGIRICRKGFPNRILYGDFRQRYRILnpvaIPEGQfIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01385 627 MLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
100-768 |
7.68e-154 |
|
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: 489.31 E-value: 7.68e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQSLELSLKEKTSC---VEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTnNPYDYAFVSQ-GEVSVASIDDSEELMATDSAF 337
Cdd:cd14873 159 IQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLNQsGCVEDKTISDQESFREVITAM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 338 DVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDadkSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14873 238 EVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALGR---SAELLGLDPTQLTDALTQRSMFLRGEEILTPLN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQyFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14873 315 VQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 498 EQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHlgkSNN--FQKPRnikgKQE 575
Cdd:cd14873 394 EQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH---ANNhfYVKPR----VAV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 576 AHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTGDSGKSKGGKKKgssfQTVSALHRE 655
Cdd:cd14873 466 NNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRR----PTVSSQFKD 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 656 NLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP-VAIPE 734
Cdd:cd14873 542 SLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRnLALPE 621
|
650 660 670
....*....|....*....|....*....|....
gi 124376530 735 gqfiDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14873 622 ----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
101-768 |
1.84e-147 |
|
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: 471.10 E-value: 1.84e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKK-RSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASIAAigdrgkKDNANankgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKLSP------SDDSD-----LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGEVSVASIDDSEELMATDSAFDV 339
Cdd:cd14897 152 LGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELEYYRQMFHD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 340 L-------GFTSEEKAGVYKLTGAIMHYGNMKFkqkqrEEQAEPDGTEDADK-----SAYLMGLNSADLLKGLCHPRVKV 407
Cdd:cd14897 231 LtnimkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 408 GNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYF-----IGVLDIAGFEIFDFNSFEQLCINFT 482
Cdd:cd14897 306 RGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 483 NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLyDNHLGKS 561
Cdd:cd14897 386 NERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCGES 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 562 NNFQKPrniKGKQEAhFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYatadtgdsgkskggkk 641
Cdd:cd14897 464 PRYVAS---PGNRVA-FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY---------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 642 kgssfqtvsalHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 721
Cdd:cd14897 524 -----------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFV 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 124376530 722 QRYRILNPVAIPEGQFIDSRkgTEKLLSSLDIDhnQYKFGHTKVFFK 768
Cdd:cd14897 593 KRYKEICDFSNKVRSDDLGK--CQKILKTAGIK--GYQFGKTKVFLK 635
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-768 |
3.43e-145 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 465.57 E-value: 3.43e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 178 GESGAGKTVNTKRVIQYFASIAAigdrGKKDNAnankgtlEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG----GRKDKT-------IAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSN-KKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSA 336
Cdd:cd14904 150 KLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 337 FDVLGFTSEEKAGVYKLTGAIMHYGNMKFkQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd14904 230 LSLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 417 SVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQY-FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14904 309 APVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 496 VLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNH--LGKSNNFQKPRNikgk 573
Cdd:cd14904 389 KTVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKV---- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 574 QEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLF-SSYATADTGDSGKSKGGKKKgssfQTVSAL 652
Cdd:cd14904 464 KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFgSSEAPSETKEGKSGKGTKAP----KSLGSQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 653 HRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPvai 732
Cdd:cd14904 540 FKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFP--- 616
|
650 660 670
....*....|....*....|....*....|....*..
gi 124376530 733 PEGQFIDSRKGTEKLLSSLDIDHN-QYKFGHTKVFFK 768
Cdd:cd14904 617 PSMHSKDVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
101-727 |
2.34e-143 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 459.39 E-value: 2.34e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAY-----------RGKKRSEAPPHIFSISDNAYQYM--- 165
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 166 -LTDRENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRGKKdNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSR 244
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASV-SMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 245 FGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILsnkkpelldmllvtnnpydyafVSQGEVSVASi 324
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMA----------------------IGASEAARKR- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 325 DDSEELMAtdsAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDA-------DKSAYLMGLNSADLL 397
Cdd:cd14900 219 DMYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 398 KGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATL-----ETKQPRQYFIGVLDIAGFEIFDFN 472
Cdd:cd14900 296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPKN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 473 SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKA 551
Cdd:cd14900 376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLAS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 552 KLYdNHLGKSNNFQKPRNIKGKqeAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKsslklmatlfssyatadtg 631
Cdd:cd14900 455 KLY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVY------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 632 dsgkskggkkkgssfqtvSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGF 711
Cdd:cd14900 513 ------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGF 574
|
650
....*....|....*.
gi 124376530 712 PNRILYGDFRQRYRIL 727
Cdd:cd14900 575 PIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
101-768 |
4.36e-139 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 449.10 E-value: 4.36e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGK--------KRSEAPPHIFSISDNAYQYMLTDREN 171
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 172 QSILITGESGAGKTVNTKRVIQYFASIAA--------IGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSS 243
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevLTLTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 244 RFGKFIRIHFG-ATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNP--YDYAFVSQGE-V 319
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLsgDRYDYLKKSNcY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 320 SVASIDDSEELMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQ--REEQAEPDGTEDADKSAYLMGLNSADLL 397
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 398 KGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATL--------ETKQPRQYFIGVLDIAGFEIF 469
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 470 DFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF--IDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATD 546
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 547 MTFKAKLYDNHlgksNNFQKPRNIKGKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSsya 626
Cdd:cd14907 482 EKLLNKIKKQH----KNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFS--- 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 627 TADTGDSGKSKGGKKKGSSFQTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRI 706
Cdd:cd14907 555 GEDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRV 634
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124376530 707 CRKGFPNRILYGDFRQRYRILNpvaipegqfidsrkgtekllssldidhNQYKFGHTKVFFK 768
Cdd:cd14907 635 RKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
105-768 |
1.73e-136 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 441.65 E-value: 1.73e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 105 LKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYML----TDRENQSILITGES 180
Cdd:cd14889 7 LKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVISGES 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 181 GAGKTVNTKRVIQYFASIAaigdRGKKDnanankgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGKLA 260
Cdd:cd14889 87 GAGKTESTKLLLRQIMELC----RGNSQ--------LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 261 SADIETYLLEKSRVIFQLKAERNYHIFYQI---LSNKKPELLDMLLVTNNPY-DYAFVSQGEVSVASIDDSEELmatdSA 336
Cdd:cd14889 154 GAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLLDPGKYRYlNNGAGCKREVQYWKKKYDEVC----NA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 337 FDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREE-QAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKG 415
Cdd:cd14889 230 MDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 416 QSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQY---FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 492
Cdd:cd14889 310 HTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVelrEIGILDIFGFENFAVNRFEQACINLANEQLQYFFNH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 493 HMFVLEQEEYKKEGIEWTFIDFgMDLQACIDL-IEKPMGIMSILEEECMFPKATDMTFKAKLyDNHLGKSNNFQKPRNik 571
Cdd:cd14889 390 HIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGKSRS-- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 572 gkQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTGDSGKSKGGKKKGSSF----- 646
Cdd:cd14889 466 --KSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSDNFnstrk 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 647 QTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14889 544 QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKI 623
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 124376530 727 LnpvaIPEGQFIDSRKGTEKLLSSLDIdhNQYKFGHTKVFFK 768
Cdd:cd14889 624 L----LCEPALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-734 |
1.84e-135 |
|
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: 439.73 E-value: 1.84e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYR--GKKRS---EAP----PHIFSISDNAYQYMLTD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 169 RENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 249 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQIL------SNKKPELLDMLLVTNN-PYDYAFVSQGEV-S 320
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDGITGGLQlPNEFHYTGQGGApD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 321 VASIDDSEELMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAY---LMGLNSADLL 397
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 398 KGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATL--ETKQPRQYFIGVLDIAGFEIFDFNSFE 475
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 476 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFP-KATDMTFKAKL 553
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 554 YDNHLGKSNN-------FQKPRNIKGKqeAHFSLIHYAGTVDYNI-LGWLEKNKDPLNETVVALYQKSslklmaTLFssy 625
Cdd:cd14908 480 YETYLPEKNQthsentrFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESG------QQF--- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 626 atadtgdsgkskggkkkgssfqtvsalhRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIR 705
Cdd:cd14908 549 ----------------------------KAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVR 600
|
650 660
....*....|....*....|....*....
gi 124376530 706 ICRKGFPNRILYGDFRQRYRILNPVaIPE 734
Cdd:cd14908 601 VARSGYPVRLPHKDFFKRYRMLLPL-IPE 628
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-729 |
3.41e-134 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 437.40 E-value: 3.41e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYR--------GKKRSEAPPHIFSISDNAYQYML-TD 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 169 RENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVE--IGKRILQTNPILESFGNAQTIRNDNSSRFGKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 249 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDmLLVTNNPYDYAFVSQGEVSVA-----S 323
Cdd:cd14902 159 IKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD-LLGLQKGGKYELLNSYGPSFArkravA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 324 IDDSEELMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDA---DKSAYLMGLNSADLLKGL 400
Cdd:cd14902 238 DKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 401 CHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRIN-------ATLETKQPRQYF--IGVLDIAGFEIFDF 471
Cdd:cd14902 318 SSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSdeinyfdSAVSISDEDEELatIGILDIFGFESLNR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 472 NSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLqACIDLIE-KPMGIMSILEEECMFPKATDMTFK 550
Cdd:cd14902 398 NGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNA-ACLALFDdKSNGLFSLLDQECLMPKGSNQALS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 551 AKLYDNHLGksnnfqkprnikgkqEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSS----YA 626
Cdd:cd14902 477 TKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADenrdSP 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 627 TADTGDSGKSKGGKKKGSsfqTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRI 706
Cdd:cd14902 542 GADNGAAGRRRYSMLRAP---SVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRI 618
|
650 660
....*....|....*....|...
gi 124376530 707 CRKGFPNRILYGDFRQRYRILNP 729
Cdd:cd14902 619 ARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-768 |
3.99e-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: 3.99e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAA--WMIYTYSGLFCVTVNPYKWLPvyNAEVvAAYRGKKRSEAPPHIFSISDNAYQYMLTDRE---NQS 173
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 174 ILITGESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANKG-------TLEDQIIQANPALEAFGNAKTVRNDNSSRFG 246
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKkrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 247 KFIRIHFGATG-KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTnNPYDYAFVSQ-GEVSVASI 324
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLL-SPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 325 DDSEELMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREE----QAEPDGTEDADKSAYLMGLNSADLLKGL 400
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 401 CHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFD-FNSFEQLCI 479
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 480 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLYDNHl 558
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 559 GKSNNFQKPRNiKGKQEAhFSLIHYAGTVDYNILGWLEKNKDPLNEtvvalyQKSSLKLMATLFSsyatadtgdsgkskg 638
Cdd:cd14891 475 KRHPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPE------DFEDLLASSAKFS--------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 639 gkkkgssfqtvsalhrENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 718
Cdd:cd14891 532 ----------------DQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYA 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 124376530 719 DFRqryRILNPVAIPEGQFIDS---RKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14891 596 ELV---DVYKPVLPPSVTRLFAendRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-768 |
1.57e-126 |
|
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: 413.02 E-value: 1.57e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIaaigdrgKKDNANANKGTLEDQIiqanPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGK 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL-------YQDQTEDRLRQPEDVL----PILESFGHAKTILNANASRFGQVLRLHL-QHGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGEV-SVASIDDSEELMATDSAF 337
Cdd:cd14896 149 IVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 338 DVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDAD--KSAYLMGLnSADLLKGLCHPRVKVGN-EYVTK 414
Cdd:cd14896 228 QGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQV-PPERLEGAVTHRVTETPyGRVSR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 415 GQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYF--IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 492
Cdd:cd14896 307 PLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 493 HMFVLEQEEYKKEGIEWTFIDfGMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRNik 571
Cdd:cd14896 387 TLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL-- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 572 gkQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSyATADTGDSGKSKggkkkgssfqTVSA 651
Cdd:cd14896 463 --PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE-AEPQYGLGQGKP----------TLAS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 652 LHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVA 731
Cdd:cd14896 530 RFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSER 609
|
650 660 670
....*....|....*....|....*....|....*...
gi 124376530 732 IPEgqfIDSRKGTEKLLSS-LDIDHNQYKFGHTKVFFK 768
Cdd:cd14896 610 QEA---LSDRERCGAILSQvLGAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
62-821 |
5.54e-125 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 414.81 E-value: 5.54e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 62 ETENGKTVTVKEDQVLQQNPP-KFDKIEDMAMLTFLHEPAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVA 140
Cdd:PTZ00014 72 DPPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 141 AYR-GKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASiaaigdrGKKDNanaNKGTLED 219
Cdd:PTZ00014 152 RYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS-------SKSGN---MDLKIQN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 220 QIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELL 299
Cdd:PTZ00014 222 AIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 300 DMLLVTNNPyDYAFVSQGEVSVASIDDSEELMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKqrEEQAEPDGT 379
Cdd:PTZ00014 302 EKYKLKSLE-EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGK--EEGGLTDAA 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 380 EDADKS-------AYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQ 452
Cdd:PTZ00014 379 AISDESlevfneaCELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPG 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 453 PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGI-----EWTfidfgmDLQACIDLI-E 526
Cdd:PTZ00014 459 GFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGIsteelEYT------SNESVIDLLcG 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 527 KPMGIMSILEEECMFPKATDMTFKAKLYDNHlgKSNNFQKPRniKGKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETV 606
Cdd:PTZ00014 533 KGKSVLSILEDQCLAPGGTDEKFVSSCNTNL--KNNPKYKPA--KVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPEL 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 607 VALYQKSSLKLMATLFSsyatadtGDSGKSKGGKKKgssfQTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVM 686
Cdd:PTZ00014 609 VEVVKASPNPLVRDLFE-------GVEVEKGKLAKG----QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDW 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 687 DNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNpVAIPEGQFIDSRKGTEKLLSSLDIDHNQYKFGHTKVF 766
Cdd:PTZ00014 678 NSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVF 756
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124376530 767 FKAGLLGLLEEMRDERLS------RIITRMqaqargqLMRIEFKKIVERRDALLV-IQWNIR 821
Cdd:PTZ00014 757 LKKDAAKELTQIQREKLAaweplvSVLEAL-------ILKIKKKRKVRKNIKSLVrIQAHLR 811
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
99-768 |
5.46e-121 |
|
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: 399.33 E-value: 5.46e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNaevVAAYRGK--KRSEAPPHIFSISDNAYQYMLT-------D 168
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 169 RENQSILITGESGAGKTVNTKRVIQYFASIAAigDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 248
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSK--HTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 249 IRIHFG-----ATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDML-LVTNNPYDYAFVSQGEVSVA 322
Cdd:cd14895 156 VRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELqLELLSAQEFQYISGGQCYQR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 323 S--IDDSEELMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDA------------------ 382
Cdd:cd14895 236 NdgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqhl 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 383 DKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQY------ 456
Cdd:cd14895 316 DIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaan 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 457 -----FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMG 530
Cdd:cd14895 396 kdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPSG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 531 IMSILEEECMFPKATDMTFKAKLYdNHLGKSNNFQKPRniKGKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALY 610
Cdd:cd14895 475 IFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 611 QKSSLKLMATLFSSYATADTGDSGKSKGGKKKGSSFQT---VSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMD 687
Cdd:cd14895 552 GKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSsvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFD 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 688 NPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILnpVAIPEGQFIDSrkgtEKLLSSLDIDHNQykFGHTKVFF 767
Cdd:cd14895 632 MAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLL--VAAKNASDATA----SALIETLKVDHAE--LGKTRVFL 703
|
.
gi 124376530 768 K 768
Cdd:cd14895 704 R 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-768 |
7.02e-120 |
|
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: 394.35 E-value: 7.02e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRG-KKRSEAPPHIFSIS----DNAYQYmltdRENQS 173
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTArralENLHGV----NKSQT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 174 ILITGESGAGKTVNTKRVIQYFASiaaigdrGKKDNANankGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF 253
Cdd:cd14876 77 IIVSGESGAGKTEATKQIMRYFAS-------AKSGNMD---LRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 254 GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLD--MLLVTNnpyDYAFVSQGEVSVASIDDSEELM 331
Cdd:cd14876 147 ASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSkyHLLGLK---EYKFLNPKCLDVPGIDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 332 ATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQReeqaepDGTEDA-----------DKSAYLMGLNSADLLKGL 400
Cdd:cd14876 224 EVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTE------QGVDDAaaisneslevfKEACSLLFLDPEALKREL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 401 CHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCIN 480
Cdd:cd14876 298 TVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFIN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 481 FTNEKLQQFFNHHMFVLEQEEYKKEGI-----EWTfidfgmDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLY 554
Cdd:cd14876 378 ITNEMLQKNFIDIVFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 555 DNHlgKSNNFQKPrnIKGKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATaDTGDSG 634
Cdd:cd14876 452 SKL--KSNGKFKP--AKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVV-EKGKIA 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 635 KSkggkkkgssfQTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNR 714
Cdd:cd14876 527 KG----------SLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYR 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 124376530 715 ILYGDFRQRYRILNPvAIPEGQFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14876 597 RPFEEFLYQFKFLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
101-729 |
3.79e-110 |
|
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: 366.87 E-value: 3.79e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEA-PPHIFSISDNAYQYMLTDRE--NQSILI 176
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 177 TGESGAGKTVNTKRVIQYFASIAAiGDRGKKDNANANKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 256
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAA-SPTSWESHKIAER--IEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 257 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILsnkKPELLDMLLVTNNP--YDYAFVSQGEVSVasidDSEELMATD 334
Cdd:cd14880 160 QQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQIC---KGASADERLQWHLPegAAFSWLPNPERNL----EEDCFEVTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 335 SAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQA---EPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEY 411
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 412 VT--KGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPR-QYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQ 488
Cdd:cd14880 313 QVfkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 489 FFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDmtfkAKLYDNHLGK--SNNFQ 565
Cdd:cd14880 393 HFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSS----AAQLQTRIESalAGNPC 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 566 KPRNiKGKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSsyatADTGDSGKSKGGKKKGSS 645
Cdd:cd14880 468 LGHN-KLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFP----ANPEEKTQEEPSGQSRAP 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 646 FQTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 725
Cdd:cd14880 543 VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
....
gi 124376530 726 ILNP 729
Cdd:cd14880 623 LLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
101-728 |
6.06e-108 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 362.37 E-value: 6.06e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKR-SEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAiGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT-G 257
Cdd:cd14906 83 ESGSGKTEASKTILQYLINTSS-SNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 258 KLASADIETYLLEKSRVIFQL-KAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASI------------ 324
Cdd:cd14906 162 KIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsnhn 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 325 ---DDSEELMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQ---REEQAEPDGTEDADKSAYLMGLNSADLLK 398
Cdd:cd14906 242 nktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 399 GLCHPRVKVGNE--YVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINAT-LETKQPRQ----------YFIGVLDIAG 465
Cdd:cd14906 322 ALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKfNQNTQSNDlaggsnkknnLFIGVLDIFG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 466 FEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKA 544
Cdd:cd14906 402 FENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 545 TDMTFKAKlYDNHLGKSNNFQKPRNIKGKqeahFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSS 624
Cdd:cd14906 481 SEQSLLEK-YNKQYHNTNQYYQRTLAKGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQ 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 625 YATADTGDSGKSKGGKkkgssfqTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGI 704
Cdd:cd14906 556 QITSTTNTTKKQTQSN-------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTI 628
|
650 660
....*....|....*....|....
gi 124376530 705 RICRKGFPNRILYGDFRQRYRILN 728
Cdd:cd14906 629 KVRKMGYSYRRDFNQFFSRYKCIV 652
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
100-725 |
1.05e-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: 361.72 E-value: 1.05e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYR-------GKKRSEA---PPHIFSISDNAYQYMLTD 168
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 169 RENQSILITGESGAGKTVNTKRVIQYFA------SIAAIGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNS 242
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAvhcgtgNNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 243 SRFGKFIRIHF-GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNK----KPELLDMLLVTNNPYDYAFVSQG 317
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 318 EVSVA--SIDDSEELMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQ--KQREEQAEPDGTEDA----------D 383
Cdd:cd14899 242 LCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 384 KSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQY------- 456
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 457 --------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlQACIDLIE-K 527
Cdd:cd14899 402 ddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 528 PMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVV 607
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 608 ALYQKSSLKLMATLFSSYATAD-TGDSGKSKGGKKKGSSFQT------VSALHRENLNKLMTNLRTTHPHFVRCIIPNER 680
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDaNGDSELDGFGGRTRRRAKSaiaavsVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 124376530 681 KAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 725
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
101-768 |
8.48e-105 |
|
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: 352.38 E-value: 8.48e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 181 GAGKTVNTKRVIQYFASIA-AIGDRGKKDNANAnkgtledqiiqANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAgSVGGVLSVEKLNA-----------ALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFvsqGEVSVASIDD----SEELMATDS 335
Cdd:cd01386 152 ASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF---GIVPLQKPEDkqkaAAAFSKLQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 336 AFDVLGFTSEEKAGVYKLTGAIMHYGN---MKFKQKQREEQAEPdgtEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 412
Cdd:cd01386 229 AMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 413 T---------------KGQSVQQvyySIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN----- 472
Cdd:cd01386 306 TtssgqesparsssggPKLTGVE---ALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrg 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 473 -SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEK---------------PMGIMSILE 536
Cdd:cd01386 383 aTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 537 EECMFPKATDMTFKAKLYdNHLGKSNNFQKPRNI-KGKQEAHFSLIHYAGT--VDYNILGWLEKNK-DPLNETVVALYQK 612
Cdd:cd01386 463 EEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLrRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQE 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 613 SSLKLMATLFSSYATAdtgdsgkskggkkkgSSFQtvsalhrenLNKLMTNLRTTHPHFVRCIIPN------ERKAPGV- 685
Cdd:cd01386 542 SQKETAAVKRKSPCLQ---------------IKFQ---------VDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPa 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 686 -----MDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPV----AIPEGQFIDSRKGTEKLLSSLDIDHN 756
Cdd:cd01386 598 agdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkkLGLNSEVADERKAVEELLEELDLEKS 677
|
730
....*....|..
gi 124376530 757 QYKFGHTKVFFK 768
Cdd:cd01386 678 SYRIGLSQVFFR 689
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
105-768 |
1.44e-104 |
|
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: 350.34 E-value: 1.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 105 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRS-----EAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASIAAIGDRgkkdnanankgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSST-----------DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYdYAFVSQGEVSVA-SIDDSEELMATDSAF 337
Cdd:cd14886 156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASKCYDApGIDDQKEFAPVRSQL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 338 DVLgFTSEEKAGVYKLTGAIMHYGNMKFKQKQR---EEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 414
Cdd:cd14886 235 EKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIIS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 415 GQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 494
Cdd:cd14886 314 PVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 495 FVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKP-MGIMSILEEECMFPKATDMTFKAKLyDNHLgKSNNFQKPrniKGK 573
Cdd:cd14886 394 FKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSFIPG---KGS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 574 QeAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSyATADTGDSGKskggkkkgssfQTVSALH 653
Cdd:cd14886 468 Q-CNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSD-IPNEDGNMKG-----------KFLGSTF 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 654 RENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIP 733
Cdd:cd14886 535 QLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSS 614
|
650 660 670
....*....|....*....|....*....|....*...
gi 124376530 734 ---EGQfiDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14886 615 sqnAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
101-732 |
5.41e-104 |
|
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: 349.11 E-value: 5.41e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 101 VLFNLKERYAAWMI-YTYSGLFCVTVNPYKWLPvYNAEVvaaYRGKKRSEA-----PPHIFSISDNAY-QYMLTDRENQS 173
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMP-FNSEE---ERKKYLALPdprllPPHIWQVAHKAFnAIFVQGLGNQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 174 ILITGESGAGKTVNTKRVIQYfasiaaIGDRGKKDNANANKGTLEDQIIQ----ANPALEAFGNAKTVRNDNSSRFGKFI 249
Cdd:cd14875 79 VVISGESGSGKTENAKMLIAY------LGQLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 250 RIHF-GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDY-------AFVSQGeVSV 321
Cdd:cd14875 153 KLYFdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYkclnggnTFVRRG-VDG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 322 ASIDDSEELMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDAdKSAYLMGLNSADLLKGLC 401
Cdd:cd14875 232 KTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 402 hprVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLetkQPRQ-----YFIGVLDIAGFEIFDFNSFEQ 476
Cdd:cd14875 311 ---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASI---TPQGdcsgcKYIGLLDIFGFENFTRNSFEQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 477 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLYD 555
Cdd:cd14875 385 LCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 556 NHLGKSNNFQKPRNIKGKQeahFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADtgdsgk 635
Cdd:cd14875 464 QWANKSPYFVLPKSTIPNQ---FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLA------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 636 skggkkkgSSFQTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRI 715
Cdd:cd14875 535 --------RRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRR 606
|
650
....*....|....*...
gi 124376530 716 LYGDF-RQRYRILNPVAI 732
Cdd:cd14875 607 PIEQFcRYFYLIMPRSTA 624
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-743 |
5.82e-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: 5.82e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKwlPVYNAEVVAAYRgKKRSEAPPHIFSISDNAYQYMLTdRENQSILITGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASiaaigdrgkkdnANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgaTGKL 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE------------RTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpelldmLLVTNNPYDYAFVSQGEVSVasIDDSEELMATDSAFDV 339
Cdd:cd14898 144 TGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSAMKS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 340 LGFTSEEKagVYKLTGAIMHYGNMKFKQkqrEEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 419
Cdd:cd14898 216 LGIANFKS--IEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 420 QVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQyfIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14898 291 QARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 500 EEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKAT--DMTFKAKLYDNHlgksnnfqkprNIKGKQEAH 577
Cdd:cd14898 369 GMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNG-----------FINTKARDK 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 578 FSLIHYAGTVDYNILGWLEKNKdplnetvvalyQKSSLKLmatlFSSYATADTGDSgkskggkkkgssfQTVSALHRENL 657
Cdd:cd14898 437 IKVSHYAGDVEYDLRDFLDKNR-----------EKGQLLI----FKNLLINDEGSK-------------EDLVKYFKDSM 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 658 NKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPVAIpegQF 737
Cdd:cd14898 489 NKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLF---EV 565
|
....*.
gi 124376530 738 IDSRKG 743
Cdd:cd14898 566 VDYRKG 571
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
100-736 |
8.09e-94 |
|
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: 319.45 E-value: 8.09e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYR---GKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 176
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 177 TGESGAGKTVNTKRVIQYFASiaaigdrgkkdNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 256
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTC-----------RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 257 GK-LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGE----VSVASIDDSEELM 331
Cdd:cd14878 151 KKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHL-NNLCAHRYLNQTMredvSTAERSLNREKLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 332 ATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEY 411
Cdd:cd14878 230 VLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 412 VTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQ 487
Cdd:cd14878 310 IIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 488 QFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLyDNHLGKSNNFQK 566
Cdd:cd14878 390 HYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPSGFLSLLDEESQMIWSVEPNLPKKL-QSLLESSNTNAV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 567 PRNIKG--------KQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATadtgdsgkskg 638
Cdd:cd14878 469 YSPMKDgngnvalkDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLV----------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 639 gkkkgssfqTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 718
Cdd:cd14878 538 ---------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFS 608
|
650
....*....|....*...
gi 124376530 719 DFRQRYRILNPVAIPEGQ 736
Cdd:cd14878 609 DFLSRYKPLADTLLGEKK 626
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-768 |
1.62e-89 |
|
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: 308.89 E-value: 1.62e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAA--------WMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 171 NQSILITGESGAGKTVNTKRVIQYfasIAAIGDRGKkdnaNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIR 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTY---LAAVSDRRH----GADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 251 IHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKK-PELLDMLLVTNNPYDYafvsqgevsvasiddseE 329
Cdd:cd14887 154 LHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVaAATQKSSAGEGDPEST-----------------D 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 330 LMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEP-----------DGTEDADKSAYLMGLNS----- 393
Cdd:cd14887 217 LRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKrkltsvsvgceETAADRSHSSEVKCLSSglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 394 -------ADLLKGLCHPRVKVGNEYV------------TKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPR 454
Cdd:cd14887 297 easrkhlKTVARLLGLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 455 QY--------------FIGVLDIAGFEIF---DFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEG--IEWTFIDFG 515
Cdd:cd14887 377 SEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCSAFP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 516 MDLQACIDLIEKP------------------------MGIMSILEEE-CMFPKATDMTFKAKLYDNHLGKS-NNFQKPRN 569
Cdd:cd14887 457 FSFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKNiINSAKYKN 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 570 IK---GKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYqksslklmatLFSSYATADTGDSGKSKGGKKKGSSf 646
Cdd:cd14887 537 ITpalSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF----------LACSTYTRLVGSKKNSGVRAISSRR- 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 647 QTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14887 606 STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYET 685
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 124376530 727 LNPVAIPEgqFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14887 686 KLPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
105-767 |
3.56e-86 |
|
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: 296.77 E-value: 3.56e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 105 LKERYAAWMIYTY---SGLfcVTVNPYKWLPVYNAEVVAAYR-------GKKRSEAPPHIFSISDNAYQYMLTDRENQSI 174
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 175 LITGESGAGKTVNTKRVIQYFASIAAIGDRGKKdnanankgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 254
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSSHSKKGTK---------LSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 255 ATGKLASADIETYLLEKSRVIfQLKA-ERNYHIFYQILSNKKPELLDmLLVTNNPYDYAFV----SQGEVSVASIDDSE- 328
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQ-HLGLDDPSDYALLasygCHPLPLGPGSDDAEg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 329 --ELMAtdsAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQkqreeqaEPDGTEDA---------DKSAYLMGLNSADLL 397
Cdd:cd14879 237 fqELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTY-------DHEGGEESavvkntdvlDIVAAFLGVSPEDLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 398 KGLCHPRVKVGNEYVT-----KGQSVQQvyysiGALAKAVYEKMFNWMVTRINATL-ETKQPRQYFIGVLDIAGFEIFD- 470
Cdd:cd14879 307 TSLTYKTKLVRKELCTvfldpEGAAAQR-----DELARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSs 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 471 --FNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEEC-MFPKATD 546
Cdd:cd14879 382 tgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 547 MTFKAKLyDNHLGKSNNFQKPRNIKGKQEAH-FSLIHYAGTVDYNILGWLEKNKDPLNETVValyqksslklmaTLFSSY 625
Cdd:cd14879 461 EQMLEAL-RKRFGNHSSFIAVGNFATRSGSAsFTVNHYAGEVTYSVEGFLERNGDVLSPDFV------------NLLRGA 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 626 ATadtgdsgkskggkkkgssfqtvsalHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIR 705
Cdd:cd14879 528 TQ-------------------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAA 582
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124376530 706 ICRKGFPNRILYGDFRQRYrilnpvaIPEGQFIDSRKGTEKLLSSLDIDHNQYKFGHTKVFF 767
Cdd:cd14879 583 RLRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
101-768 |
1.10e-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: 295.00 E-value: 1.10e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEvvaaYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 181 GAGKTVNTKRVIQYFASIAaigdrgKKDNANANkgTLEDqiiqANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 260
Cdd:cd14937 79 GSGKTEASKLVIKYYLSGV------KEDNEISN--TLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 261 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPyDYAFVSQGEVSVASIDDSEELMATDSAFDVL 340
Cdd:cd14937 147 SSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDKM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 341 GFTSEEKAGVYKLTGAIMhYGNMKFKQ-----KQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKG 415
Cdd:cd14937 226 NMHDMKDDLFLTLSGLLL-LGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 416 QSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14937 305 LSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 496 VLEQEEYKKEGIEWTFIDFGMDlQACIDLIEKPMGIMSILEEECMFPKATDMTFkAKLYDNHLGKSNNFQkprNIKGKQE 575
Cdd:cd14937 385 EKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYA---STKKDIN 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 576 AHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATADTGDSGkskggkkkgssfQTVSALHRE 655
Cdd:cd14937 460 KNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK------------NLITFKYLK 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 656 NLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRIcRKGFPNRILYGDFRQRYRILNPVAIPEG 735
Cdd:cd14937 528 NLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDS 606
|
650 660 670
....*....|....*....|....*....|...
gi 124376530 736 QFIDSRKGTEKLLSSLDIDhnQYKFGHTKVFFK 768
Cdd:cd14937 607 SLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-716 |
1.93e-73 |
|
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: 260.61 E-value: 1.93e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEA-------PPHIFSISDNAYQYMLTDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 171 NQSILITGESGAGKTVNTKRVIQYFASIaaigdrgkkdNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIR 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----------QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 251 IHF---------GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGE--- 318
Cdd:cd14884 151 LIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEshq 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 319 ---------VSVASIDDSEELMATDSA-FDVL-------GFTSEEKAGVYKLTGAIMHYGNMKFKQkqreeqaepdgted 381
Cdd:cd14884 231 krsvkgtlrLGSDSLDPSEEEKAKDEKnFVALlhglhyiKYDERQINEFFDIIAGILHLGNRAYKA-------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 382 adkSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINAT----------LETK 451
Cdd:cd14884 297 ---AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNvlkckekdesDNED 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 452 QPR--QYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF--GMDLQACIDLIEK 527
Cdd:cd14884 374 IYSinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVApsYSDTLIFIAKIFR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 528 PMGIMSILEEECMfpKATDMTFKAKLYDNH----------LGKSNNF-----QKPRNIKgkqEAHFSLIHYAGTVDYNIL 592
Cdd:cd14884 454 RLDDITKLKNQGQ--KKTDDHFFRYLLNNErqqqlegkvsYGFVLNHdadgtAKKQNIK---KNIFFIRHYAGLVTYRIN 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 593 GWLEKNKDPLNETVVALYQKSSlklMATLFSSYATADTGDsgkskggkkkgssFQTVSALHRENLNKLMTNLRTTHPHFV 672
Cdd:cd14884 529 NWIDKNSDKIETSIETLISCSS---NRFLREANNGGNKGN-------------FLSVSKKYIKELDNLFTQLQSTDMYYI 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 124376530 673 RCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRIL 716
Cdd:cd14884 593 RCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-748 |
3.21e-71 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 252.34 E-value: 3.21e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPvyNAEVVAAYRGKKRSeapPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 180 SGAGKTVNTKRVIQYFASIAaigdrGKKDNANANKgtledQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGKL 259
Cdd:cd14881 77 SGSGKTYASMLLLRQLFDVA-----GGGPETDAFK-----HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDGAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDML-LVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14881 146 YRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLhLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKACLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLG--FTSeekagVYKLTGAIMHYGNMKFKQKQrEEQAEPDGTEDADKSAYLMGLNSADLLKGL---CHprvkvgneyVT 413
Cdd:cd14881 226 ILGipFLD-----VVRVLAAVLLLGNVQFIDGG-GLEVDVKGETELKSVAALLGVSGAALFRGLttrTH---------NA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 414 KGQ---SVQQVYYSIG---ALAKAVYEKMFNWMVTRIN------ATLETKQpRQYFIGVLDIAGFEIFDFNSFEQLCINF 481
Cdd:cd14881 291 RGQlvkSVCDANMSNMtrdALAKALYCRTVATIVRRANslkrlgSTLGTHA-TDGFIGILDMFGFEDPKPSQLEHLCINL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 482 TNEKLQQFFNHHMFVLEQEEYKKEGIewtfidfGMDLQA-------CIDLIEK-PMGIMSILEEECMfPKATDMTFKAKL 553
Cdd:cd14881 370 CAETMQHFYNTHIFKSSIESCRDEGI-------QCEVEVdyvdnvpCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 554 YDNHlgKSNN-FQKPRNIKGKQeahFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLmatlfsSYATaDTGD 632
Cdd:cd14881 442 KVQH--RQNPrLFEAKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF------GFAT-HTQD 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 633 sgkskggkkkgssFQTvsalhreNLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFP 712
Cdd:cd14881 510 -------------FHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYP 569
|
650 660 670
....*....|....*....|....*....|....*.
gi 124376530 713 NRILYGDFRQRYRILNPVAiPEGQFIDSRKGTEKLL 748
Cdd:cd14881 570 HRMRFKAFNARYRLLAPFR-LLRRVEEKALEDCALI 604
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
100-768 |
3.17e-69 |
|
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: 246.32 E-value: 3.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 100 AVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYrgkkrseappHIFSISDNAYQYMLTDREN-QSILITG 178
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 179 ESGAGKTVNTKRVIQYFASiaaigdrgkkdNANANKGTLEDQIIQAnpALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14874 72 ESGSGKSYNAFQVFKYLTS-----------QPKSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLYKRNVL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNpYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14874 139 TGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL-QKFFYINQGNSTENIQSDVNHFKHLEDALH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 339 VLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQR---EEQAEPDGTEDADK-SAYLMGLNSADLLKGLChPRVKVGNEYvtk 414
Cdd:cd14874 218 VLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKwVAFLLEVDFDQLVNFLL-PKSEDGTTI--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 415 gqSVQQVYYSIGALAKAVYEKMFNWMVTRINatLETKQPRQY-FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 493
Cdd:cd14874 294 --DLNAALDNRDSFAMLIYEELFKWVLNRIG--LHLKCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKH 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 494 MFVLEQEEYKKEGIEwtfIDFGMdlQACID-------LIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNnFQK 566
Cdd:cd14874 370 SFHDQLVDYAKDGIS---VDYKV--PNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 567 PRNikgKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYaTADTGDSgkskggkkkgssF 646
Cdd:cd14874 444 ARN---KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY-SSNTSDM------------I 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 647 QTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14874 508 VSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRC 587
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 124376530 727 LNPVAIPEGQfiDSRKGTEKLLSSLDIDH-NQYKFGHTKVFFK 768
Cdd:cd14874 588 LLPGDIAMCQ--NEKEIIQDILQGQGVKYeNDFKIGTEYVFLR 628
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
105-720 |
7.82e-68 |
|
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: 243.46 E-value: 7.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 105 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYrgKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAG 183
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 184 KTVNTKRVIQYFASIAAigDRGKkdnanankgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASAD 263
Cdd:cd14905 85 KSENTKIIIQYLLTTDL--SRSK---------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 264 IETYLLEKSRVIFQLKAERNYHIFYQILSN-KKPELLDMLLVTNNPYDYaFVSQGEVSVASIDDSEELMATDSAFDVLGF 342
Cdd:cd14905 154 LYSYFLDENRVTYQNKGERNFHIFYQFLKGiTDEEKAAYQLGDINSYHY-LNQGGSISVESIDDNRVFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 343 TSEEKAGVYKLTGAIMHYGNMKFKQKQREeqaepdgTEDADKSaylmglnsadLLKGLCH----PRVKVGNEYVT-KGQS 417
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRT----------LIESLSHnitfDSTKLENILISdRSMP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLetkQPRQY--FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14905 296 VNEAVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 496 VLEQEEYKKEGIEW-TFIDFgMDLQACIDLIEKpmgIMSILEEECMFPKATDMTFKAKLydnhlgksNNFQKPRNIKGKQ 574
Cdd:cd14905 373 KQEQREYQTERIPWmTPISF-KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 575 EAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMAT---LFSSYATADTGDSGKSKGGKKKGSSFQTVSA 651
Cdd:cd14905 441 PNKFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSrdgVFNINATVAELNQMFDAKNTAKKSPLSIVKV 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 652 L------HRENLNKLMTN-------------------LRTTHP-------------HFVRCIIPNERKAPGVMDNPLVMH 693
Cdd:cd14905 521 LlscgsnNPNNVNNPNNNsgggggggnsgggsgsggsTYTTYSstnkainnsncdfHFIRCIKPNSKKTHLTFDVKSVNE 600
|
650 660 670
....*....|....*....|....*....|.
gi 124376530 694 QLRCNGVLEGIRICRKGFP----NRILYGDF 720
Cdd:cd14905 601 QIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-767 |
3.19e-63 |
|
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: 231.40 E-value: 3.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 102 LFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKR----------SEAPPHIFSISDNAYQYMLTDREN 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 172 QSILITGESGAGKTVNTKRVIQYFASIA-AIGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIR 250
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGdETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 251 IHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKK--PELLDMLLVTNNPYDYAFVSQG--EVSVASID- 325
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFALDa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 326 -DSEELMatdSAFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLN-------SADLL 397
Cdd:cd14893 244 rDYRDLM---SSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQSCALKdpaqillAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 398 KglCHPRV------------KVGNEYVT--KGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPR--------- 454
Cdd:cd14893 321 E--VEPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksnivin 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 455 QYFIGVLDIAGFEIFD--FNSFEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEG--IEWTFIDFGMDLQACIDLI 525
Cdd:cd14893 399 SQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 526 E-KPMGIMSILEEECMFPKATDMTFKAKLYDNH-----LGKSNNFQKPRNIKGKQEAHFSLI----HYAGTVDYNILGWL 595
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNeavggLSRPNMGADTTNEYLAPSKDWRLLfivqHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 596 EKNKDPLNETVVALYQKSSLKLMATLFSSYATADTGDS--GKSKGGKKKGSSFQTVSALHRENLN--------------K 659
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKaaKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 660 LMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRilnpvaipegqFID 739
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK-----------NVC 707
|
730 740 750
....*....|....*....|....*....|...
gi 124376530 740 SRKGT-EKLLSSLD----IDHNQYKFGHTKVFF 767
Cdd:cd14893 708 GHRGTlESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-251 |
2.72e-60 |
|
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: 204.50 E-value: 2.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 121 FCVTVNPYKWLPVYNAEVV-AAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASIA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 124376530 200 AIGDRGKKDNANAN----KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 251
Cdd:cd01363 81 FNGINKGETEGWVYlteiTVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
101-768 |
5.89e-60 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 219.61 E-value: 5.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 101 VLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 181 GAGKTVNTKRVIQYfasIAAIGDrgkkdnanANKGTLEdQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 260
Cdd:cd14882 83 YSGKTTNARLLIKH---LCYLGD--------GNRGATG-RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 261 SADIETYLLEKSRVIFQLKAERNYHIFYQILS--NKKPELLDMLLVTNNPYDYAFVSQG-------------EVSVASID 325
Cdd:cd14882 151 GAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERYK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 326 DSEELmatdsaFDVLGFTSEEKAGVYKLTGAIMHYGNMKFKQKQREeqAEPDGTEDADKSAYLMGLNSADLLKGLCHPRV 405
Cdd:cd14882 231 EFEEI------LKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 406 KVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETkqPR-----QYFIGVLDIAGFEIFDFNSFEQLCIN 480
Cdd:cd14882 303 IKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 481 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEecmfpKATDMTFKAKLYDNHLGK 560
Cdd:cd14882 381 TLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 561 SNNFQKPRNikgkqeAH-FSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLFSSYATadtgdsgkskgg 639
Cdd:cd14882 456 HSQFVKKHS------AHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQV------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 640 kkkgSSFQTVSALHR----ENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRI 715
Cdd:cd14882 518 ----RNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRI 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 124376530 716 LYGDFRQRYRILnpvAIPEGQFIDSRKGTEKLLsSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14882 594 PFQEFLRRYQFL---AFDFDETVEMTKDNCRLL-LIRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-766 |
1.62e-48 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 186.58 E-value: 1.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 99 PAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSE-APPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 178 GESGAGKTVNTKRVIQYFA------------SIAAIGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRF 245
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAyqvkgsrrlptnLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 246 GKFIRIHFgATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYdYAFVSQGEVSVASID 325
Cdd:cd14938 161 SKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIEN-YSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 326 DSEELMATDSAFDVLGFTSEEKAGVYKLTGAIMHYGN-------------MKFKQKQRE----------EQAEPDGTEDA 382
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 383 DKSAYL----MGLNSADLLKGLCHPRVkVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYF- 457
Cdd:cd14938 319 VKNLLLacklLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININt 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 458 --IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM--GIMS 533
Cdd:cd14938 398 nyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 534 ILEEECMfPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGKQEAhFSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKS 613
Cdd:cd14938 478 LLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 614 SLKLMATLFSSYATADTGDSGKSKGGKKKGSSF-----------QTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKA 682
Cdd:cd14938 556 ENEYMRQFCMFYNYDNSGNIVEEKRRYSIQSALklfkrrydtknQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKR 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 683 P-GVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPvaipegqfiDSRKGTEKLLSSLDIDHNQYKFG 761
Cdd:cd14938 636 ElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMIG 706
|
....*
gi 124376530 762 HTKVF 766
Cdd:cd14938 707 NNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1175-1929 |
1.00e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 129.41 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1175 KMRRdlEEATLQHEATAAALrKKHADSVAELGEQIDNLQRVKQKLEKEKsefklELddvtsnmeqiikaKANLEKVSRTL 1254
Cdd:TIGR02168 171 KERR--KETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERYK-----EL-------------KAELRELELAL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1255 edqaneYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHA 1334
Cdd:TIGR02168 230 ------LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1335 LQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKK------LAQRLQDAEEAVEA 1408
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaeleeLESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1409 VNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEwkqkyeesqselessqKEARSLSTELFKLKN 1488
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE----------------AELKELQAELEELEE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1489 AYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFN 1568
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1569 QIKAEIERKLAekdeeMEQAKRNH--QRVVDSLQTSLDA-ETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAE----- 1640
Cdd:TIGR02168 528 LISVDEGYEAA-----IEAALGGRlqAVVVENLNAAKKAiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIegflg 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1641 --------AQKQVKSLQSLLKDTQI--QLDDAVRANDDLKENIAIV------------------ERRNNLL--QAELEEL 1690
Cdd:TIGR02168 603 vakdlvkfDPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRIVtldgdlvrpggvitggsaKTNSSILerRREIEEL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1691 RAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEE 1770
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1771 LKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIK 1850
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKE--------ELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124376530 1851 ELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1929
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
842-1610 |
1.55e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 119.01 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 842 LKSAETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKV 921
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 922 KEMNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKAL 1001
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1002 QEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLEraKRKLEGDLKLTQESIMDLEndklQLEEK 1081
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQAELEELE----EELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1082 LKKKEFDINQQNSKIEDEQVLALQ----LQKKLKENQARIEELEEELEAERT---ARAKVEKLRSDLSRELEEISER--- 1151
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQaldaAERELAQLQARLDSLERLQENLEGfseGVKALLKNQSGLSGILGVLSELisv 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1152 -------LEEAGGATSVQIEMNKKREAefqkmrRDLEEATLQHEATAAAL----RKKHADSVAELGEQIDNLQRVKQ--- 1217
Cdd:TIGR02168 532 degyeaaIEAALGGRLQAVVVENLNAA------KKAIAFLKQNELGRVTFlpldSIKGTEIQGNDREILKNIEGFLGvak 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1218 KLEKEKSEFKLEL----------DDVTSNMEQIIKAKANLEKVSRTLE------------DQAN----EYRVKLEEAQRS 1271
Cdd:TIGR02168 606 DLVKFDPKLRKALsyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDlvrpggvitggsAKTNssilERRREIEELEEK 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1272 LNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEE 1351
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1352 ETEAKAELQRVLSKANSEVAQWRTKYETDAIQRT------EELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQN 1425
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrealDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1426 EIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTEL-------FKLKNAYEESLEHLE 1498
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELreleskrSELRRELEELREKLA 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1499 TFKRENKNLQEEISDLTEQLGEGGKNVHELekvrkqLEVEKLELQSALEEAEASLEHEEGKI-------LRAQLEFNQIK 1571
Cdd:TIGR02168 926 QLELRLEGLEVRIDNLQERLSEEYSLTLEE------AEALENKIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELK 999
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 124376530 1572 aeiERK--LAEKDEEMEQAKRNHQRVVDslqtSLDAETRSR 1610
Cdd:TIGR02168 1000 ---ERYdfLTAQKEDLTEAKETLEEAIE----EIDREARER 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
835-1454 |
1.96e-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: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 835 YFKIKPLLKSAETE---KEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLI 911
Cdd:COG1196 215 YRELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 912 KNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEII 991
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 992 AKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDL 1071
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1072 ENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAK---------VEKLRSDLS 1142
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLaglrglagaVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1143 RELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKE 1222
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1223 KSEFKLELDDVTSnmeqiikAKANLEKVSRTLEDQANEYRVKLEEAQRSLndftTQRAKLQTENGELARQLEEKEALISQ 1302
Cdd:COG1196 615 YYVLGDTLLGRTL-------VAARLEAALRRAVTLAGRLREVTLEGEGGS----AGGSLTGGSRRELLAALLEAEAELEE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1303 LTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAqwrtKYETDAI 1382
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPEP 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1383 QRTEELEEAKKKLAQRLQD-------AEEAVEAVNAKCSSLEKTKHRLQNEIEDLM-----VDVERSNAAAAALDKKQRN 1450
Cdd:COG1196 760 PDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEeaieeIDRETRERFLETFDAVNEN 839
|
....
gi 124376530 1451 FDKI 1454
Cdd:COG1196 840 FQEL 843
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
912-1745 |
3.27e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 117.85 E-value: 3.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 912 KNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECS------ELKKDIDDLELTLAKVEKEKHAtenkvknltEEMA 985
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEkaerykELKAELRELELALLVLRLEELR---------EELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 986 GLDEIIAKLTKEKKALQEAhqqalddLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRK-------LE 1058
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAE-------LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIlrerlanLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1059 GDLKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLR 1138
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1139 SDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATL-QHEATAAALRKKHADSVAELGEQIDNLQRVKQ 1217
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELeELEEELEELQEELERLEEALEELREELEEAEQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1218 KLEKEKSEF------KLELDDVTSNMEQIIKAKANLEKVSRTLEDQ----------ANEYRVKLEEA-QRSLNDFTTQRA 1280
Cdd:TIGR02168 476 ALDAAERELaqlqarLDSLERLQENLEGFSEGVKALLKNQSGLSGIlgvlselisvDEGYEAAIEAAlGGRLQAVVVENL 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1281 KLQTENGELARQLEEKEALISQLTRGKLSYTQ--QMEDLKRQLEEEGKAKN-------------------ALAHALQSAR 1339
Cdd:TIGR02168 556 NAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQgnDREILKNIEGFLGVAKDlvkfdpklrkalsyllggvLVVDDLDNAL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1340 HDCDLLREQYEEETeakaeLQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAkcssLEKT 1419
Cdd:TIGR02168 636 ELAKKLRPGYRIVT-----LDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAE----LRKE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1420 KHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLET 1499
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1500 -------FKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKA 1572
Cdd:TIGR02168 787 leaqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1573 EIErKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQS-L 1651
Cdd:TIGR02168 867 LIE-ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErL 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1652 LKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEqtersrkLAEQELIETSERVQLLHSQNTSLINQKKK 1731
Cdd:TIGR02168 946 SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNL-------AAIEEYEELKERYDFLTAQKEDLTEAKET 1018
|
890
....*....|....
gi 124376530 1732 MESDLTQLQSEVEE 1745
Cdd:TIGR02168 1019 LEEAIEEIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1261-1933 |
6.84e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 117.08 E-value: 6.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1261 YRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQltrgklsyTQQMEDLKRQLEEegKAKNALAHALQSARH 1340
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEK--------AERYKELKAELRE--LELALLVLRLEELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1341 DCDLLREQYEEETEAKAELQRVLSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTK 1420
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKL---------------EELRLEVSELEEEIEELQKELYALANEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1421 HRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETF 1500
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1501 KRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLE--------FNQIKA 1572
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelqeelerLEEALE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1573 EIERKLAEKDEEMEQAKRNHQR------VVDSLQTSLDAETRSRNEVLRVKKKMEGDLN--------------EMEIQL- 1631
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILGvlselisvdegyeaAIEAALg 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1632 ----------SHANRMAAEAQKQVKS------LQSLLKDTQIQLDDAVRAN----------------------------- 1666
Cdd:TIGR02168 545 grlqavvvenLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDREILKniegflgvakdlvkfdpklrkalsyllgg 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1667 ----DDLKENIAI----------------------------VERRNNLL--QAELEELRAVVEQTERSRKLAEQELIETS 1712
Cdd:TIGR02168 625 vlvvDDLDNALELakklrpgyrivtldgdlvrpggvitggsAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELR 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1713 ERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTI 1792
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1793 KDLQHRLDEAeQIALKGGKKQLQKLEARVRELEGE-------LEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLR 1865
Cdd:TIGR02168 785 EELEAQIEQL-KEELKALREALDELRAELTLLNEEaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124376530 1866 LQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKQ 1933
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
978-1853 |
5.69e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.00 E-value: 5.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 978 KNLTEEMAGldeiIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVddlegslEQEKKVRmDLERAKRKL 1057
Cdd:TIGR02168 158 RAIFEEAAG----ISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQA-------EKAERYK-ELKAELREL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1058 EGDLkltqesimdLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKL 1137
Cdd:TIGR02168 226 ELAL---------LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1138 RSDLSRELEEISERLEEAGG---ATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQR 1214
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERqleELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1215 VKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEyrVKLEEAQRSLNDFTTQRAKLQTENGELARQLE 1294
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE--IEELLKKLEEAELKELQAELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1295 EKEALISQLTRGKLSYTQQMEDLkRQLEEEGKAKNALAHALQSarhdcdlLREQYEEETEAKAELQRVLSKANSEVAQWR 1374
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLER-------LQENLEGFSEGVKALLKNQSGLSGILGVLS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1375 TKYETDaiqrtEELEEAKKK-LAQRLQ-----DAEEAVEAVNA-------KCSSLEKTKHR---LQNEIEDLMVDVERSN 1438
Cdd:TIGR02168 527 ELISVD-----EGYEAAIEAaLGGRLQavvveNLNAAKKAIAFlkqnelgRVTFLPLDSIKgteIQGNDREILKNIEGFL 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1439 AAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNL-----QEEISD 1513
Cdd:TIGR02168 602 GVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSsilerRREIEE 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1514 LTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEheegkilraqlefnqikaEIERKLAEKDEEMEQAKRNHQ 1593
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE------------------ELSRQISALRKDLARLEAEVE 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1594 RVvdslqtsldAETRSRNEVLRVKKKMEgdLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDavranddLKENI 1673
Cdd:TIGR02168 744 QL---------EERIAQLSKELTELEAE--IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-------LREAL 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1674 AIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSErvqllhsqntslinQKKKMESDLTQLQSEVEEAVQECRNA 1753
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE--------------QIEELSEDIESLAAEIEELEELIEEL 871
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1754 EEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELEGELEAEQK 1833
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE-KLAQLELRLEGLEVRIDNLQERLSEEYS 950
|
890 900
....*....|....*....|....*...
gi 124376530 1834 RNAESVKGM--------RKSERRIKELT 1853
Cdd:TIGR02168 951 LTLEEAEALenkieddeEEARRRLKRLE 978
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1108-1911 |
1.00e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 109.77 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1108 KKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEaggatsVQIEMNKKReaEFQKMRRDLEEAtlqh 1187
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLER------LRREREKAE--RYQALLKEKREY---- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1188 EATAAALRKKHADsvaelgEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANL-EKVSRTLEDQANEYRVKLE 1266
Cdd:TIGR02169 224 EGYELLKEKEALE------RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1267 EaqrslndFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLR 1346
Cdd:TIGR02169 298 E-------LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1347 EQYEEETEAKAELQRvlskansEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNE 1426
Cdd:TIGR02169 371 AELEEVDKEFAETRD-------ELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1427 IEDLMVDVErsnaaaaALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTElfklknayeesLEHLETFKRENKN 1506
Cdd:TIGR02169 443 KEDKALEIK-------KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE-----------LAEAEAQARASEE 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1507 LQEEISDLTEQLGEGGKNVHELekVRKQLEVEKlELQSALEEA-----------------EASLEHEEGKILRAQ-LEFN 1568
Cdd:TIGR02169 505 RVRGGRAVEEVLKASIQGVHGT--VAQLGSVGE-RYATAIEVAagnrlnnvvveddavakEAIELLKRRKAGRATfLPLN 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1569 QIKAE--------------IERKLAEKDEEMEQAKRNHQR---VVDSLQT-----------SLDAE-----------TRS 1609
Cdd:TIGR02169 582 KMRDErrdlsilsedgvigFAVDLVEFDPKYEPAFKYVFGdtlVVEDIEAarrlmgkyrmvTLEGElfeksgamtggSRA 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1610 RNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEE 1689
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1690 LRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLtqLQSEVEEAVQECRNAEEKAKKAITDAAMMAE 1769
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1770 ELKKEQDTSAHLERMKKNMEQTIKDLQHRLDE-AEQIALKGGKK-----QLQKLEARVRELEGELEAEQKRNAESVKGMR 1843
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiEKEIENLNGKKeeleeELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124376530 1844 KSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSkFRKVQHELDEAEER 1911
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
989-1851 |
2.81e-23 |
|
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: 108.28 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 989 EIIAKLTKE--KKALQEAHQQaLDDLQVEEDKVNSL-SKSKVKLEQQVDDLEGSLEQ---EKKVRMDLERAKRKLEGDLK 1062
Cdd:pfam15921 66 KIIAYPGKEhiERVLEEYSHQ-VKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1063 ltqesiMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAE------------RTA 1130
Cdd:pfam15921 145 ------NQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1131 RAKVEKLRSDLSRELEEISERLEEAGGA-TSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQI 1209
Cdd:pfam15921 219 GSAISKILRELDTEISYLKGRIFPVEDQlEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1210 DNLQRVKQKLEKEKSEFKLELDDVTSNMEQIikaKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGEL 1289
Cdd:pfam15921 299 SQLEIIQEQARNQNSMYMRQLSDLESTVSQL---RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1290 ARQLE---------EKEALISQLTRGKL-----SYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEA 1355
Cdd:pfam15921 376 DDQLQklladlhkrEKELSLEKEQNKRLwdrdtGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1356 KAElqrVLSKANSEVAQWRTKYE---------TDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNE 1426
Cdd:pfam15921 456 KNE---SLEKVSSLTAQLESTKEmlrkvveelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1427 IEDLMVD---VERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFK-- 1501
Cdd:pfam15921 533 LQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKil 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1502 RENKNLQeeisdlteqlgeggknVHELEKVRKQLEVEKLELQSALEE---AEASLEHEEGKILR----AQLEFNQIKAEI 1574
Cdd:pfam15921 613 KDKKDAK----------------IRELEARVSDLELEKVKLVNAGSErlrAVKDIKQERDQLLNevktSRNELNSLSEDY 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1575 E---RKLAEKDEEMEQAKRNHQRVVDSLQTSLDaetRSRNEVlrvkKKMEG-DLNEMEIQLSHANRMAAEaQKQVKSLQS 1650
Cdd:pfam15921 677 EvlkRNFRNKSEEMETTTNKLKMQLKSAQSELE---QTRNTL----KSMEGsDGHAMKVAMGMQKQITAK-RGQIDALQS 748
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1651 LLKDTQIQLDDAVRANDDLKE-------NIAIVERRNNLLQAELEELRAvvEQTERSRKLAEQELIETSERVQLLHSQNt 1723
Cdd:pfam15921 749 KIQFLEEAMTNANKEKHFLKEeknklsqELSTVATEKNKMAGELEVLRS--QERRLKEKVANMEVALDKASLQFAECQD- 825
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1724 slINQKKKMESDLTQLQS--EVEEAVQECRNAEEKAKKAITDAAMMAE---ELKKEQDTSAHL-----------ERMKKN 1787
Cdd:pfam15921 826 --IIQRQEQESVRLKLQHtlDVKELQGPGYTSNSSMKPRLLQPASFTRthsNVPSSQSTASFLshhsrktnalkEDPTRD 903
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124376530 1788 MEQTIKDLQHRLDEAEQIAL-----KGGKKQLQKLEARVRELEGELE-----AEQKRNAESVKGMRKSERRIKE 1851
Cdd:pfam15921 904 LKQLLQELRSVINEEPTVQLskaedKGRAPSLGALDDRVRDCIIESSlrsdiCHSSSNSLQTEGSKSSETCSRE 977
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
842-1591 |
4.13e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 107.85 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 842 LKSAETEKEMAtmkEEFGRIKEtlEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKV 921
Cdd:TIGR02169 200 LERLRREREKA---ERYQALLK--EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 922 KEMNERLEDE-EEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 1000
Cdd:TIGR02169 275 EELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1001 LQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLegdlkltQESIMDLENDKLQLEE 1080
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL-------QEELQRLSEELADLNA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1081 KLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERL----EEAG 1156
Cdd:TIGR02169 428 AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseERVR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1157 GATSVQIEMNKKREAEFQKMRrDLEEATLQHEA---TAAALRKKHA----DSVAElgEQIDNLQRVKQ------KLEKEK 1223
Cdd:TIGR02169 508 GGRAVEEVLKASIQGVHGTVA-QLGSVGERYATaieVAAGNRLNNVvvedDAVAK--EAIELLKRRKAgratflPLNKMR 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1224 SEFKL-----------------ELDD--------------VTSNME----QIIK----------------------AKAN 1246
Cdd:TIGR02169 585 DERRDlsilsedgvigfavdlvEFDPkyepafkyvfgdtlVVEDIEaarrLMGKyrmvtlegelfeksgamtggsrAPRG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1247 LEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGK 1326
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1327 AKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQDAEEAV 1406
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL---SKLEEEVSRIEARLREIEQKL 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1407 EAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKL 1486
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1487 KNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHE----------LEKVRKQLEvEKLELQSALEEAE--ASLE 1554
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQ-RVEEEIRALEPVNmlAIQE 980
|
810 820 830
....*....|....*....|....*....|....*...
gi 124376530 1555 HEEGKILRAQLEFNQIKAEIERK-LAEKDEEMEQAKRN 1591
Cdd:TIGR02169 981 YEEVLKRLDELKEKRAKLEEERKaILERIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1312-1931 |
4.88e-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: 4.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1312 QQMEDLKRQ---------LEEEGKAK--NALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVaqwrtkyetd 1380
Cdd:COG1196 200 RQLEPLERQaekaeryreLKEELKELeaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL---------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1381 aiqrtEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQ 1460
Cdd:COG1196 270 -----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1461 KYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKL 1540
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1541 ELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRsrnevLRVKKKM 1620
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-----LLLLLEA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1621 EGDlnemeiqlshanrmAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQaeleelRAVVEQTERS 1700
Cdd:COG1196 500 EAD--------------YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ------NIVVEDDEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1701 RKLAEQELIETSERVQLLHSqntSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAH 1780
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPL---DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1781 LERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVkgmRKSERRIKELTYQTEEDK 1860
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL---EEALLAEEEEERELAEAE 713
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124376530 1861 KNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSkfrKVQHELDEAEERADIAESQVNKLRAKSRDIGA 1931
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLE---EEALEELPEPPDLEELERELERLEREIEALGP 781
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
845-1580 |
1.01e-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: 103.22 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 845 AETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKND--------------------------------LQLQ 892
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKaeryqallkekreyegyellkekealerqkeaIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 893 VQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDE-EEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKH 971
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 972 ATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLE 1051
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1052 RAKRKLegdlkltQESIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTAR 1131
Cdd:TIGR02169 406 RELDRL-------QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1132 AKVEKLRSDLSRELEEISERL----EEAGGATSVQIEMNKKREAEFQKMrRDLEEATLQHEA---TAAALRKKHA----D 1200
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQAraseERVRGGRAVEEVLKASIQGVHGTV-AQLGSVGERYATaieVAAGNRLNNVvvedD 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1201 SVAElgEQIDNLQRVK------------QKLEKEKS--------EFKLELDDVTSNMEQIIKAKANLEKVSRTLE---DQ 1257
Cdd:TIGR02169 558 AVAK--EAIELLKRRKagratflplnkmRDERRDLSilsedgviGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEaarRL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1258 ANEYR-VKLE--------------EAQRSLNDFTT-QRAKLQTENGELARQLEEKEALISQLTRGK---LSYTQQMEDLK 1318
Cdd:TIGR02169 636 MGKYRmVTLEgelfeksgamtggsRAPRGGILFSRsEPAELQRLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDAS 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1319 RQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQwrtkYETDAIQRTEELEEAKKKLAQr 1398
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE----LEEDLHKLEEALNDLEARLSH- 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1399 lqdaeEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARS 1478
Cdd:TIGR02169 791 -----SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1479 LSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEg 1558
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE- 944
|
810 820
....*....|....*....|..
gi 124376530 1559 KILRAQLEFNQIKAEIERKLAE 1580
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRVEEE 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1075-1731 |
1.15e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.09 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1075 KLQLEEKLKKKE---FDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISER 1151
Cdd:COG1196 217 ELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1152 LEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALrkkhadsvAELGEQIDNLQRVKQKLEKEKSEFKLELD 1231
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL--------EELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1232 DVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTrgklsyt 1311
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE------- 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1312 QQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEA 1391
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1392 KKKLAQRLQDAEEAVEAVnakcsslektkhrLQNEIEDLMVDVERSNAAAAAldkKQRNFDKILAEWKQKYEESQSELES 1471
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAA-------------LEAALAAALQNIVVEDDEVAA---AAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1472 SQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKnvhelekVRKQLEVEKLELQSALEEAEA 1551
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR-------RAVTLAGRLREVTLEGEGGSA 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1552 SLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQL 1631
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1632 ShanrmaaeaqkqvkslqsLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEqtersrkLAEQELIET 1711
Cdd:COG1196 739 E------------------ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNL-------LAIEEYEEL 793
|
650 660
....*....|....*....|
gi 124376530 1712 SERVQLLHSQNTSLINQKKK 1731
Cdd:COG1196 794 EERYDFLSEQREDLEEARET 813
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1202-1830 |
1.22e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.63 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1202 VAELGEQIDNLQRVKQKLEKEKsEFKLELDdvtsnmeqIIKAKANLEKVsRTLEDQANEYRVKLEEAQRSLNDFTTQRAK 1281
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYR-ELKEELK--------ELEAELLLLKL-RELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1282 LQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELqr 1361
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL-- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1362 vlskansevaqwrtkyETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAA 1441
Cdd:COG1196 343 ----------------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1442 AALDKKQRNFDKILAewkqkyeesqselessqkEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEG 1521
Cdd:COG1196 407 EAEEALLERLERLEE------------------ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1522 GKNVHELEKVRKQLEVEKLELQS---ALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQRVVDS 1598
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAArllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1599 LQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLlkDTQIQLDDAVRANDDLKENIAIVER 1678
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAV--DLVASDLREADARYYVLGDTLLGRT 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1679 RNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAK 1758
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124376530 1759 KAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELEGELEA 1830
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
951-1862 |
7.54e-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: 97.06 E-value: 7.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 951 ELKKDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQAL--DDLQVEEDKV--------- 1019
Cdd:TIGR02169 154 ERRKIIDEIA-GVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYegyellkek 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1020 NSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDL-ENDKLQLEEKLKKKEFDINQQNSKIED 1098
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1099 eqvlalqLQKKLKENQARieeleeeleaertaRAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRR 1178
Cdd:TIGR02169 313 -------KERELEDAEER--------------LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1179 DLEEAtlqhEATAAALRKKHADSVAEL---GEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVS---- 1251
Cdd:TIGR02169 372 ELEEV----DKEFAETRDELKDYREKLeklKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKedka 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1252 ---RTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLE------ 1322
Cdd:TIGR02169 448 leiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtv 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1323 -EEGKAKNALAHALQSArhdcdllreqyeeeteAKAELQRVLSKaNSEVAQWRTKYETDA-IQRTEELEEAKKKLAQRLQ 1400
Cdd:TIGR02169 528 aQLGSVGERYATAIEVA----------------AGNRLNNVVVE-DDAVAKEAIELLKRRkAGRATFLPLNKMRDERRDL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1401 DAEEAVEAVNAKCSSLEktkhrLQNEIEDLMVDVERSNAAAAALDKKQRNFDKI---------------LAEWKQKYEES 1465
Cdd:TIGR02169 591 SILSEDGVIGFAVDLVE-----FDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYrmvtlegelfeksgaMTGGSRAPRGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1466 QSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVR-------KQLEVE 1538
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEeklkerlEELEED 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1539 KLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQRVVDslqtsldaETRSRNEvlrvkk 1618
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE--------EEVSRIE------ 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1619 kmeGDLNEMEIQLSHANRMAAEAQKQVKSLQSLlkdtqiqlddavraNDDLKENIAIVERRNNLLQAELEELRAVVEQTE 1698
Cdd:TIGR02169 812 ---ARLREIEQKLNRLTLEKEYLEKEIQELQEQ--------------RIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1699 RSRKLAEQELIEtservqlLHSQNTSLINQKKKMESDLTQLQSEVEEAvqECRNAEEKAKKAItdaamMAEELKkeqdts 1778
Cdd:TIGR02169 875 AALRDLESRLGD-------LKKERDELEAQLRELERKIEELEAQIEKK--RKRLSELKAKLEA-----LEEELS------ 934
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1779 aHLERMKKNMEQtikdlqhrlDEAEQIALKGGKKQLQKLEARVRELEG-------ELEAEQKRNAESVKGMRK--SERR- 1848
Cdd:TIGR02169 935 -EIEDPKGEDEE---------IPEEELSLEDVQAELQRVEEEIRALEPvnmlaiqEYEEVLKRLDELKEKRAKleEERKa 1004
|
970
....*....|....
gi 124376530 1849 IKELTYQTEEDKKN 1862
Cdd:TIGR02169 1005 ILERIEEYEKKKRE 1018
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
221-708 |
6.24e-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: 94.04 E-value: 6.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 221 IIQANPALEAFGNAKTVRNDNSSRFGKF--IRIHFGATG---KLASADIETYLLEKSRVIFQL------KAERNYHIFYQ 289
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 290 ILSNKKPELLDMLLVTNNPYD------YAFVSQGEVSVASIDDSEELMATD--------SAFDVLGFTSEEKAGVYKLTG 355
Cdd:cd14894 329 MVAGVNAFPFMRLLAKELHLDgidcsaLTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 356 AIMHYGNMKFKQKQREEQAEPDGT---EDADKSAYLMGLNSADLLKGLCHPR---VKVGNEYVTKGQSVQQVYYSIGALA 429
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 430 KAVYEKMFNWMV------TRINATLETKQPRQY-----------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLqqffnh 492
Cdd:cd14894 489 RLLYQLAFNYVVfvmneaTKMSALSTDGNKHQMdsnasapeavsLLKIVDVFGFEDLTHNSLDQLCINYLSEKL------ 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 493 hmFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMT----------FKAKLYDNHlgkSN 562
Cdd:cd14894 563 --YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNaqqeekrnklFVRNIYDRN---SS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 563 NFQKPRNIKGKQEAH---------FSLIHYAGTVDYNILGWLEKNKDPLNETVVALYQKSSLKLMATLF---SSYATADT 630
Cdd:cd14894 638 RLPEPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLnesSQLGWSPN 717
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124376530 631 GDSGKSKGGKKKGSSFQTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICR 708
Cdd:cd14894 718 TNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
855-1593 |
1.10e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.67 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 855 KEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQ-DNLNDAEERCDQLIKNKIQLEAKVKEMNERLED--- 930
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEakk 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 931 -EEEMNAELTAK---------KRKLEDECSELKKDIDDLEltlaKVEKEKHATENKVknlTEEMAGLDEIIAKLTKEKKA 1000
Cdd:PTZ00121 1245 aEEERNNEEIRKfeearmahfARRQAAIKAEEARKADELK----KAEEKKKADEAKK---AEEKKKADEAKKKAEEAKKA 1317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1001 ------LQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEgDLKLTQESIMDLEND 1074
Cdd:PTZ00121 1318 deakkkAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-AAKKKAEEKKKADEA 1396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1075 KLQLEEKLKKKEfdinqQNSKIEDEQVLALQLQKKLKENQarieeleeeleaertaRAKVEKLRSDLSRELEEISERLEE 1154
Cdd:PTZ00121 1397 KKKAEEDKKKAD-----ELKKAAAAKKKADEAKKKAEEKK----------------KADEAKKKAEEAKKADEAKKKAEE 1455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1155 AGGATSVQIEMNKKREAEfqKMRRDLEEATLQHEATAAALR-KKHADSVAELGEQIDNLQRVKQKLEKEKSEfKLELDDV 1233
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKAD--EAKKKAEEAKKADEAKKKAEEaKKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEE 1532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1234 TSNMEQIIKA--KANLEKVSRTLEDQANEYRVKLEEAQRSlndftTQRAKLQTENGELARQLEEKEaLISQLTRGKLSYT 1311
Cdd:PTZ00121 1533 AKKADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKA-----EEDKNMALRKAEEAKKAEEAR-IEEVMKLYEEEKK 1606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1312 QQMEDLKRqlEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEEL--- 1388
Cdd:PTZ00121 1607 MKAEEAKK--AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkka 1683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1389 -EEAKKKLAQRLQDAEEA--VEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSnaaaaaldKKQRNFDKILAEWKQKYEES 1465
Cdd:PTZ00121 1684 eEDEKKAAEALKKEAEEAkkAEELKKKEAEEKKKAEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEE 1755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1466 QSELESSQKEARSLSTELFKLKNAY--EESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLE-- 1541
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKev 1835
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124376530 1542 ---LQSALEEAEASLEH------EEGKILRAQLEFNQIKAEIErklaEKDEEMEQAKRNHQ 1593
Cdd:PTZ00121 1836 adsKNMQLEEADAFEKHkfnknnENGEDGNKEADFNKEKDLKE----DDEEEIEEADEIEK 1892
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
913-1805 |
1.73e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.90 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 913 NKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDEC-SELKKDIDDLELT-LAKVEKEKHATENKVKnlTEEMAGLDEi 990
Cdd:PTZ00121 1056 HEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEAtEEAFGKAEEAKKTeTGKAEEARKAEEAKKK--AEDARKAEE- 1132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 991 iAKLTKEKKALQEAhQQALDDLQVEEDKVNSLSKsKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLtqESIMD 1070
Cdd:PTZ00121 1133 -ARKAEDARKAEEA-RKAEDAKRVEIARKAEDAR-KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKA--EAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1071 LENDKlQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKV-----EKLRSDLSREL 1145
Cdd:PTZ00121 1208 AEEER-KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaikaeEARKADELKKA 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1146 EEIsERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsvAELGEQIDNLQRVKQKLEKEKSE 1225
Cdd:PTZ00121 1287 EEK-KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK-----AEEAKKAAEAAKAEAEAAADEAE 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1226 FKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTtQRAKLQTENGELARQLEEKEAliSQLTR 1305
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKKK--ADEAK 1437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1306 GKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARhdCDLLREQYEEETEAKaELQRVLSKANSEVAQWRTKYEtdAIQRT 1385
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK--ADEAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAE--AKKKA 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1386 EELEEAK-KKLAQRLQDAEEAVEAVNAKcSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKyee 1464
Cdd:PTZ00121 1513 DEAKKAEeAKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK--- 1588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1465 sqsELESSQKEARSLSTELFKLKnAYEESLEHLETFKRENKNLQEEISDLTEQLGEggknvHELEKVRKQLEVEKLELQS 1544
Cdd:PTZ00121 1589 ---AEEARIEEVMKLYEEEKKMK-AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK-----KEAEEKKKAEELKKAEEEN 1659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1545 ALEEAEASLEHEEGKI----LRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKM 1620
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKkaeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1621 EGDlnemeiqlshaNRMAAEAQKQVKSLQsllKDTQIQLDDAVRANDDLKENIAIVERRnnlLQAELEELRAVVEQTERS 1700
Cdd:PTZ00121 1740 EED-----------KKKAEEAKKDEEEKK---KIAHLKKEEEKKAEEIRKEKEAVIEEE---LDEEDEKRRMEVDKKIKD 1802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1701 RKlaeqeliETSERVQLLHSQNTSLINQKKKMESdltqlqSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAH 1780
Cdd:PTZ00121 1803 IF-------DNFANIIEGGKEGNLVINDSKEMED------SAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEAD 1869
|
890 900
....*....|....*....|....*
gi 124376530 1781 LERMKKNMEQTIKDLQHRlDEAEQI 1805
Cdd:PTZ00121 1870 FNKEKDLKEDDEEEIEEA-DEIEKI 1893
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
919-1795 |
1.82e-18 |
|
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: 92.82 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 919 AKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKKdIDDLELTLAKVE-----KEKHATENKVKNLTEEMAGLDEIIAK 993
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 994 LTKEKKALQEAHQQALDDLQVEEDKVNSLSKSK-VKLEQQVDDLEGSLEQekkvrmdlerakrkLEGDLKLTQESIMDLE 1072
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAEIAS--------------LERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1073 NDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERL 1152
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1153 EEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHAdsvaelgeqidnlqrvkqKLEKEKSEFKLELDD 1232
Cdd:TIGR02169 402 NEL-----------KRELDRLQEELQRLSEELADLNAAIAGIEAKIN------------------ELEEEKEDKALEIKK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1233 VTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEA-------LISQLTR 1305
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1306 GKLSYTQQMEDLKRQ------LEEEGKAKNA--LAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKY 1377
Cdd:TIGR02169 533 VGERYATAIEVAAGNrlnnvvVEDDAVAKEAieLLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1378 ETD---AIQRT---EELEEAKK--------KLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAA 1443
Cdd:TIGR02169 613 EPAfkyVFGDTlvvEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1444 LDKKQRNFDKILAEWKQKyeesqselessqkeARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGK 1523
Cdd:TIGR02169 693 LQSELRRIENRLDELSQE--------------LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1524 NVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEF-NQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQts 1602
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKlEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ-- 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1603 ldaETRSRNEVLRVKKKMEGD-LNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDavranddlkeniaiverrnn 1681
Cdd:TIGR02169 837 ---ELQEQRIDLKEQIKSIEKeIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE-------------------- 893
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1682 lLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMES------DLTQLQSEVEEAVQECRNAEE 1755
Cdd:TIGR02169 894 -LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelSLEDVQAELQRVEEEIRALEP 972
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 124376530 1756 KAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDL 1795
Cdd:TIGR02169 973 VNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1085-1885 |
2.37e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.51 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1085 KEFDINQQNSKIEDEQVLalQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIE 1164
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATE--EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1165 MNKKREAEFQKMR--RDLEEATLQHEA-TAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEfKLELDDVTSNMEQII 1241
Cdd:PTZ00121 1155 EIARKAEDARKAEeaRKAEDAKKAEAArKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1242 KAKANLEKVSRTLEDQANEYRVKLEEAQrsLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQL 1321
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEAR--MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1322 EEEGKAKNALAHAlQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELE--EAKKKLAQRL 1399
Cdd:PTZ00121 1312 EEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKkaDAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1400 QDAEEA---VEAVNAKCSSLEKtKHRLQNEIEDLMVDVERSNAAAAAldKKQRNFDKILAEWKQKYEESQSELESSQKEA 1476
Cdd:PTZ00121 1391 KKADEAkkkAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1477 RSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQlGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHE 1556
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1557 EGKILRaqlefnqiKAEiERKLAEKDEEMEQAKRNHQRVVDSLQtsldaetrsRNEVLRvkKKMEGDLNEMEIQLSHANR 1636
Cdd:PTZ00121 1547 KADELK--------KAE-ELKKAEEKKKAEEAKKAEEDKNMALR---------KAEEAK--KAEEARIEEVMKLYEEEKK 1606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1637 MAAEAQKqvKSLQSLLKDTQIQLDDAVRanddlkeniaivERRNNLLQAELEELRavveQTERSRKLAEQELIETSErvq 1716
Cdd:PTZ00121 1607 MKAEEAK--KAEEAKIKAEELKKAEEEK------------KKVEQLKKKEAEEKK----KAEELKKAEEENKIKAAE--- 1665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1717 llhsqntslinQKKKMESDltqlqsevEEAVQECRNAEEKAKKAitdaammAEELKKEQDTSAHLERMKKNMEQTIKdlq 1796
Cdd:PTZ00121 1666 -----------EAKKAEED--------KKKAEEAKKAEEDEKKA-------AEALKKEAEEAKKAEELKKKEAEEKK--- 1716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1797 hrldEAEQIalkggKKQLQKLEARVRELEGELEaEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLK 1876
Cdd:PTZ00121 1717 ----KAEEL-----KKAEEENKIKAEEAKKEAE-EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
....*....
gi 124376530 1877 VKAYKRQAE 1885
Cdd:PTZ00121 1787 EEDEKRRME 1795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1214-1913 |
2.64e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.51 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1214 RVKQKLEKEKSEFKLELDDVTSNMEQIIK---AKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTE--NGE 1288
Cdd:PTZ00121 1088 RADEATEEAFGKAEEAKKTETGKAEEARKaeeAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDarKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1289 LARQLEEK---EALISQLTRGKLSYTQQMEDLK-----RQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAK-AEL 1359
Cdd:PTZ00121 1168 EARKAEDAkkaEAARKAEEVRKAEELRKAEDARkaeaaRKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkAEE 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1360 QRvlskANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDlmvdversNA 1439
Cdd:PTZ00121 1248 ER----NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE--------AK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1440 AAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELfklkNAYEESLEHLETFKRENKNLQEEISDLTEQlg 1519
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA----EAAEEKAEAAEKKKEEAKKKADAAKKKAEE-- 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1520 eggknVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEfnqiKAEIERKLAEKDEEMEQAKRNHQRVVDSL 1599
Cdd:PTZ00121 1390 -----KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK----KADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1600 QTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQsllKDTQIQLDDAVRANDDLK---ENIAIV 1676
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK---KADEAKKAEEAKKADEAKkaeEAKKAD 1537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1677 ERRNNLLQAELEELRAV--VEQTERSRKlAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAE 1754
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAeeLKKAEEKKK-AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1755 EKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGG--KKQLQKLEARVRELEGElEAEQ 1832
Cdd:PTZ00121 1617 EAKIKA--------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeAKKAEEDKKKAEEAKKA-EEDE 1687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1833 KRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAE---EQANTNLSKFRKVQHELDEAE 1909
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEE 1767
|
....
gi 124376530 1910 ERAD 1913
Cdd:PTZ00121 1768 KKAE 1771
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1204-1929 |
4.66e-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: 91.39 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1204 ELGEQIDNLQRVKQKLEKEKSEFKleldDVTSNMEQIIKAKANLEKVSRT---LEDQANEYRVKLEEAQRSLNDFTtqra 1280
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELK----ELEKKHQQLCEEKNALQEQLQAeteLCAEAEEMRARLAARKQELEEIL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1281 klqtenGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKnalaHALQSARHDCDLLREQYEEETEAKAELQ 1360
Cdd:pfam01576 78 ------HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAAR----QKLQLEKVTTEAKIKKLEEDILLLEDQN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1361 RVLSKAnsevaqwrtkyetdaiqrteeleeaKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAA 1440
Cdd:pfam01576 148 SKLSKE-------------------------RKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1441 AAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGE 1520
Cdd:pfam01576 203 RQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLES 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1521 GGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQ 1600
Cdd:pfam01576 283 ERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1601 TSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEniaiverRN 1680
Cdd:pfam01576 363 EQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAE-------KL 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1681 NLLQAELEELRAVVEQTE-RSRKLA------EQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNA 1753
Cdd:pfam01576 436 SKLQSELESVSSLLNEAEgKNIKLSkdvsslESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNV 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1754 EEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKggkkqLQKLEARVRELEGELEAEQK 1833
Cdd:pfam01576 516 ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDK-----LEKTKNRLQQELDDLLVDLD 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1834 RNAESVKGMRKSERRIKELTyqtEEDKKNLLRLQDLVDKlqlkvkaykrqaeeAEEQANTNLSKFRKVQHELDEAEERAD 1913
Cdd:pfam01576 591 HQRQLVSNLEKKQKKFDQML---AEEKAISARYAEERDR--------------AEAEAREKETRALSLARALEEALEAKE 653
|
730
....*....|....*.
gi 124376530 1914 IAESQVNKLRAKSRDI 1929
Cdd:pfam01576 654 ELERTNKQLRAEMEDL 669
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
843-1513 |
1.49e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.82 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 843 KSAETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQaEQDNLNDAEERCDQLIKNKIQLEAKVK 922
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAE-EAKKADEAKKKAEEAKKKADAAKKKAE 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 923 EMNERLE--DEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 1000
Cdd:PTZ00121 1340 EAKKAAEaaKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK 1419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1001 LQEAHQQAlddlqvEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGD-LKLTQESIMDLENDKLQLE 1079
Cdd:PTZ00121 1420 ADEAKKKA------EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAEEAKKADEAKKKAE 1493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1080 EKLKKKEfdinqQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggat 1159
Cdd:PTZ00121 1494 EAKKKAD-----EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK---- 1564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1160 svQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEfklelDDVTSNMEQ 1239
Cdd:PTZ00121 1565 --KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKKVEQ 1637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1240 IIKAKANLEKVSRTLEDQANEYRVKLEEAQRslndfttqRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKR 1319
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAK--------KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1320 QLEEEGKAKNALAHALQSARHDCDLLREQyEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEEL-----EEAKKK 1394
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeavieEELDEE 1788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1395 LAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKilAEWKQKYEESQSELESSQK 1474
Cdd:PTZ00121 1789 DEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEAD--AFEKHKFNKNNENGEDGNK 1866
|
650 660 670
....*....|....*....|....*....|....*....
gi 124376530 1475 EARSlSTELFKLKNAYEESLEHLETFKRENKNLQEEISD 1513
Cdd:PTZ00121 1867 EADF-NKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
862-1229 |
2.48e-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: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 862 KETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAK 941
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 942 KRKLEDECSELKKDIDDLELTLAKVEK-----EKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEE 1016
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1017 DKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSKI 1096
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1097 EDEQVLALQLQKK---LKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEIsERLEEAGGATSVQIEMNKKREAEF 1173
Cdd:TIGR02169 913 EKKRKRLSELKAKleaLEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDEL 991
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 124376530 1174 QKMRRDLEEATLQHEATAAALRKKHADSVAELGEQI-DNLQRVKQKLEKEKSEFKLE 1229
Cdd:TIGR02169 992 KEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAInENFNEIFAELSGGTGELILE 1048
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
862-1575 |
3.27e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 88.15 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 862 KETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLiKNKIQ-LEAKVKEMNERLEDEEEMNAELTA 940
Cdd:TIGR04523 25 KNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNS-NNKIKiLEQQIKDLNDKLKKNKDKINKLNS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 941 KKRKLEDECSELKKDIDDLELTLAKVEKEKHATE-------NKVKNLTEEMAGLDEIIAKLTKEKKALqeahqqalddlq 1013
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEEL------------ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1014 veEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLErakrKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDINQQN 1093
Cdd:TIGR04523 172 --ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1094 SKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEaggatsvqiEMNKKREAEF 1173
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ---------DWNKELKSEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1174 QKMRRDLEEATLQheataaalRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRT 1253
Cdd:TIGR04523 317 KNQEKKLEEIQNQ--------ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1254 LEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLtrgklsyTQQMEDLKRQLEEEGKAKNALAH 1333
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN-------NSEIKDLTNQDSVKELIIKNLDN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1334 ALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQDAEEAVEAVNAKC 1413
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL---------------KKLNEEKKELEEKVKDLTKKISSLKEKI 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1414 SSLEKTKHRLQNEIEDLMVDVER--SNAAAAALDKKQRNFDKILAEWKQKYEesqselessqkearslstelfKLKNAYE 1491
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQK---------------------SLKKKQE 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1492 ESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIK 1571
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEII 665
|
....
gi 124376530 1572 AEIE 1575
Cdd:TIGR04523 666 KKIK 669
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
872-1427 |
7.52e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.02 E-value: 7.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 872 RKELEEKmvsllqEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTakkrkledecsE 951
Cdd:PRK02224 193 KAQIEEK------EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE-----------T 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 952 LKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEkKALQEAHQQALDDLQVEedkvnslskskvkLEQ 1031
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLDDADAEAVEARREE-------------LED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1032 QVDDLEGSLEQekkVRMDLERAKRKLEGdlklTQESIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLK 1111
Cdd:PRK02224 322 RDEELRDRLEE---CRVAAQAHNEEAES----LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1112 ENQARIE-------ELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGG--------------ATSVQIEMNKKRE 1170
Cdd:PRK02224 395 ELRERFGdapvdlgNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDR 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1171 AEFQKMRRDLEEATLQHEATAAALRKkhADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKV 1250
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLER--AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1251 SRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELAR------QLEEKEALISQLtRGKLSYTQQMEDLKR-QLEE 1323
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaAIADAEDEIERL-REKREALAELNDERReRLAE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1324 EGKAKNALAHALQSARhdcdllreqYEEETEAKAELQRVLSKANSEVAQWRTkyETDAIQRT--------EELEEAKKKL 1395
Cdd:PRK02224 632 KRERKRELEAEFDEAR---------IEEAREDKERAEEYLEQVEEKLDELRE--ERDDLQAEigavenelEELEELRERR 700
|
570 580 590
....*....|....*....|....*....|..
gi 124376530 1396 AQrLQDAEEAVEAVNAKCSSLEKTKHRLQNEI 1427
Cdd:PRK02224 701 EA-LENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1624-1925 |
3.53e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1624 LNEMEIQLSHANRMAAEAQKqVKSLQSLLKDTQIQLddAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKL 1703
Cdd:COG1196 195 LGELERQLEPLERQAEKAER-YRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1704 AEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1783
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1784 MKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKgMRKSERRIKELTYQTEEDKKNL 1863
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA-EEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124376530 1864 LRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1925
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1146-1888 |
5.04e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.81 E-value: 5.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1146 EEISERLEEAGGATSVQIEMNKKREAEFQKMR--RDLEEATLQHEA-TAAALRKKHADSVAELGEQIDNLQRVKQKLEKE 1222
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEdaRKAEEARKAEDArKAEEARKAEDAKRVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1223 KSefklelddvtsnmeQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKlQTENGELARQLEEKEALISQ 1302
Cdd:PTZ00121 1174 DA--------------KKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAEEAKKD 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1303 LTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAI 1382
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1383 QRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAaaaldKKQRNFDKILAEWKQKY 1462
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-----KKKADAAKKKAEEKKKA 1393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1463 EESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEvEKLEL 1542
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE-EAKKA 1472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1543 QSALEEAEASLEHEEgkiLRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQrvvdslqtsldaetrsrnevlrvKKKMEg 1622
Cdd:PTZ00121 1473 DEAKKKAEEAKKADE---AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE-----------------------AKKAD- 1525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1623 dlnemEIQLSHANRMAAEAQK--QVKSLQSLLKDTQIQLDDAVRANDDLKENiaivERRNNLLQAELEELRAVVE-QTER 1699
Cdd:PTZ00121 1526 -----EAKKAEEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEaRIEE 1596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1700 SRKLAEQELIETSERVQLLHSQNTSlINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSA 1779
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1780 HLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEED 1859
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
730 740
....*....|....*....|....*....
gi 124376530 1860 KKNLLRLQDLVDKLQLKVKAYKRQAEEAE 1888
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
842-1403 |
6.98e-16 |
|
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: 84.01 E-value: 6.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 842 LKSAETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNlndAEERCDQLIKNKIQLEAKV 921
Cdd:pfam15921 250 LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 922 kemnerledeEEMNAELTAKKRKLEDECSELKKD--IDDLELTLAKVEKEKHATENkvKNLTEEmagLDEIIAKLTKEKK 999
Cdd:pfam15921 327 ----------SQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQ---LQKLLADLHKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1000 ALQEAHQQ--------------------ALDDLQVEEDKVNSL-----SKSKVKLEQQVDDLEG---SLEQEKKVRMDLE 1051
Cdd:pfam15921 392 ELSLEKEQnkrlwdrdtgnsitidhlrrELDDRNMEVQRLEALlkamkSECQGQMERQMAAIQGkneSLEKVSSLTAQLE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1052 RAKRKLEGDLKLTQESIMDLENDKL---QLEEKLKKKEFDINQQNS---KIEDEQVLALQLQKKLKENQARIEELEEELE 1125
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLESSERtvsDLTASLQEKERAIEATNAeitKLRSRVDLKLQELQHLKNEGDHLRNVQTECE 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1126 AERTARAKVEKLRSDLSRELEEISERLEEAG---GATSV-----QIEMNKKR-EAEFQKMRRDLEEATLQH-EATAAALR 1195
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGrtaGAMQVekaqlEKEINDRRlELQEFKILKDKKDAKIRElEARVSDLE 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1196 KKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDF 1275
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1276 TTQRAKLQTENGE-------LARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARH-------D 1341
Cdd:pfam15921 712 RNTLKSMEGSDGHamkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATeknkmagE 791
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124376530 1342 CDLLREQYEEETEAKAELQRVLSKANSEVAQWRtkyetDAIQRTEElEEAKKKLAQRLQDAE 1403
Cdd:pfam15921 792 LEVLRSQERRLKEKVANMEVALDKASLQFAECQ-----DIIQRQEQ-ESVRLKLQHTLDVKE 847
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
845-1457 |
7.17e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.96 E-value: 7.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 845 AETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEM 924
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 925 NERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN-------LTEEMAGLDEIIAKLTKE 997
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGgraveevLKASIQGVHGTVAQLGSV 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 998 K----KALQEAHQQALDDLQVEED--------------------------KVNSLSKSKVKLEQQVDDLEGSLEQEKKVR 1047
Cdd:TIGR02169 534 GeryaTAIEVAAGNRLNNVVVEDDavakeaiellkrrkagratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPKYE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1048 -------------MDLERAKRkLEGDLKLtqesimdlendkLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQ 1114
Cdd:TIGR02169 614 pafkyvfgdtlvvEDIEAARR-LMGKYRM------------VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLR 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1115 ARIEELEEELEAERTARAKVEKLR-------SDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLE--EATL 1185
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLdelsqelSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEnvKSEL 760
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1186 QH--------EATAAALRKKHADSVAELG-EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLED 1256
Cdd:TIGR02169 761 KElearieelEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1257 QANEYRVKLEEAQRSLNDfttqrakLQTENGELARQLEEKEALISQLtrgklsyTQQMEDLKRQLEEEGKAKNALAHALQ 1336
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIEN-------LNGKKEELEEELEELEAALRDL-------ESRLGDLKKERDELEAQLRELERKIE 906
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1337 SARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQD-------AEEAVEAV 1409
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE--DEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEV 984
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 124376530 1410 NAKCSSLEKTKHRLQNEIEDL-----MVDVERSNAAAAALDKKQRNFDKILAE 1457
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
941-1589 |
1.00e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 83.15 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 941 KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLD----EIIAKLTKEKKALQEAHQqaldDLQVEE 1016
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEqqikDLNDKLKKNKDKINKLNS----DLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1017 DKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKL-------TQESIMDLENDKLQLEEKLKKKEFDI 1089
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKlnnkyndLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1090 NQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKr 1169
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1170 eaefqkmrrdLEEATLQHEATAAALRkkhadsvaELGEQIDNLQRVKQKLEKEKSEfkleldDVTSNMEQIIKakaNLEK 1249
Cdd:TIGR04523 269 ----------LSEKQKELEQNNKKIK--------ELEKQLNQLKSEISDLNNQKEQ------DWNKELKSELK---NQEK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1250 VSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSY-------TQQMEDLKRQLE 1322
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYkqeiknlESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1323 EEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYetdaiqrteeleeakKKLAQRLQDA 1402
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELII---------------KNLDNTRESL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1403 EEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTE 1482
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1483 LFKLKnaYEESLEHLETFKRENknlQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILR 1562
Cdd:TIGR04523 547 LNKDD--FELKKENLEKEIDEK---NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
650 660
....*....|....*....|....*..
gi 124376530 1563 AQLEFNQIKAEIERKLAEKDEEMEQAK 1589
Cdd:TIGR04523 622 AKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
960-1787 |
1.04e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 83.48 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 960 ELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGS 1039
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1040 LEQEKKvrmdlERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQ-----LQKKLKENQ 1114
Cdd:pfam02463 260 IEKEEE-----KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEkekkkAEKELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1115 ARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKM----------RRDLEEAT 1184
Cdd:pfam02463 335 EEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEElelkseeekeAQLLLELA 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1185 LQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVK 1264
Cdd:pfam02463 415 RQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1265 LEEAQRSlndfttQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHAlqsarhDCDL 1344
Cdd:pfam02463 495 LEERSQK------ESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD------EVEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1345 LREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSL--EKTKHR 1422
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELtkLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1423 LQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKR 1502
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1503 ENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKD 1582
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1583 EEMEQAKRNH----QRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQlsHANRMAAEAQKQVKSLQSLLKDTQIQ 1658
Cdd:pfam02463 803 LRALEEELKEeaelLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE--ELERLEEEITKEELLQELLLKEEELE 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1659 LDDAVRanddlkENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQ 1738
Cdd:pfam02463 881 EQKLKD------ELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN 954
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 124376530 1739 LQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKN 1787
Cdd:pfam02463 955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
848-1855 |
2.66e-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: 82.09 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 848 EKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQ-----------AEQDNLNDAEERCDQLIKNKIQ 916
Cdd:pfam15921 102 EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQntvheleaakcLKEDMLEDSNTQIEQLRKMMLS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 917 LEAKVKEMNERLEDEEE-------------------MNAELTAKKRKLEDECSELKKDIDDLEltlAKVEKEKHATENKV 977
Cdd:pfam15921 182 HEGVLQEIRSILVDFEEasgkkiyehdsmstmhfrsLGSAISKILRELDTEISYLKGRIFPVE---DQLEALKSESQNKI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 978 KNLTEEMAG-LDEIIAKLTKEKKALQE----AHQQAlDDLQVEEDKVNSLSKSKVKL-EQQVDDLEGSLEQekkVRMDLE 1051
Cdd:pfam15921 259 ELLLQQHQDrIEQLISEHEVEITGLTEkassARSQA-NSIQSQLEIIQEQARNQNSMyMRQLSDLESTVSQ---LRSELR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1052 RAKRKLEGDLKLTQESIMdLENDKLQlEEKLKKKEFdiNQQNSKIEDeqvlalQLQKKLkenqarieeleeeleaertar 1131
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLV-LANSELT-EARTERDQF--SQESGNLDD------QLQKLL--------------------- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1132 AKVEKLRSDLSRELEEiSERLEEAGGATSVQIEmnkkreaefqKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDN 1211
Cdd:pfam15921 384 ADLHKREKELSLEKEQ-NKRLWDRDTGNSITID----------HLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1212 LQRVKQKLEKeksefklelddVTSNMEQIIKAKANLEKVSRTLEDQaneyRVKLEEAQRSLNDFTTqraklqtengelar 1291
Cdd:pfam15921 453 IQGKNESLEK-----------VSSLTAQLESTKEMLRKVVEELTAK----KMTLESSERTVSDLTA-------------- 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1292 QLEEKEALIsQLTRGKLSYTQQMEDLKrqLEEEGKAKNALAHaLQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVA 1371
Cdd:pfam15921 504 SLQEKERAI-EATNAEITKLRSRVDLK--LQELQHLKNEGDH-LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVG 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1372 QW----------RTKYETDAIQRTEELEEAK----------KKLAQRLQDAE-EAVEAVNAKCSSLEKTKHrLQNEIEDL 1430
Cdd:pfam15921 580 QHgrtagamqveKAQLEKEINDRRLELQEFKilkdkkdakiRELEARVSDLElEKVKLVNAGSERLRAVKD-IKQERDQL 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1431 MVDVERSNaaaAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEE-------------SLEHL 1497
Cdd:pfam15921 659 LNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdghamkvamGMQKQ 735
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1498 ETFKRENKN-LQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEheegkILRAQlefnqikaeiER 1576
Cdd:pfam15921 736 ITAKRGQIDaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELE-----VLRSQ----------ER 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1577 KLAEKDEEMEQAKRNHqrvvdSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQ---LSHANRMAAEAQKQVKSLQSLLK 1653
Cdd:pfam15921 801 RLKEKVANMEVALDKA-----SLQFAECQDIIQRQEQESVRLKLQHTLDVKELQgpgYTSNSSMKPRLLQPASFTRTHSN 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1654 DTQIQLDDAVRANDDLKENiAIVERRNNLLQAELEELRAVVEQTE-----------------RSRKLAEQELIETSERVQ 1716
Cdd:pfam15921 876 VPSSQSTASFLSHHSRKTN-ALKEDPTRDLKQLLQELRSVINEEPtvqlskaedkgrapslgALDDRVRDCIIESSLRSD 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1717 LLHSQNTSLINQKKKMESDLTQlqseveEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDL- 1795
Cdd:pfam15921 955 ICHSSSNSLQTEGSKSSETCSR------EPVLLHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSPKKSPVHSLLTSSa 1028
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124376530 1796 --------QHR----------LDEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQ 1855
Cdd:pfam15921 1029 egsigsssQYRsaktihspdsVKDSQSLPIETTGKTCRKLQNRLESLQTLVEDLQLKNQAMSSMIRNQEKRIQKVKDQ 1106
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
859-1454 |
1.02e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.11 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 859 GRIKETLEKSEARRK---------ELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLE 929
Cdd:PRK03918 135 GEIDAILESDESREKvvrqilgldDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 930 DEEEMNAELtAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEahqqal 1009
Cdd:PRK03918 215 ELPELREEL-EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE------ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1010 ddLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEqekkvrmdlerakrKLEGDLKLTQESIMDLENDKLQLEEkLKKKEFDI 1089
Cdd:PRK03918 288 --LKEKAEEYIKLSEFYEEYLDELREIEKRLS--------------RLEEEINGIEERIKELEEKEERLEE-LKKKLKEL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1090 NQQNSKIEdEQVLALQLQKKLKENQARIEELEEELEAERTARA--KVEKLRSDLSRELEEISER---LEEAGGATSVQIE 1164
Cdd:PRK03918 351 EKRLEELE-ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEleELEKAKEEIEEEISKITARigeLKKEIKELKKAIE 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1165 MNKKREAEFQKMRRDLEE---ATLQHEATAAAlrKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKlELDDVTSNMEQII 1241
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEehrKELLEEYTAEL--KRIEKELKEIEEKERKLRKELRELEKVLKKES-ELIKLKELAEQLK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1242 KAKANLEKVS-RTLEDQANEYR------VKLEEAQRSLNDFTTQRAKLQTENGELARQL----EEKEALISQLTRGKLSY 1310
Cdd:PRK03918 507 ELEEKLKKYNlEELEKKAEEYEklkeklIKLKGEIKSLKKELEKLEELKKKLAELEKKLdeleEELAELLKELEELGFES 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1311 TQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRV---LSKANSEVAQWRTKYETDaiqRTEE 1387
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETekrLEELRKELEELEKKYSEE---EYEE 663
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124376530 1388 LEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKI 1454
Cdd:PRK03918 664 LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKV 730
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1310-1907 |
1.41e-14 |
|
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: 79.78 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1310 YTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVaqwrtkyeTDAIQRT-EEL 1388
Cdd:pfam15921 83 YSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL--------RNQLQNTvHEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1389 EEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHrlqnEIEDLMVDVERSNAaaaaldkkqrnfDKILAEWKQKYEESQSE 1468
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ----EIRSILVDFEEASG------------KKIYEHDSMSTMHFRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1469 LESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQE-------------------EISDLTEQLGEGGKNVH--- 1526
Cdd:pfam15921 219 GSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIElllqqhqdrieqlisehevEITGLTEKASSARSQANsiq 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1527 -ELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQR-------VVDS 1598
Cdd:pfam15921 299 sQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQfsqesgnLDDQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1599 LQTSLdAETRSRNEVLRVKKKMEGDLNEME----IQLSHANRMAAEAQKQVKSLQSLLK----DTQIQLDDAVRANDDLK 1670
Cdd:pfam15921 379 LQKLL-ADLHKREKELSLEKEQNKRLWDRDtgnsITIDHLRRELDDRNMEVQRLEALLKamksECQGQMERQMAAIQGKN 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1671 ENIAIVERRNNLLQAELEELRAVVEQTErsrklAEQELIETSERVqlLHSQNTSLINQKKKME---SDLTQLQSEVEEAV 1747
Cdd:pfam15921 458 ESLEKVSSLTAQLESTKEMLRKVVEELT-----AKKMTLESSERT--VSDLTASLQEKERAIEatnAEITKLRSRVDLKL 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1748 QEC---RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTI------------------KDLQHRLDEAEQIA 1806
Cdd:pfam15921 531 QELqhlKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVgqhgrtagamqvekaqleKEINDRRLELQEFK 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1807 LKGGKKqlqklEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTE----EDKKNLLRLQDLVDKLQLKVKAYKR 1882
Cdd:pfam15921 611 ILKDKK-----DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDqllnEVKTSRNELNSLSEDYEVLKRNFRN 685
|
650 660
....*....|....*....|....*
gi 124376530 1883 QAEEAEEQANTNLSKFRKVQHELDE 1907
Cdd:pfam15921 686 KSEEMETTTNKLKMQLKSAQSELEQ 710
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1260-1842 |
1.83e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.31 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1260 EYRVKLEEAQRSLNDFttqRAKLQTENGELARQLEEKEA--LISQLTRGKLSYTQQMEDLKRQLEEEGKAKnalahalqS 1337
Cdd:PRK02224 166 EYRERASDARLGVERV---LSDQRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQAR--------E 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1338 ARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYET------DAIQRTEELEEAKKKLAQRLQDAEEAVEAVNA 1411
Cdd:PRK02224 235 TRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREElaeevrDLRERLEELEEERDDLLAEAGLDDADAEAVEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1412 KCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQkyeesqselessqkEARSLSTELfklknayE 1491
Cdd:PRK02224 315 RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE--------------EAAELESEL-------E 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1492 ESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIK 1571
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1572 -----------------AEIERKLAEKDEEMEQAKRNHQRVVDSLQTSLDA-ETRSRNEVLRVKKKMEGDL-NEMEIQLS 1632
Cdd:PRK02224 454 cpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDLvEAEDRIERLEERREDLEELiAERRETIE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1633 HANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERsRKLAEQELIETS 1712
Cdd:PRK02224 534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLR 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1713 ERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEA-VQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQT 1791
Cdd:PRK02224 613 EKREALAELNDERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 124376530 1792 IKDLQHRLDeaeqiALKGGKKQLQKLEARVRELE---GELEAE-QKRNAESVKGM 1842
Cdd:PRK02224 693 LEELRERRE-----ALENRVEALEALYDEAEELEsmyGDLRAElRQRNVETLERM 742
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1176-1873 |
1.94e-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: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1176 MRRDLEEATLQHEATAAAlrKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDvtsnmEQIIKAKANLEKvsrtLE 1255
Cdd:COG4913 240 AHEALEDAREQIELLEPI--RELAERYAAARERLAELEYLRAALRLWFAQRRLELLE-----AELEELRAELAR----LE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1256 DQANEYRVKLEEAQRSLNDFTTQRAKLQTEN-GELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHA 1334
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1335 LQSARHDCDLLREQYEEeteAKAELQRVLSKANSEVAQWRTkyETDAIQRT-----EELEEAKKKLAQRLQDAEEAVEAV 1409
Cdd:COG4913 389 AAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEA--EIASLERRksnipARLLALRDALAEALGLDEAELPFV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1410 nakCSSLE-KTKHRL-QNEIE--------DLMVDVERSNAAAAALDK---KQR-NFDKIlaewkqkyEESQSELESSQKE 1475
Cdd:COG4913 464 ---GELIEvRPEEERwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPRLD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1476 ARSLSTELFKLKNAYEESLEHL-------------ETFKRENKNLqeeisdlTEQ-LGEGGKNVHELEKVRKqlevekle 1541
Cdd:COG4913 533 PDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRAI-------TRAgQVKGNGTRHEKDDRRR-------- 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1542 LQSAL---EEAEASLEHEEGKILRAQLEFNQIKAEIErKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRnevlrvkk 1618
Cdd:COG4913 598 IRSRYvlgFDNRAKLAALEAELAELEEELAEAEERLE-ALEAELDALQERREALQRLAEYSWDEIDVASAER-------- 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1619 kmegDLNEMEIQLSHANrmaaEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTE 1698
Cdd:COG4913 669 ----EIAELEAELERLD----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1699 RSRKLAEQELIEtsERVQLLHSQNtSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKK--------------AITDA 1764
Cdd:COG4913 741 DLARLELRALLE--ERFAAALGDA-VERELRENLEERIDALRARLNRAEEELERAMRAFNRewpaetadldadleSLPEY 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1765 AMMAEELKkEQDTSAHLERMK----KNMEQTIKDLQHRLDEAEQIAlkggKKQLQKLEARVRELE-GE-----LEAEQKR 1834
Cdd:COG4913 818 LALLDRLE-EDGLPEYEERFKellnENSIEFVADLLSKLRRAIREI----KERIDPLNDSLKRIPfGPgrylrLEARPRP 892
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 124376530 1835 NAEsVKGMRKSERRIKELTYQTEED--KKNLLRLQDLVDKL 1873
Cdd:COG4913 893 DPE-VREFRQELRAVTSGASLFDEElsEARFAALKRLIERL 932
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
839-1376 |
3.21e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 839 KPLLKSAETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQlqvqAEQDNLNDAEERCDQLIKNKIQLE 918
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 919 AKVKEMNERLEdeeemnaELTAKKRKLED-------------ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMA 985
Cdd:PRK03918 259 EKIRELEERIE-------ELKKEIEELEEkvkelkelkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 986 GLDEIIAKLTKEKKALQEahqqALDDLQVEEDKVNSLSKSKVKLEQ--QVDDLEGSLEQEKKVRM--DLERAKRKLEGDL 1061
Cdd:PRK03918 332 ELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEAKAKKEEleRLKKRLTGLTPEKLEKEleELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1062 KLTQESIMDLENDKLQLE---EKLKKKEFDINQQNSKIEDEQVLAL---------QLQKKLKENQARIEELEEELEAERT 1129
Cdd:PRK03918 408 SKITARIGELKKEIKELKkaiEELKKAKGKCPVCGRELTEEHRKELleeytaelkRIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1130 ARAKVEKLRS--DLSRELEEISERLEEaggatsVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHA--DSVAEL 1205
Cdd:PRK03918 488 VLKKESELIKlkELAEQLKELEEKLKK------YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkKKLAEL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1206 GEQIDNLQRVKQKLEKEKSEFKL----ELDDVTSNMEQIIKAKANLEKVSRTLEDQANEyrvkLEEAQRSLNDFTTQRAK 1281
Cdd:PRK03918 562 EKKLDELEEELAELLKELEELGFesveELEERLKELEPFYNEYLELKDAEKELEREEKE----LKKLEEELDKAFEELAE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1282 LQTENGELARQLEEKEALISQLTRGKLSytQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQr 1361
Cdd:PRK03918 638 TEKRLEELRKELEELEKKYSEEEYEELR--EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE- 714
|
570
....*....|....*
gi 124376530 1362 VLSKANSEVAQWRTK 1376
Cdd:PRK03918 715 KLEKALERVEELREK 729
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
32-76 |
5.16e-14 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 67.84 E-value: 5.16e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 124376530 32 DIRTECFVPDDKEEFVKAKILSREGGKVIAETENGKTVTVKEDQV 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1293-1921 |
1.58e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1293 LEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAkNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQ 1372
Cdd:PTZ00121 1026 IEKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKA-EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAK 1104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1373 wrtKYETDAIQRTEELEEAKKKL--------AQRLQDAEEAVEAVNAKCSSLEKTKHRLQN----EIEDLMVDVERSNAA 1440
Cdd:PTZ00121 1105 ---KTETGKAEEARKAEEAKKKAedarkaeeARKAEDARKAEEARKAEDAKRVEIARKAEDarkaEEARKAEDAKKAEAA 1181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1441 AAALDKKQ-----RNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLT 1515
Cdd:PTZ00121 1182 RKAEEVRKaeelrKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1516 EQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQRV 1595
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA 1341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1596 VDSLQTSLDAETRSRNEVLRVKKKMEGDlnemEIQLSHANRMAAEAQKQVKSLQSLlKDTQIQLDDAVRANDDLKENIAi 1675
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAA----EKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAA- 1415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1676 VERRNNLLQAELEELRavveQTERSRKLAEQEliETSERVQLLHSQNTSLINQKKKMESdlTQLQSEVEEAVQECRNAEE 1755
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKK----KADEAKKKAEEA--KKADEAKKKAEEAKKAEEAKKKAEE--AKKADEAKKKAEEAKKADE 1487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1756 KAKKAiTDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELEGELEAEQKRN 1835
Cdd:PTZ00121 1488 AKKKA-EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK-ADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1836 AESVkgmRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIA 1915
Cdd:PTZ00121 1566 AEEA---KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642
|
....*.
gi 124376530 1916 ESQVNK 1921
Cdd:PTZ00121 1643 AEEKKK 1648
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
845-1583 |
1.65e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 76.55 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 845 AETEKEMATMKEEfgriketLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEM 924
Cdd:pfam02463 275 KEEEKEKKLQEEE-------LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 925 NERLEDEEEMNAELTAKKRKLEDECSELkkdiddleltLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEA 1004
Cdd:pfam02463 348 EIKREAEEEEEEELEKLQEKLEQLEEEL----------LAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1005 HQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESimdLENDKLQLEEKLKK 1084
Cdd:pfam02463 418 EDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV---KLQEQLELLLSRQK 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1085 KEFDINQQNSKIEDEQVLALQ--LQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQ 1162
Cdd:pfam02463 495 LEERSQKESKARSGLKVLLALikDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELP 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1163 IEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIK 1242
Cdd:pfam02463 575 LGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSL 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1243 AKANLEK--VSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEK-------EALISQLTRGKLSYTQQ 1313
Cdd:pfam02463 655 EEGLAEKseVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEelkklklEAEELLADRVQEAQDKI 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1314 MEDLKRQLEEEGKAKNALAHALQSARHDCDLLREqyEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKK 1393
Cdd:pfam02463 735 NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE--LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKE 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1394 KLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSN----AAAAALDKKQRNFDKILAEWKQKYEESQSEL 1469
Cdd:pfam02463 813 EAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELErleeEITKEELLQELLLKEEELEEQKLKDELESKE 892
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1470 ESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEA 1549
Cdd:pfam02463 893 EKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL 972
|
730 740 750
....*....|....*....|....*....|....
gi 124376530 1550 EASLEHEEGKILRAQLEFNQIKAEIERKLAEKDE 1583
Cdd:pfam02463 973 GKVNLMAIEEFEEKEERYNKDELEKERLEEEKKK 1006
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
845-1387 |
2.02e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.87 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 845 AETEKEMATMKEEFGRIKEtLEKSEARRKELEEKMVSLLQEKNDLQLQ----------VQAEQDNLNDAEERCDQLIKNK 914
Cdd:PRK03918 269 EELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRlsrleeeingIEERIKELEEKEERLEELKKKL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 915 IQLEAKVKEMNERLEDEEEMNAeLTAKKRKLEDECSELkkDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKL 994
Cdd:PRK03918 348 KELEKRLEELEERHELYEEAKA-KKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 995 TKEKKALQEAHQQ--ALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESimDLE 1072
Cdd:PRK03918 425 KKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK--ELA 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1073 NDKLQLEEKLKKKEFDinqqnskiedeqvlalQLQKKLKEnqarieeleeeleaERTARAKVEKLRSDLSRELEEIsERL 1152
Cdd:PRK03918 503 EQLKELEEKLKKYNLE----------------ELEKKAEE--------------YEKLKEKLIKLKGEIKSLKKEL-EKL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1153 EEAggatsvqiemnKKREAEFQKMRRDLEE--ATLQHEataaaLRKKHADSVAELGEQIDNLQRVKQK---LEKEKSEFK 1227
Cdd:PRK03918 552 EEL-----------KKKLAELEKKLDELEEelAELLKE-----LEELGFESVEELEERLKELEPFYNEyleLKDAEKELE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1228 LELDDVTSNMEQIIKAKANLEKVSRTLEdqanEYRVKLEEAQRSLNDftTQRAKLQTENGELARQLEEKEALISQLTRGK 1307
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLE----ELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRR 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1308 LSYTQQMEDLKRQLEEEGKAKNALaHALQSARHDCDLLREQY-----EEETEAKAELQRVLSKANSEVAQwrTKYETDAI 1382
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKKEL-EKLEKALERVEELREKVkkykaLLKERALSKVGEIASEIFEELTE--GKYSGVRV 766
|
....*
gi 124376530 1383 QRTEE 1387
Cdd:PRK03918 767 KAEEN 771
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1572-1931 |
4.69e-13 |
|
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: 74.72 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1572 AEIERKLAEKDEEMEQAKRNHQR---VVDSLQTSLDAETRSRNEVLRV------KKKMEG-----DLNEMEIQLSHANRM 1637
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERYqallkeKREYEGyellkEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1638 AAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENI-AIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQ 1716
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1717 LLHSQNTSLINQKKKMESDL-------TQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDtsaHLERMKKNME 1789
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIeeerkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE---KLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1790 QTIKDLQHRLDEAEQIALKGG--KKQLQKLEARVRELEGELEAEQKRnaesvkgMRKSERRIKELTYQTEEDKKNLLRLQ 1867
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELAdlNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQELYDLK 475
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124376530 1868 DLVDKLQlkvkaykrqaeeaeeqantnlSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGA 1931
Cdd:TIGR02169 476 EEYDRVE---------------------KELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1210-1929 |
5.95e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 74.62 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1210 DNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRsLNDFTTQRAKLQTENGEL 1289
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQ-KREAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1290 ARQLEEKEALISqltrgKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSE 1369
Cdd:TIGR00618 266 RARIEELRAQEA-----VLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1370 VAQWRTkyETDAIQRTEELEEAKKKLAQRLQDAEEAVEavnakcsslekTKHRLQNEIEDLMVDVERSNAAAAALDKKQR 1449
Cdd:TIGR00618 341 EEQRRL--LQTLHSQEIHIRDAHEVATSIREISCQQHT-----------LTQHIHTLQQQKTTLTQKLQSLCKELDILQR 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1450 NFDKILAEwKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGgKNVHELE 1529
Cdd:TIGR00618 408 EQATIDTR-TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK-EQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1530 KVRKQLEVEKLELQSALE-EAEASLEHEEGK-------------ILRAQLEFNQIKAEIERKLAEKDEEMEQAKR---NH 1592
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPcPLCGSCIHPNPArqdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQRASlkeQM 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1593 QRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEN 1672
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1673 IAIVERRNNLLQAELEE-LRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQsEVEEAVQECR 1751
Cdd:TIGR00618 646 TALHALQLTLTQERVREhALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIE-EYDREFNEIE 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1752 NAEEKAKKAItdaammaeelkkEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKggKKQLQKLEARVRELEGELEAE 1831
Cdd:TIGR00618 725 NASSSLGSDL------------AAREDALNQSLKELMHQARTVLKARTEAHFNNNEE--VTAALQTGAELSHLAAEIQFF 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1832 QKRNAESVKgmrkserRIKELTYQTEEDKKNllrlqdlvDKLQLKVKAYKRQAEEaeEQANTNLSKFRKVQHELDEAEER 1911
Cdd:TIGR00618 791 NRLREEDTH-------LLKTLEAEIGQEIPS--------DEDILNLQCETLVQEE--EQFLSRLEEKSATLGEITHQLLK 853
|
730
....*....|....*...
gi 124376530 1912 ADIAESQVNKLRAKSRDI 1929
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKI 871
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1015-1929 |
1.05e-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: 73.93 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1015 EEDKVNSLSKSKvKLEQQVDDLEG------SLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFD 1088
Cdd:TIGR00606 158 QEDSNWPLSEGK-ALKQKFDEIFSatryikALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1089 INQQNSKiEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGatsvQIEMNKK 1168
Cdd:TIGR00606 237 REIVKSY-ENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLN----DLYHNHQ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1169 REA-EFQKMRRDLEEATLQHEATAAALRKKHADSVAELGE-----QIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIK 1242
Cdd:TIGR00606 312 RTVrEKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRlqlqaDRHQEHIRARDSLIQSLATRLELDGFERGPFSERQ 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1243 AKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLT---RGKLSYTQQ----ME 1315
Cdd:TIGR00606 392 IKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQeelKFVIKELQQlegsSD 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1316 DLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEetEAKAELQRVLSKANSEVAQWRTKYETdaiqRTEELEEAKKKL 1395
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEKNSLTETLKKEVKSLQ--NEKADLDRKLRKLDQEMEQLNHHTTT----RTQMEMLTKDKM 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1396 aqrlqDAEEAVEAVNAKCSS--------------LEKTKHRLQNEI---EDLMVDVERSNAAAAALDKKQRNFDKILAEW 1458
Cdd:TIGR00606 546 -----DKDEQIRKIKSRHSDeltsllgyfpnkkqLEDWLHSKSKEInqtRDRLAKLNKELASLEQNKNHINNELESKEEQ 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1459 KQKYEES-------------QSELESSQKEARSLSTELFKLKNAYEESLEHLET------------FKREnKNLQEEISD 1513
Cdd:TIGR00606 621 LSSYEDKlfdvcgsqdeesdLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDenqsccpvcqrvFQTE-AELQEFISD 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1514 LTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLA--EKDEEMEQAKRN 1591
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNdiEEQETLLGTIMP 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1592 HQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEiqlshanrmAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKE 1671
Cdd:TIGR00606 780 EEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQ---------GSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1672 NIAIVERRNNLLQAELEELRA----VVEQTERSRKLAEQeLIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAV 1747
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKSeklqIGTNLQRRQQFEEQ-LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELI 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1748 QecrNAEEKAKKAITDAAMMAEELKK--------EQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEA 1819
Cdd:TIGR00606 930 S---SKETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDDYLKQKETELNTVNAQLEECEK--------HQEKINE 998
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1820 RVRELEGELEAE--QKRNAESVKGMRKSERRIKEL-----TYQTEEDKKNLLRLQDLVDKLQLKVKAYKR-------QAE 1885
Cdd:TIGR00606 999 DMRLMRQDIDTQkiQERWLQDNLTLRKRENELKEVeeelkQHLKEMGQMQVLQMKQEHQKLEENIDLIKRnhvlalgRQK 1078
|
970 980 990 1000
....*....|....*....|....*....|....*....|....
gi 124376530 1886 EAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1929
Cdd:TIGR00606 1079 GYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDI 1122
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
848-1602 |
1.06e-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: 73.93 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 848 EKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQ--VQAEQDNLNDAEERCDQL----------IKNKI 915
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQadRHQEHIRARDSLIQSLATrleldgfergPFSER 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 916 QLEAKVKEMNERLEDEEEMNAELTA--------KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL 987
Cdd:TIGR00606 391 QIKNFHTLVIERQEDEAKTAAQLCAdlqskerlKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSS 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 988 DEIIAK---LTKEKKALQEAHQQALDDLQVEEDKV-----NSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEG 1059
Cdd:TIGR00606 471 DRILELdqeLRKAERELSKAEKNSLTETLKKEVKSlqnekADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQ 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1060 DLKLTQESIMDLEN------DKLQLEEKLKKKEFDINQQNSKIED---EQVLALQLQKKLKENQARIEELEEELEAERTA 1130
Cdd:TIGR00606 551 IRKIKSRHSDELTSllgyfpNKKQLEDWLHSKSKEINQTRDRLAKlnkELASLEQNKNHINNELESKEEQLSSYEDKLFD 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1131 RAKVEKLRSDLSR---ELEEISERLEEAGGATSVQ-----------------IEMNKKREAEFQKMRRDLEEATL----Q 1186
Cdd:TIGR00606 631 VCGSQDEESDLERlkeEIEKSSKQRAMLAGATAVYsqfitqltdenqsccpvCQRVFQTEAELQEFISDLQSKLRlapdK 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1187 HEATAAALRKKHADSVAELGeQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIikaKANLEKVSRTLEdqanEYRVKLE 1266
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLG-LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL---KNDIEEQETLLG----TIMPEEE 782
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1267 EAQRSLNDFTTQRaklqtengELARQLEEKEALISQLTRgklsyTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLR 1346
Cdd:TIGR00606 783 SAKVCLTDVTIME--------RFQMELKDVERKIAQQAA-----KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNR 849
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1347 EQYEEETEAKAELQRVLSKANSEVAQWRTkyetdAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNE 1426
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKTNELKSEKLQIGT-----NLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1427 IEDLMVDVERSNAAAA-ALDKKQRNFDKILAEWK--QKYEESQSELESSQKEarslsTELFKLKNAYEESLEHLETFKRE 1503
Cdd:TIGR00606 925 KEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKdiENKIQDGKDDYLKQKE-----TELNTVNAQLEECEKHQEKINED 999
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1504 NKNLQEEI-------SDLTEQLGEGGKN--VHELEKVRKQLEVEKLELQ--------SALEEAEASLEHEEGKILRAQLE 1566
Cdd:TIGR00606 1000 MRLMRQDIdtqkiqeRWLQDNLTLRKREneLKEVEEELKQHLKEMGQMQvlqmkqehQKLEENIDLIKRNHVLALGRQKG 1079
|
810 820 830
....*....|....*....|....*....|....*.
gi 124376530 1567 FNQIKAEIERKLAEKdeEMEQAKRNHQRVVDSLQTS 1602
Cdd:TIGR00606 1080 YEKEIKHFKKELREP--QFRDAEEKYREMMIVMRTT 1113
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1383-1934 |
1.79e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1383 QRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKhrlqNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEwKQKY 1462
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEE-LKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1463 EESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEveklEL 1542
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK----EL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1543 QSALEEAEASLE-HEEGKILRAQLEfnQIKAEIE----RKLAEKDEEMEQAKRNHQRVVDSLQT---SLDAETRSRNEVL 1614
Cdd:PRK03918 351 EKRLEELEERHElYEEAKAKKEELE--RLKKRLTgltpEKLEKELEELEKAKEEIEEEISKITArigELKKEIKELKKAI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1615 RVKKKMEGD--LNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDavranddlkeniaiverrnnlLQAELEELRA 1692
Cdd:PRK03918 429 EELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERK---------------------LRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1693 VVEQTERSRKLAEqelietservqllhsqntsLINQKKKMESDLTQLQSE-VEEAVQECRNAEEKAKKAITDAAMMAEEL 1771
Cdd:PRK03918 488 VLKKESELIKLKE-------------------LAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1772 KKEQDtsahLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELEgELEAEQKRNAESVKGMRKSERRIKE 1851
Cdd:PRK03918 549 EKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKELEREEKELKK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1852 LTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQ--AEEAEEQANTNLSKFRK---VQHELDEAEERADIAESQVNKLRAKS 1926
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELREEYLELSRElagLRAELEELEKRREEIKKTLEKLKEEL 703
|
....*...
gi 124376530 1927 RDIGAKQK 1934
Cdd:PRK03918 704 EEREKAKK 711
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1055-1802 |
2.08e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 72.36 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1055 RKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIeeleeeleaertarakv 1134
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKI----------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1135 EKLRSDLSRELEEISERLEEaggatsvqieMNKKrEAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQR 1214
Cdd:TIGR04523 99 NKLNSDLSKINSEIKNDKEQ----------KNKL-EVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1215 VKQKLEKEKSEFKLELDDVTSNMEQI-------------IKAK-----------ANLEKVSRTLEDQANEYRVKLEEAQR 1270
Cdd:TIGR04523 167 QKEELENELNLLEKEKLNIQKNIDKIknkllklelllsnLKKKiqknkslesqiSELKKQNNQLKDNIEKKQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1271 SLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNA-----LAHALQSARHDCDLL 1345
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1346 REQYEEETEAKAELQRVLSKANSEvaqwRTKYETDAIQRTEELEEAKKK------------------------LAQRLQD 1401
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKE----LTNSESENSEKQRELEEKQNEieklkkenqsykqeiknlesqindLESKIQN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1402 AEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLST 1481
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1482 ELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEaeasleheegkil 1561
Cdd:TIGR04523 483 NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK------------- 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1562 raqLEFNQIKAEIERKLAEKDEEMEQAKRNhqrvvdslQTSLDAETRSRNEVLRVKKKMEGDLNemeiqlshanrmaaea 1641
Cdd:TIGR04523 550 ---DDFELKKENLEKEIDEKNKEIEELKQT--------QKSLKKKQEEKQELIDQKEKEKKDLI---------------- 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1642 qKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQElietservqllhsq 1721
Cdd:TIGR04523 603 -KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKK-------------- 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1722 ntslINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDE 1801
Cdd:TIGR04523 668 ----IKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKFDD 743
|
.
gi 124376530 1802 A 1802
Cdd:TIGR04523 744 A 744
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
849-1772 |
2.11e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 72.77 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 849 KEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKnDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERL 928
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 929 EDEEEMNAELTAKKRKLEDECSELKKDIDdleltlakvekekHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAH--- 1005
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKtel 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1006 --QQALDDLQVEEDKVNSLSKSKVKLEQQ----VDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLE 1079
Cdd:TIGR00606 346 lvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1080 EKLKKKEFDINQQNSKIEDEQVlalqlqkKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggat 1159
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKE-------ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNS---- 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1160 svQIEMNKKREAEFQKMRRDLEEaTLQHEATAAALRKKHADSVaelgEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQ 1239
Cdd:TIGR00606 495 --LTETLKKEVKSLQNEKADLDR-KLRKLDQEMEQLNHHTTTR----TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLG 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1240 IIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLndfttqrAKLQTENGELARQLEEKEALISQLTR------GKLSYTQQ 1313
Cdd:TIGR00606 568 YFPNKKQLEDWLHSKSKEINQTRDRLAKLNKEL-------ASLEQNKNHINNELESKEEQLSSYEDklfdvcGSQDEESD 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1314 MEDLKRQLEEEGKAKNALAHAlqSARHDCDLLREQYEEET---------EAKAELQRVLSKANSEVAQWRTKYEtdaiQR 1384
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGA--TAVYSQFITQLTDENQSccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLK----ST 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1385 TEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQN---EIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQK 1461
Cdd:TIGR00606 715 ESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKvnrDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIM 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1462 YEESQSELESSQKEARSLS-TELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKL 1540
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAkLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKL 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1541 ELQSALEEAEASLEHEEGKILRAQLEFNQIK---------AEIERKLAEKDEEM----EQAKRNHQRVVDSLQTSLDAET 1607
Cdd:TIGR00606 875 QIGTNLQRRQQFEEQLVELSTEVQSLIREIKdakeqdsplETFLEKDQQEKEELisskETSNKKAQDKVNDIKEKVKNIH 954
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1608 RSRNEVLR-VKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAE 1686
Cdd:TIGR00606 955 GYMKDIENkIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVE 1034
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1687 LEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEavQECRNAEEKAKKAITDAAM 1766
Cdd:TIGR00606 1035 EELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE--PQFRDAEEKYREMMIVMRT 1112
|
....*.
gi 124376530 1767 MAEELK 1772
Cdd:TIGR00606 1113 TELVNK 1118
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
854-1520 |
7.18e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 70.91 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 854 MKEEFGRIKETLEKSEARRKELEEKMVSLlqeKNDLQLQVQAEQDNLNDAEercdqliKNKIQLEAKVKEMNERLED-EE 932
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDL---NNNIEKMILAFEELRVQAE-------NARLEMHFKLKEDHEKIQHlEE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 933 EMNAELTAKKRK---LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQAL 1009
Cdd:pfam05483 230 EYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSM 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1010 -------DDLQVEEDKVNSLSKSKvklEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKL 1082
Cdd:pfam05483 310 stqkaleEDLQIATKTICQLTEEK---EAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMEL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1083 KKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISErLEEAGGATSVQ 1162
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHD-LEIQLTAIKTS 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1163 IEMNKKreaEFQKMRRDLEEATLQHeataaalrkkhadsvAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIK 1242
Cdd:pfam05483 466 EEHYLK---EVEDLKTELEKEKLKN---------------IELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKK 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1243 AKANLEKVSRTLEDQANEYRVKLEEAQRslnDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLE 1322
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1323 EEGKAknalahaLQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDA 1402
Cdd:pfam05483 605 NKNKN-------IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEV 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1403 EEAVEAVNAKCSSLEKTKHRLQNEIEDLMvdversnaaaAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTE 1482
Cdd:pfam05483 678 EKAKAIADEAVKLQKEIDKRCQHKIAEMV----------ALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIE 747
|
650 660 670
....*....|....*....|....*....|....*...
gi 124376530 1483 LFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGE 1520
Cdd:pfam05483 748 LSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1489-1926 |
7.97e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.84 E-value: 7.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1489 AYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEheegKILRAQLEFN 1568
Cdd:PRK02224 245 EHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAE----AVEARREELE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1569 QIKAEIERKLAEKDEEMEQAKRNHQRVVDSLqtsldAETRSRNEVLRVK-KKMEGDLNEMEIQLSHANRMAAEAQKQVKS 1647
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDA-----DDLEERAEELREEaAELESELEEAREAVEDRREEIEELEEEIEE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1648 LQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSR---KLAE--QElIETSERVQLLHSQN 1722
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagKCPEcgQP-VEGSPHVETIEEDR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1723 tsliNQKKKMESDLTQLQSEVEEAvqecrnaEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEA 1802
Cdd:PRK02224 475 ----ERVEELEAELEDLEEEVEEV-------EERLERA--------EDLVEAEDRIERLEERREDLEELIAERRETIEEK 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1803 EQialkggkkQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKL--------Q 1874
Cdd:PRK02224 536 RE--------RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaiadaedE 607
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 124376530 1875 LKVKAYKRQA-EEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKS 1926
Cdd:PRK02224 608 IERLREKREAlAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
837-1329 |
1.32e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.17 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 837 KIKPLLKSAETEKEMATMKEEfgrikETLEKSEARRKELEEKmvsllqeKNDLQLQVQAEQDNlNDAEERCDQLIKNKIQ 916
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKE-----EAKKKADAAKKKAEEK-------KKADEAKKKAEEDK-KKADELKKAAAAKKKA 1420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 917 LEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKKdiddLELTLAKVEKEKHATENKVKnlTEEMAGLDEIIAKLTK 996
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK----AEEAKKKAEEAKKADEAKKK--AEEAKKADEAKKKAEE 1494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 997 EKKALQEAHQQALDDLQVEEDKvnslskskvKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLEnDKL 1076
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAK---------KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE-EKK 1564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1077 QLEEKlKKKEFDINQQNSKIEdeqvLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAg 1156
Cdd:PTZ00121 1565 KAEEA-KKAEEDKNMALRKAE----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL- 1638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1157 gatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEqidnlQRVKQKLEKEKSEFKLELDDVTSN 1236
Cdd:PTZ00121 1639 ----------KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE-----AKKAEEDEKKAAEALKKEAEEAKK 1703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1237 MEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGE------LARQLEEKEALISQLTRGKLSY 1310
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEkkkiahLKKEEEKKAEEIRKEKEAVIEE 1783
|
490
....*....|....*....
gi 124376530 1311 TQQMEDLKRQLEEEGKAKN 1329
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIKD 1802
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
848-1541 |
1.41e-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: 70.00 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 848 EKEMATMKEEFGRIKETLEKSEARRKELEEKMvSLLQEKNDLQLQVQ---AEQDNLNDAEERCDQLIKnKIQLEAKVKEM 924
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYLTQKREAQEEQL-KKQQLLKQLRARIEelrAQEAVLEETQERINRARK-AAPLAAHIKAV 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 925 NERLEDEEEMNAELTAKKRKLEDE---CSELKKDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDEIiakLTKEKKAL 1001
Cdd:TIGR00618 303 TQIEQQAQRIHTELQSKMRSRAKLlmkRAAHVKQQSSIE-EQRRLLQTLHSQEIHIRDAHEVATSIREI---SCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1002 QEAHQQAlDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEgdLKLTQESIMDLENDKLQLEEK 1081
Cdd:TIGR00618 379 QHIHTLQ-QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE--LQQRYAELCAAAITCTAQCEK 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1082 LKKKEFDINQQNSKIEDEQvlaLQLQKKLKENQARIeeleeeleaeRTARAKVEKLRSDLSRELEEiSERLEEAGGATSV 1161
Cdd:TIGR00618 456 LEKIHLQESAQSLKEREQQ---LQTKEQIHLQETRK----------KAVVLARLLELQEEPCPLCG-SCIHPNPARQDID 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1162 QIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQII 1241
Cdd:TIGR00618 522 NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQ----RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1242 KAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQL 1321
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLAS 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1322 EEegkaknALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETdaiqRTEELEEAKKKLAQRLQD 1401
Cdd:TIGR00618 678 RQ------LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSS----LGSDLAAREDALNQSLKE 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1402 AEEavEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNaAAAALDKKQRNFDKILAEWKQKyEESQSELESSQKEARSLST 1481
Cdd:TIGR00618 748 LMH--QARTVLKARTEAHFNNNEEVTAALQTGAELSH-LAAEIQFFNRLREEDTHLLKTL-EAEIGQEIPSDEDILNLQC 823
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124376530 1482 ELFklknayEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQL--EVEKLE 1541
Cdd:TIGR00618 824 ETL------VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIiqLSDKLN 879
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
882-1702 |
1.45e-11 |
|
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: 69.87 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 882 LLQEKNDLQLQVQAEQDNLNDAEERC---DQLIKNKIQLEAK---VKEMNERLEDEEEMNAEltaKKRKLEDECSELKKD 955
Cdd:pfam12128 153 TLLGRERVELRSLARQFALCDSESPLrhiDKIAKAMHSKEGKfrdVKSMIVAILEDDGVVPP---KSRLNRQQVEHWIRD 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 956 IDdlelTLAKVEKEKHatenKVKNLTEEMAGLDEIIAKLTKEKKALQEaHQQALDDLQVEEDKvnslskSKVKLEQQVDD 1035
Cdd:pfam12128 230 IQ----AIAGIMKIRP----EFTKLQQEFNTLESAELRLSHLHFGYKS-DETLIASRQEERQE------TSAELNQLLRT 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1036 LEgslEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEeklkkkefDINQQNSKIEDEQvlALQLQKKLKENQA 1115
Cdd:pfam12128 295 LD---DQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFL--------DADIETAAADQEQ--LPSWQSELENLEE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1116 RIEELEEELeaeRTARAKVEKLRSDLSRELEEISERLeeaggatsvqiemNKKREAEFQKMRRDLEEATLQHEATAAALR 1195
Cdd:pfam12128 362 RLKALTGKH---QDVTAKYNRRRSKIKEQNNRDIAGI-------------KDKLAKIREARDRQLAVAEDDLQALESELR 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1196 KKHADSVAELGEQidnlqrvKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEdqaneyrvKLEEAQRSLNDF 1275
Cdd:pfam12128 426 EQLEAGKLEFNEE-------EYRLKSRLGELKLRLNQATATPELLLQLENFDERIERARE--------EQEAANAEVERL 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1276 TTQRAKLQTENGELARQLEEKEALISQLtRGKLSYTQQMED------LKRQLEEEGKAKNALAHALQSAR-HDCDLLREQ 1348
Cdd:pfam12128 491 QSELRQARKRRDQASEALRQASRRLEER-QSALDELELQLFpqagtlLHFLRKEAPDWEQSIGKVISPELlHRTDLDPEV 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1349 YEEETEAKAELQRV-LSKANSEVAQWrtkyetdaIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEI 1427
Cdd:pfam12128 570 WDGSVGGELNLYGVkLDLKRIDVPEW--------AASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREE 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1428 EDlmvdversnaAAAAL----DKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRE 1503
Cdd:pfam12128 642 TF----------ARTALknarLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKRE 711
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1504 NKN-----LQEEISDLTEQLGeggknvhelekvrkQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKL 1578
Cdd:pfam12128 712 ARTekqayWQVVEGALDAQLA--------------LLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREI 777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1579 AEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLShanRMAAEAQKQVKSLQSLLK---DT 1655
Cdd:pfam12128 778 RTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLA---RLIADTKLRRAKLEMERKaseKQ 854
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 124376530 1656 QIQLDDAVRANDDLKENIAIVERRNNLLQAELE--ELRAVVEQTERSRK 1702
Cdd:pfam12128 855 QVRLSENLRGLRCEMSKLATLKEDANSEQAQGSigERLAQLEDLKLKRD 903
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
836-1248 |
1.54e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 836 FKIKPLLKSAETEKEMATMKEEFGRIKET---LEKSEARRKELEEKMVSLLQEKNDLQLQVQ------AEQDNLNDAEER 906
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERikeLEEKEERLEELKKKLKELEKRLEELEERHElyeeakAKKEELERLKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 907 CDQLIKNKIqlEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLE-----LTLAKVEKEKHATEN------ 975
Cdd:PRK03918 381 LTGLTPEKL--EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkCPVCGRELTEEHRKElleeyt 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 976 -KVKNLTEEMAGLDEIIAKLTKEKKALQEA---------HQQALDDLQVEEDKVNSLSKSkvKLEQQVDDLEGSLEQEKK 1045
Cdd:PRK03918 459 aELKRIEKELKEIEEKERKLRKELRELEKVlkkeselikLKELAEQLKELEEKLKKYNLE--ELEKKAEEYEKLKEKLIK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1046 VRMDLERAKRKLegdlkltqESIMDLENDKLQLEEKLKKKEFDINQQNSKI-----EDEQVLALQLQK---------KLK 1111
Cdd:PRK03918 537 LKGEIKSLKKEL--------EKLEELKKKLAELEKKLDELEEELAELLKELeelgfESVEELEERLKElepfyneylELK 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1112 ENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVqiEMNKKREAEFQKMRRDLEEATLQHEaTA 1191
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELE-EL 685
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 124376530 1192 AALRKKHADSVAELGEQIDNLQRVKQKLEKekseFKLELDDVTSNMEQIIKAKANLE 1248
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELREKVKKYKALLK 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1475-1920 |
2.61e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1475 EARSLSTELFKLKNAYEESLEhletfKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEasLE 1554
Cdd:COG4913 226 AADALVEHFDDLERAHEALED-----AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1555 HEEGKILRAQLEFNQIKAEIERkLAEKDEEMEQAKRNHQ-RVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSH 1633
Cdd:COG4913 299 ELRAELARLEAELERLEARLDA-LREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1634 A----NRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEN-------IAIVERRNNLLQAELEELRAVVEqteRSRK 1702
Cdd:COG4913 378 SaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRElreleaeIASLERRKSNIPARLLALRDALA---EALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1703 LAEQ------ELIETS----------ERVqlLHSQNTSL-------------INQKK----------------------- 1730
Cdd:COG4913 455 LDEAelpfvgELIEVRpeeerwrgaiERV--LGGFALTLlvppehyaaalrwVNRLHlrgrlvyervrtglpdperprld 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1731 ------KMESDLTQLQSEVEEAVQE------CRNAEE--KAKKAITDAAMMAEELKK-EQDTSAHLER---MKKNMEQTI 1792
Cdd:COG4913 533 pdslagKLDFKPHPFRAWLEAELGRrfdyvcVDSPEElrRHPRAITRAGQVKGNGTRhEKDDRRRIRSryvLGFDNRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1793 KDLQHRLDEAEQiALKGGKKQLQKLEARVRELEGELEAEQK--RNAESVKGMRKSERRIKELtyqtEEDKKNLLRLQDLV 1870
Cdd:COG4913 613 AALEAELAELEE-ELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL----EAELERLDASSDDL 687
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 124376530 1871 DKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVN 1920
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
942-1576 |
2.96e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 942 KRKLEDECSELKKDIDDLELTLAKVEKEKHATE--NKVKNLTEEMAGLDEIIAKLTKEKKALQ-EAHQQALDDLQVEEDK 1018
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1019 vnsLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDlkltqeSIMDLENDKLQLEEKLKKKEFDINQQNSKIED 1098
Cdd:COG4913 300 ---LRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1099 EQVLALQLQKKLKENQARIEELEEELEAER----TARAKVEKLRSDLSRELEEISERLEEaggatsvqIEMNKKR-EAEF 1173
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELealeEALAEAEAALRDLRRELRELEAEIAS--------LERRKSNiPARL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1174 QKMRRDLEEATLQHEA-------------------TAA--ALR---------KKHADSVAELGEQID-----NLQRVKQK 1218
Cdd:COG4913 443 LALRDALAEALGLDEAelpfvgelievrpeeerwrGAIerVLGgfaltllvpPEHYAAALRWVNRLHlrgrlVYERVRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1219 LEKEKSEF--------KLELDD--VTSNMEQIIKAKANLEKVsRTLEDQANEYR-------VKLEEAQRSLNDFTTQRAK 1281
Cdd:COG4913 523 LPDPERPRldpdslagKLDFKPhpFRAWLEAELGRRFDYVCV-DSPEELRRHPRaitragqVKGNGTRHEKDDRRRIRSR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1282 LQT--ENgelARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQyEEETEAKAEL 1359
Cdd:COG4913 602 YVLgfDN---RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-REIAELEAEL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1360 QRvLSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVErsna 1439
Cdd:COG4913 678 ER-LDASSDDL---------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE---- 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1440 AAAALDKKQRNFDkiLAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKnlqeeisDLTEQLG 1519
Cdd:COG4913 738 AAEDLARLELRAL--LEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWP-------AETADLD 808
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1520 EGGKNVHELEKVRKQLEVEKL-ELQSALEEAEASLEHEEGKILRAQL--EFNQIKAEIER 1576
Cdd:COG4913 809 ADLESLPEYLALLDRLEEDGLpEYEERFKELLNENSIEFVADLLSKLrrAIREIKERIDP 868
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1283-1921 |
4.39e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.63 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1283 QTENGELARQLEEKEALISQLTRGKLSYTQQMEDLkRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQR- 1361
Cdd:PTZ00121 1105 KTETGKAEEARKAEEAKKKAEDARKAEEARKAEDA-RKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARk 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1362 -VLSKANSEVAQWRTKYETDAIQRTEE---LEEAKK----KLAQRLQDAEEA-VEAVNAKCSSLEKTKHRLQNEIEDLMV 1432
Cdd:PTZ00121 1184 aEEVRKAEELRKAEDARKAEAARKAEEerkAEEARKaedaKKAEAVKKAEEAkKDAEEAKKAEEERNNEEIRKFEEARMA 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1433 DVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEIS 1512
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK 1343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1513 DLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKI----LRAQLEFNQIKAEIERKLAEKDEEMEQA 1588
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkadeAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1589 KRNHQRVVDSLQTSLDAETRSRNEVLRvKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLlKDTQIQLDDAVRANDD 1668
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADE 1501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1669 LKENIAIVERRNNLLQAE----LEELRAVvEQTERSRKLAEQELIETSERV----QLLHSQNTSLINQKKKMESDLTQLQ 1740
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEeakkADEAKKA-EEAKKADEAKKAEEKKKADELkkaeELKKAEEKKKAEEAKKAEEDKNMAL 1580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1741 SEVEEAVQ-ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlkggkkqlqklea 1819
Cdd:PTZ00121 1581 RKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK------------- 1647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1820 rvrelegelEAEQKRNAESVKGMRKSERRIKEltyqtEEDKknllrlqdlvdklqlkvkaykRQAEEAeeqantnlskfR 1899
Cdd:PTZ00121 1648 ---------KAEELKKAEEENKIKAAEEAKKA-----EEDK---------------------KKAEEA-----------K 1681
|
650 660
....*....|....*....|..
gi 124376530 1900 KVQHELDEAEERADIAESQVNK 1921
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKK 1703
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
843-1429 |
7.60e-11 |
|
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: 67.51 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 843 KSAETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVK 922
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 923 EMNERLEDEEEMN--------------AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLD 988
Cdd:pfam01576 535 EDAGTLEALEEGKkrlqrelealtqqlEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEK 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 989 EIIAKLT------------KEKKALQEAHqqALDDLQveeDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRK 1056
Cdd:pfam01576 615 AISARYAeerdraeaeareKETRALSLAR--ALEEAL---EAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRA 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1057 LEGDLKLTQESIMDLEnDKLQLEEKLKKKeFDINQQNSKIEDEQVLAL---QLQKKLKENQARIEELEEELEAERTARAK 1133
Cdd:pfam01576 690 LEQQVEEMKTQLEELE-DELQATEDAKLR-LEVNMQALKAQFERDLQArdeQGEEKRRQLVKQVRELEAELEDERKQRAQ 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1134 VEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHE---ATAAALRKKHADSVAE---LGE 1207
Cdd:pfam01576 768 AVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDeilAQSKESEKKLKNLEAEllqLQE 847
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1208 QIDNLQRVKQKLEKEKSEFKLELDDVTSNmeqiikaKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENG 1287
Cdd:pfam01576 848 DLAASERARRQAQQERDELADEIASGASG-------KSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVE 920
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1288 ELARQLEEKEALISQLTRGKLSYTQQMEDLKRQL-EEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKA 1366
Cdd:pfam01576 921 QLTTELAAERSTSQKSESARQQLERQNKELKAKLqEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRT 1000
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124376530 1367 NSEVAQWRTKYETD---AIQRTEELEEAK---KKLAQRLQDAEEAVEAVNAkcsslekTKHRLQNEIED 1429
Cdd:pfam01576 1001 EKKLKEVLLQVEDErrhADQYKDQAEKGNsrmKQLKRQLEEAEEEASRANA-------ARRKLQRELDD 1062
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1490-1830 |
7.80e-11 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 67.02 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1490 YEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQsaleEAEASLEHEEGKILRAQLEFNQ 1569
Cdd:pfam05622 140 YKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1570 IKA-------EIERKLAEKD---EEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAA 1639
Cdd:pfam05622 216 LEEklealqkEKERLIIERDtlrETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1640 EAQKQvkSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRavveqtersRKLAEQElietservqllh 1719
Cdd:pfam05622 296 LGQEG--SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQ---------KALQEQG------------ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1720 SQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---T 1791
Cdd:pfam05622 353 SKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksV 432
|
330 340 350
....*....|....*....|....*....|....*....
gi 124376530 1792 IKDLQHRLDEAEQIALKGGKKQLQKLEARVRELEGELEA 1830
Cdd:pfam05622 433 IKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEK 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1617-1935 |
8.28e-11 |
|
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: 67.39 E-value: 8.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1617 KKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQsllkdtqIQLDDAVRANDdLKENIAIVERRnnLLQAELEELRAVVEQ 1696
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLE-------RQAEKAERYKE-LKAELRELELA--LLVLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1697 TERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQD 1776
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1777 TSAHLERMKKNMEQTIKDLQHRLDEAE------QIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIK 1850
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKeeleslEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1851 ELTYQTEEDKKNLLRLQ----DLVDKLQ-LKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1925
Cdd:TIGR02168 404 RLEARLERLEDRRERLQqeieELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
330
....*....|
gi 124376530 1926 SRDIGAKQKM 1935
Cdd:TIGR02168 484 LAQLQARLDS 493
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1670-1934 |
1.07e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1670 KENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQ-----------ELIETSERVQLLHSQNTSLINQKKKMESDLTQ 1738
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERQAEKAERYRELKEElkeleaellllKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1739 LQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLE 1818
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE-ELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1819 ARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKF 1898
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270
....*....|....*....|....*....|....*.
gi 124376530 1899 RKVQHELDEAEERADIAESQVNKLRAKSRDIGAKQK 1934
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
846-1112 |
1.08e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.97 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 846 ETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMN 925
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 926 ERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEah 1005
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE-- 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1006 qqalddlqveedKVNSLSKSKVKLEQQVDDLEGSLEQEK--KVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLK 1083
Cdd:TIGR04523 525 ------------KIEKLESEKKEKESKISDLEDELNKDDfeLKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
250 260
....*....|....*....|....*....
gi 124376530 1084 KKEFDINQQNSKIEDEQVLALQLQKKLKE 1112
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1455-1939 |
1.79e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1455 LAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYE-ESLEHLETFKRENKNLQEEISDLTE-----QLGEGGKNVHEL 1528
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKaEDARKAEEARKAEDAKRVEIARKAEdarkaEEARKAEDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1529 EKVRKQLEVEKLELQSALEEA----EASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQTSLD 1604
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDArkaeAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1605 AETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQK--QVKSLQSLLKDTQiqlddAVRANDDLKENIAIVERRNNL 1682
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKaeEKKKADEAKKKAE-----EAKKADEAKKKAEEAKKKADA 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1683 LQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSlinQKKKMEsdltqlqsEVEEAVQECRNAEEKAKKAIT 1762
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE---AKKKAD--------AAKKKAEEKKKADEAKKKAEE 1402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1763 DAAMmAEELKKEQDTSAHLERMKKNMEQTIKdlqhrLDEAEQialkggkkqlqKLEARVRELEGELEAEQKRNAESVKGM 1842
Cdd:PTZ00121 1403 DKKK-ADELKKAAAAKKKADEAKKKAEEKKK-----ADEAKK-----------KAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1843 RKSERRIKELTYQTEEDKKnllrlqdlVDKLQLKVKAYKRQAEEAE--EQANTNLSKFRKVQH-----ELDEAEERADIA 1915
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKK--------ADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKAEEakkadEAKKAEEAKKAD 1537
|
490 500
....*....|....*....|....
gi 124376530 1916 ESQVNKLRAKSRDIGAKQKMHDEE 1939
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAE 1561
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1479-1925 |
2.48e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.81 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1479 LSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEA---EASLEH 1555
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIknkLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1556 ---------EEGKILRAQL-----EFNQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVK---- 1617
Cdd:TIGR04523 202 llsnlkkkiQKNKSLESQIselkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEqnnk 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1618 --KKMEGDLNEMEIQLSHANRMAA-----EAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEEL 1690
Cdd:TIGR04523 282 kiKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1691 RAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEE 1770
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1771 LKKEQDTSAHLERMKKNMEQTIKDLQHRLD-------------EAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAE 1837
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqnlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1838 SVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQL-KVKAYKRQAEEAEEQANTNLSKfrkvqhELDEAEERADIAE 1916
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLeKEIDEKNKEIEELKQTQKSLKK------KQEEKQELIDQKE 595
|
....*....
gi 124376530 1917 SQVNKLRAK 1925
Cdd:TIGR04523 596 KEKKDLIKE 604
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1049-1671 |
2.95e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1049 DLERAKRKLEgdlkLTQESIMDLEnDKLQLEEKLKKKEFDINQQnsKIEDEQVLALQLQKKLKENQARIEELEEELEAER 1128
Cdd:COG4913 236 DLERAHEALE----DAREQIELLE-PIRELAERYAAARERLAEL--EYLRAALRLWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1129 TARAKVEKLRSDLSRELEEISERLEEAGGAtsvQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQ 1208
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNGGD---RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1209 IDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNdfttQRAKLQTEN-- 1286
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA----EALGLDEAElp 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1287 --GEL--ARQLEEK---------------------------EALISQLTRGKLSYtQQMEDLKRQLEEEGKAKNALAHAL 1335
Cdd:COG4913 462 fvGELieVRPEEERwrgaiervlggfaltllvppehyaaalRWVNRLHLRGRLVY-ERVRTGLPDPERPRLDPDSLAGKL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1336 QSARHDC-DLLREQYEEET-----EAKAELQRV--------LSKANSEVAQ------WRTKYET--DAIQRTEELEEAKK 1393
Cdd:COG4913 541 DFKPHPFrAWLEAELGRRFdyvcvDSPEELRRHpraitragQVKGNGTRHEkddrrrIRSRYVLgfDNRAKLAALEAELA 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1394 KLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQN--EIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQkyeesqseles 1471
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDASSDDLAA----------- 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1472 sqkearsLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEA 1551
Cdd:COG4913 690 -------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1552 SLEHeegkiLRAQLEfNQIKAEiERKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGD-------- 1623
Cdd:COG4913 763 VERE-----LRENLE-ERIDAL-RARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDglpeyeer 835
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124376530 1624 ----LNEMEIQ-----LSHANRMAAEAQKQVKSLQSLLK------DTQIQLDDAVRANDDLKE 1671
Cdd:COG4913 836 fkelLNENSIEfvadlLSKLRRAIREIKERIDPLNDSLKripfgpGRYLRLEARPRPDPEVRE 898
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
869-1211 |
3.13e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 869 EARRKELEEKMVSLLQEKNDLQLQVQAEQDNLnDAEERCDQLIKNKI---QLEAKVKEMNERLEDEEEMNAELtakkRKL 945
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEIdvaSAEREIAELEAELERLDASSDDL----AAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 946 EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEmagLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKS 1025
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE---LDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1026 KVKLEQQVDDLEGSLEQ-EKKVRMDLERAKRKLEGDLKLTQESIMDLEndklqleeklkkkefDINQQNSKIEDEqvlal 1104
Cdd:COG4913 768 RENLEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLP---------------EYLALLDRLEED----- 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1105 qlqkKLKENQARIEELEEeleaeRTARAKVEKLRSDLSRELEEISERLEEA---------GGATSVQIEMNKKREAEFQK 1175
Cdd:COG4913 828 ----GLPEYEERFKELLN-----ENSIEFVADLLSKLRRAIREIKERIDPLndslkripfGPGRYLRLEARPRPDPEVRE 898
|
330 340 350
....*....|....*....|....*....|....*.
gi 124376530 1176 MRRDLEEATLQHEATAAALRKKHADSVAELGEQIDN 1211
Cdd:COG4913 899 FRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
845-1302 |
5.52e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 845 AETEKEMATMKEEFGRIKETLEKSEARRKELEEKM-------VSLLQEKNDLQLQVQAEQDNLND-------AEERCDQL 910
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEEcrvaaqaHNEEAESL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 911 IKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEI 990
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 991 IAKLTKEKKALQEAHQQALDDLQV-----------EEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKrkleg 1059
Cdd:PRK02224 428 EAELEATLRTARERVEEAEALLEAgkcpecgqpveGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE----- 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1060 DLKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRS 1139
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1140 DLSRE---LEEISERLEEAGGATSVQIEMNKKRE--AEFQKMRRD-LEEATLQHEATAAALrkkHADSVAELGEQIDN-- 1211
Cdd:PRK02224 583 ELKERiesLERIRTLLAAIADAEDEIERLREKREalAELNDERRErLAEKRERKRELEAEF---DEARIEEAREDKERae 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1212 --LQRVKQKLEkEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTEN-GE 1288
Cdd:PRK02224 660 eyLEQVEEKLD-ELREERDDLQAEIGAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNvET 738
|
490
....*....|....
gi 124376530 1289 LARQLEEKEALISQ 1302
Cdd:PRK02224 739 LERMLNETFDLVYQ 752
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1279-1919 |
8.29e-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: 63.97 E-value: 8.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1279 RAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLRE----------- 1347
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKEtcarsaektkk 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1348 ---QYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQ 1424
Cdd:pfam05483 174 yeyEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1425 NEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKyeesqselessqkeARSLSTELFKLKNAYEESLEHLETFKREN 1504
Cdd:pfam05483 254 NKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEK--------------KDHLTKELEDIKMSLQRSMSTQKALEEDL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1505 KNLQEEISDLTEqlgEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKdEE 1584
Cdd:pfam05483 320 QIATKTICQLTE---EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL-EE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1585 MEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKK-----------------KMEGDLNEMEIQLSHANRMAAEAQKQVKS 1647
Cdd:pfam05483 396 MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKiaeelkgkeqelifllqAREKEIHDLEIQLTAIKTSEEHYLKEVED 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1648 LQSLLKDTQIQLDDAVRANDDLK-ENIAIVERRNNLLQaeleELRAVVEQTERSRKLAEQELietsERVQLLHSQNTSLI 1726
Cdd:pfam05483 476 LKTELEKEKLKNIELTAHCDKLLlENKELTQEASDMTL----ELKKHQEDIINCKKQEERML----KQIENLEEKEMNLR 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1727 NQKKKMESDLTQLQSEVEEAVQEcrnAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRlDEAEQIA 1806
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLDK---SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQE-NKALKKK 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1807 LKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRK--SERRIKELTYQTEEDKKNL-------------LRLQDLVD 1871
Cdd:pfam05483 624 GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKeiEDKKISEEKLLEEVEKAKAiadeavklqkeidKRCQHKIA 703
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 124376530 1872 KLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQV 1919
Cdd:pfam05483 704 EMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNI 751
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1237-1707 |
1.66e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1237 MEQIIKAKANLEKVS-RTLEDQANEYRvKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLtRGKLSYTQQME 1315
Cdd:COG4717 48 LERLEKEADELFKPQgRKPELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-REELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1316 DLKRQLEEEGKAKNALAHALQSARHdcdlLREQYEEETEAKAELQRvlskANSEVAQWRTkyetdaiQRTEELEEAKKKL 1395
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEE----LEERLEELRELEEELEE----LEAELAELQE-------ELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1396 AQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDK------------ILAEWKQKYE 1463
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallaLLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1464 ESQSELESSQKEARSLS---TELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLG-EGGKNVHELEKVRKQLEvEK 1539
Cdd:COG4717 271 LILTIAGVLFLVLGLLAllfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIE-EL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1540 LELQSALEEAEASLEHEEGKILRAQLeFNQIKAEIERKLAEKDEEMEQAKRNHQRvVDSLQTSLDAETRSRNEVLRvkkk 1619
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQELKEE-LEELEEQLEELLGELEELLE---- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1620 mEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRAN--DDLKENIAIVERRNNLLQAELEELRAVVEQT 1697
Cdd:COG4717 424 -ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALELL 502
|
490
....*....|
gi 124376530 1698 ERSRKLAEQE 1707
Cdd:COG4717 503 EEAREEYREE 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1222-1804 |
1.99e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1222 EKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLE--DQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEal 1299
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE-- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1300 isqltrgklsytqqMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEE-ETEAKAELQRVLSKANSEVAQW---RT 1375
Cdd:COG4913 297 --------------LEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERerrRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1376 KYETDAIQ-------RTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQ 1448
Cdd:COG4913 363 RLEALLAAlglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1449 RNFDKILAEwkqkyeesqsELESSQKEARSLStELFKLKNAYEE--------------SL----EHLETFKR--ENKNLQ 1508
Cdd:COG4913 443 LALRDALAE----------ALGLDEAELPFVG-ELIEVRPEEERwrgaiervlggfalTLlvppEHYAAALRwvNRLHLR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1509 EEISdlTEQLGEGGKNVHELEKVRKQLeVEKLE---------LQSALE--------EAEASLEHEEGKILRAqlefNQIK 1571
Cdd:COG4913 512 GRLV--YERVRTGLPDPERPRLDPDSL-AGKLDfkphpfrawLEAELGrrfdyvcvDSPEELRRHPRAITRA----GQVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1572 AeiERKLAEKDEEMEQAKR-----NHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMA--AEAQKQ 1644
Cdd:COG4913 585 G--NGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeySWDEID 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1645 VKSLQSLLKDTQIQLDDAVRANDDLKEniaiverrnnlLQAELEELRAVVEQtersrklAEQELIETSERVQLLHSQNTS 1724
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDLAA-----------LEEQLEELEAELEE-------LEEELDELKGEIGRLEKELEQ 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1725 LinqkkkmESDLTQLQSEVEEAVQECRNAEEKAkkaitdaammAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQ 1804
Cdd:COG4913 725 A-------EEELDELQDRLEAAEDLARLELRAL----------LEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
849-1257 |
2.03e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 849 KEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQD--NLNDAEERCDQLIKNKIQLEAKVKEMNE 926
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 927 RLEDEEEMNAELTAKKRKLEDEC-----------SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 995
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 996 KEKKALQE-----------AHQQALDDLQVEEDKV---------------NSLSKSKVKLEQQVDDLEGSLEQEKKVRMD 1049
Cdd:COG4717 241 LEERLKEArlllliaaallALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1050 LERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDINQqnskiedeqvlaLQLQKKLKENQARIEELEEELEAERT 1129
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE------------LQLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1130 ARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKR--EAEFQKMRRDLEEATLQHEataaALRKKHADSVAELG- 1206
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELE----ELREELAELEAELEq 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 124376530 1207 -EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMeqiiKAKANLEKVSRTLEDQ 1257
Cdd:COG4717 465 lEEDGELAELLQELEELKAELRELAEEWAALK----LALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
916-1142 |
2.14e-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: 61.70 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 916 QLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 995
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 996 KEKK----ALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDL 1071
Cdd:COG4942 104 EELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124376530 1072 ENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIEE--LEEELEAERTARAKVEKLRSDLS 1142
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARleAEAAAAAERTPAAGFAALKGKLP 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1617-1838 |
2.26e-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: 61.70 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1617 KKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAvvEQ 1696
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA--EL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1697 TERSRKLAE-----QELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEEL 1771
Cdd:COG4942 100 EAQKEELAEllralYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124376530 1772 KKEQDTS-AHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELEGELEAEQKRNAES 1838
Cdd:COG4942 180 LAELEEErAALEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1188-1600 |
2.63e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1188 EATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFK---LELDDVTSNMEQIIKAKANLEKVSRTLED--QANEYR 1262
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAelqEELEELEEELEELEAELEELREELEKLEKllQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1263 VKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKlsytQQMEDLKRQLEEEgkAKNALAHALQSARHdc 1342
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQ----EELEELLEQLSLA--TEEELQDLAEELEE-- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1343 dlLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQrtEELEEAK------------------------------ 1392
Cdd:COG4717 204 --LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE--ERLKEARlllliaaallallglggsllsliltiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1393 -----------KKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQk 1461
Cdd:COG4717 280 flvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1462 yeesqSELESSQKEARSLSTELFKLKNA-YEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKvrkqlEVEKL 1540
Cdd:COG4717 359 -----LEEELQLEELEQEIAALLAEAGVeDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----ALDEE 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1541 ELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERklAEKDEEMEQAKRNHQRVVDSLQ 1600
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQ--LEEDGELAELLQELEELKAELR 486
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
906-1602 |
2.83e-09 |
|
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: 62.29 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 906 RCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAT----ENKVKNLT 981
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERkqvlEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 982 EEMAGLDEIIAKLTKEKKALQEAH--QQALDDLQVEEDKVNSLskskvklEQQVDDLEGSLEQEKKVRMDLERAKRKLEG 1059
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQ-------EAVLEETQERINRARKAAPLAAHIKAVTQI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1060 DLKLtqESIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKlkENQARIEELEEELEAERTARAKVEKLRS 1139
Cdd:TIGR00618 306 EQQA--QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ--EIHIRDAHEVATSIREISCQQHTLTQHI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1140 DLSRELEEISERLEEAGgATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKL 1219
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSL-CKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1220 EKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNdfttQRAKLQTENGELARQLEEKEAL 1299
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN----PARQDIDNPGPLTRRMQRGEQT 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1300 ISQLTrgklsytQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSkansEVAQWRTKYET 1379
Cdd:TIGR00618 537 YAQLE-------TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV----RLQDLTEKLSE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1380 DAIQRTEELEEAKKKLAQRLQDAEEAVEAVNaKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRnfdkilaewk 1459
Cdd:TIGR00618 606 AEDMLACEQHALLRKLQPEQDLQDVRLHLQQ-CSQELALKLTALHALQLTLTQERVREHALSIRVLPKEL---------- 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1460 qkyeesqselessqkeARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEIsdltEQLGEGGKNVHELEKVRKQLEVEK 1539
Cdd:TIGR00618 675 ----------------LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELE----THIEEYDREFNEIENASSSLGSDL 734
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124376530 1540 LELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQTS 1602
Cdd:TIGR00618 735 AAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREED 797
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
916-1296 |
2.97e-09 |
|
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: 61.83 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 916 QLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 995
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 996 KEKKAL---QEAHQQALDDLqveEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLE 1072
Cdd:pfam07888 115 EEKDALlaqRAAHEARIREL---EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1073 NDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSreleeiserl 1152
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS---------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1153 eEAGGATSvqiemnkKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDD 1232
Cdd:pfam07888 262 -SMAAQRD-------RTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEER 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124376530 1233 VTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGEL---ARQLEEK 1296
Cdd:pfam07888 334 LQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELleyIRQLEQR 400
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1182-1840 |
3.25e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 62.05 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1182 EATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDvtsNMEQIIKAKANLEKVSRTLEDQANEY 1261
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKE---DHEKIQHLEEEYKKEINDKEKQVSLL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1262 RVKLEEAQRSLNDFTTqrakLQTENGELARQLEEKEAL----ISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQS 1337
Cdd:pfam05483 246 LIQITEKENKMKDLTF----LLEESRDKANQLEEKTKLqdenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1338 A-RHDCDLLRE---QYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDAEEAVEavnakc 1413
Cdd:pfam05483 322 AtKTICQLTEEkeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QRLEKNEDQLKIITMELQKKSSELE------ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1414 sslEKTKHRLQNEIEdlMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEES 1493
Cdd:pfam05483 395 ---EMTKFKNNKEVE--LEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1494 LEHLETFKREnknlqeeisdlteqlgeggknvhelekvrkqLEVEKLElqsaleeaEASLEHEEGKILRAQLEFNQIKAE 1573
Cdd:pfam05483 470 LKEVEDLKTE-------------------------------LEKEKLK--------NIELTAHCDKLLLENKELTQEASD 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1574 IERKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLK 1653
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1654 DTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKME 1733
Cdd:pfam05483 591 ILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISE 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1734 SDL----TQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKG 1809
Cdd:pfam05483 671 EKLleevEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSN 750
|
650 660 670
....*....|....*....|....*....|....
gi 124376530 1810 GKKQLQKLEARV---RELEGELEAEQKRNAESVK 1840
Cdd:pfam05483 751 IKAELLSLKKQLeieKEEKEKLKMEAKENTAILK 784
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1105-1339 |
3.87e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1105 QLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnkkrEAEFQKMRRDLEEAT 1184
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------------EQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1185 LQheatAAALRKKHADSVAELGEQIDNLQRVKQKlekekSEFKLELDdvTSNMEQIIKAKANLEKVSRTLEDQANEYRVK 1264
Cdd:COG4942 90 KE----IAELRAELEAQKEELAELLRALYRLGRQ-----PPLALLLS--PEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1265 LEEAQRSLNDFTTQRAKL-------QTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQS 1337
Cdd:COG4942 159 LAELAALRAELEAERAELeallaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
..
gi 124376530 1338 AR 1339
Cdd:COG4942 239 AA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
846-1430 |
4.64e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 846 ETEKEMATMKEEFG---RIKETLEKSEARRKELE------EKMVSLLQEKNDLQ-----LQVQAEQDNLNDAEERCDQLI 911
Cdd:COG4913 222 DTFEAADALVEHFDdleRAHEALEDAREQIELLEpirelaERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 912 KNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLE-DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEI 990
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 991 IAKLTKEKKALQEAHQQALDDLQVEEDKvnsLSKSKVKLEQQVDDLEG---SLEQeKKVRMD--LERAKRKLEGDLKLTQ 1065
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAE---AEAALRDLRRELRELEAeiaSLER-RKSNIParLLALRDALAEALGLDE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1066 ESI------MDLEN----------------------------------DKLQLEEKL---KKKEFDINQQNSKIeDEQVL 1102
Cdd:COG4913 458 AELpfvgelIEVRPeeerwrgaiervlggfaltllvppehyaaalrwvNRLHLRGRLvyeRVRTGLPDPERPRL-DPDSL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1103 ALQLQkkLKENQARieELEEELEAERTARAKVEKLRsdlsrELEEISERLEEAGgatsvQIEMNKKReaeFQKMRRDLEE 1182
Cdd:COG4913 537 AGKLD--FKPHPFR--AWLEAELGRRFDYVCVDSPE-----ELRRHPRAITRAG-----QVKGNGTR---HEKDDRRRIR 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1183 AT--LQHEATA--AALRKKHA---DSVAELGEQIDNLQRVKQKLEKEKS------EFKLELDDVTSNMEQIIKAKANLEK 1249
Cdd:COG4913 600 SRyvLGFDNRAklAALEAELAeleEELAEAEERLEALEAELDALQERREalqrlaEYSWDEIDVASAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1250 VS------RTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEE 1323
Cdd:COG4913 680 LDassddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1324 EGKAKNALAHALQSARHDCDLLREQYEEETEAKaeLQRVLSKANSEVAQWRTKYET----DAI---QRTEELEEAKKKLA 1396
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERA--MRAFNREWPAETADLDADLESlpeyLALldrLEEDGLPEYEERFK 837
|
650 660 670
....*....|....*....|....*....|....
gi 124376530 1397 QRLQDAEEavEAVNAKCSSLEKTKHRLQNEIEDL 1430
Cdd:COG4913 838 ELLNENSI--EFVADLLSKLRRAIREIKERIDPL 869
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1442-1882 |
5.38e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1442 AALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLtEQLGEG 1521
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1522 GKNVHELEKVRKQLEVEKLELQsALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQT 1601
Cdd:COG4717 128 LPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1602 SLDAETRSRNEVLRVKKKMEGDLNEMEIQLshanrMAAEAQKQVKSLQSLLK--DTQIQLDDAVRANDDLKENIA----- 1674
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARLLLLiaAALLALLGLGGSLLSLILTIAgvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1675 ------IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQ 1748
Cdd:COG4717 282 vlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1749 ECRNAEEKAKKA----------ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKggkKQLQKLE 1818
Cdd:COG4717 362 ELQLEELEQEIAallaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE---EELEELE 438
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124376530 1819 ARVRELEGELEAEQKRnaesvkgMRKSERRIKELTYQTEEDKKnLLRLQDLVDKLQLKVKAYKR 1882
Cdd:COG4717 439 EELEELEEELEELREE-------LAELEAELEQLEEDGELAEL-LQELEELKAELRELAEEWAA 494
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1489-1933 |
5.77e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1489 AYEESLEHLETFKRENKNLQEEISDLTEQLGEGgknvhelEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFN 1568
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKTETGKAEEARKAEEAKKKA-------EDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1569 qiKAEIERKlAEKDEEMEQAKRnhqrvvdSLQTSLDAETRSRNEVlrvkKKMEGDLNEMEIQLSHANRMAAEAQK--QVK 1646
Cdd:PTZ00121 1165 --KAEEARK-AEDAKKAEAARK-------AEEVRKAEELRKAEDA----RKAEAARKAEEERKAEEARKAEDAKKaeAVK 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1647 SLQSLLKDTQiqldDAVRANddlKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNtsli 1726
Cdd:PTZ00121 1231 KAEEAKKDAE----EAKKAE---EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE---- 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1727 nQKKKMEsdltqlqsEVEEAVQECRNAEEKAKKAiTDAAMMAEELKKEQdtsahlERMKKNMEQTIKDLQHRLDEAEQIA 1806
Cdd:PTZ00121 1300 -EKKKAD--------EAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKA------EEAKKAAEAAKAEAEAAADEAEAAE 1363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1807 LKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQlKVKAYKRQAEE 1886
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEE 1442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 124376530 1887 AE--EQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKQ 1933
Cdd:PTZ00121 1443 AKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
863-1430 |
6.83e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.51 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 863 ETLEKSEARRKELEEkmvsllqeknDLQLQVQAEQdNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKK 942
Cdd:PRK04863 513 EQLQQLRMRLSELEQ----------RLRQQQRAER-LLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERR 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 943 RKLEDECSELKKDIDdlelTLAKVEKEKHATENKVKNLTEEM-------AGLDEIIAKLTKEKKALQ------EAHQQAL 1009
Cdd:PRK04863 582 MALRQQLEQLQARIQ----RLAARAPAWLAAQDALARLREQSgeefedsQDVTEYMQQLLERERELTverdelAARKQAL 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1010 DD---------------LQVEEDKVNSLSKSKVKLEQQVDD------LEGSLEQEKKVRmDLERAKRKLEGdlkltqesI 1068
Cdd:PRK04863 658 DEeierlsqpggsedprLNALAERFGGVLLSEIYDDVSLEDapyfsaLYGPARHAIVVP-DLSDAAEQLAG--------L 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1069 MDLENDKLQLEEklkkkefDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARakvEKLRSDLSRELEEI 1148
Cdd:PRK04863 729 EDCPEDLYLIEG-------DPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEVPLFGRAAR---EKRIEQLRAEREEL 798
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1149 SERLEeaggatsvqiemnkKREAEFQKMRR---DLEEATLQH---------EATAAALRKKHADSVAELGEQIDNLQRVK 1216
Cdd:PRK04863 799 AERYA--------------TLSFDVQKLQRlhqAFSRFIGSHlavafeadpEAELRQLNRRRVELERALADHESQEQQQR 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1217 QKLEKEKSEFKLelddvtsnMEQIIKAKANLEKvsRTLEDQANEYRVKLEEAQ----------RSLNDFTTQRAKLQTEN 1286
Cdd:PRK04863 865 SQLEQAKEGLSA--------LNRLLPRLNLLAD--ETLADRVEEIREQLDEAEeakrfvqqhgNALAQLEPIVSVLQSDP 934
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1287 GELA---RQLEEKEALISQLTRGK--LSYTQQM------EDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEA 1355
Cdd:PRK04863 935 EQFEqlkQDYQQAQQTQRDAKQQAfaLTEVVQRrahfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQ 1014
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1356 KAELQRVLSKANSEvaqWRTKYET--DAIQRTEEL-----EEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIE 1428
Cdd:PRK04863 1015 LAQYNQVLASLKSS---YDAKRQMlqELKQELQDLgvpadSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMD 1091
|
..
gi 124376530 1429 DL 1430
Cdd:PRK04863 1092 NL 1093
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
843-1154 |
8.45e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 843 KSAETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVK 922
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 923 EMNER----------------------------LEDEEEMNAELTAKKRKLEDECSELKKDIDDLElTLAKVEKEKHATE 974
Cdd:PRK02224 437 TARERveeaealleagkcpecgqpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLE 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 975 NKVKNLTEEMA----GLDE---IIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVR 1047
Cdd:PRK02224 516 ERREDLEELIAerreTIEEkreRAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1048 MDLERAKrKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKK-LKENQARIEELEEELEA 1126
Cdd:PRK02224 596 TLLAAIA-DAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKErAEEYLEQVEEKLDELRE 674
|
330 340
....*....|....*....|....*....
gi 124376530 1127 ERTA-RAKVEKLRSDLsRELEEISERLEE 1154
Cdd:PRK02224 675 ERDDlQAEIGAVENEL-EELEELRERREA 702
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
898-1837 |
1.08e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 60.84 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 898 DNLNDAEERCDQLIKNKiqleAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKKdiddlelTLAKVEKEKHATENKV 977
Cdd:TIGR01612 769 NKINDYAKEKDELNKYK----SKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIK-------TISIKEDEIFKIINEM 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 978 KNLTEE-MAGLDEIIAKLTKEKKALQEAHQQALD-----DLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLe 1051
Cdd:TIGR01612 838 KFMKDDfLNKVDKFINFENNCKEKIDSEHEQFAEltnkiKAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTL- 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1052 rakRKLEGDLKL---TQESIMDLENDKLQLEEKLKKK----------------EFDINQQNSKIEDEQVLA--------- 1103
Cdd:TIGR01612 917 ---KKVDEYIKIcenTKESIEKFHNKQNILKEILNKNidtikesnlieksykdKFDNTLIDKINELDKAFKdaslndyea 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1104 -----LQLQKKLKENQARIEELEEELEAERTARA------KVEKLRSDLSR-------ELEEISERLEEAGGATSVQIEM 1165
Cdd:TIGR01612 994 knnelIKYFNDLKANLGKNKENMLYHQFDEKEKAtndieqKIEDANKNIPNieiaihtSIYNIIDEIEKEIGKNIELLNK 1073
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1166 NKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKlELDDVTSNMEQIIKAKA 1245
Cdd:TIGR01612 1074 EILEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALE-EIKKKSENYIDEIKAQI 1152
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1246 N-LEKVSRTLedQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGK---LSYTQQMEDL-KRQ 1320
Cdd:TIGR01612 1153 NdLEDVADKA--ISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKginLSYGKNLGKLfLEK 1230
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1321 LEEEGKAKNALAHALQSARHDCDLLREQYEE-------ETEAKAELQrVLSKANSEvaqwRTKYETDAIQRTEELEEAKK 1393
Cdd:TIGR01612 1231 IDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEienemgiEMDIKAEME-TFNISHDD----DKDHHIISKKHDENISDIRE 1305
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1394 KLAQRLQDaeeaveavNAKCSSLEKTKHRLQNEIedlmVDVERSNAAAAALDKKQRNFDKILaewkqkyeesqselessq 1473
Cdd:TIGR01612 1306 KSLKIIED--------FSEESDINDIKKELQKNL----LDAQKHNSDINLYLNEIANIYNIL------------------ 1355
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1474 kearslstELFKLKNAYEESLEHLETFKRENKNLQEEISDlTEQLgeggknvhelekvrkqleVEKLELQSALEEAEASL 1553
Cdd:TIGR01612 1356 --------KLNKIKKIIDEVKEYTKEIEENNKNIKDELDK-SEKL------------------IKKIKDDINLEECKSKI 1408
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1554 EHE-EGKILRAQLE-FNQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNeVLRVKKK-----MEGDLNE 1626
Cdd:TIGR01612 1409 ESTlDDKDIDECIKkIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQH-ILKIKKDnatndHDFNINE 1487
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1627 MEIQLSHANRMAAEAQKQVKSLQS---LLKdtQIQLDDAVRAND----DLKENIAIVERRNNLLQAELEELRAVV----E 1695
Cdd:TIGR01612 1488 LKEHIDKSKGCKDEADKNAKAIEKnkeLFE--QYKKDVTELLNKysalAIKNKFAKTKKDSEIIIKEIKDAHKKFileaE 1565
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1696 QTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQ--SEVEEAVQECRNAEEKAKKAITDAAMMAEE--L 1771
Cdd:TIGR01612 1566 KSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLkiSDIKKKINDCLKETESIEKKISSFSIDSQDteL 1645
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124376530 1772 KKEQDTSAHLERMKKNMEQTIKDLQHRldeaeqialkggKKQLQKLEARVRELEGELEaEQKRNAE 1837
Cdd:TIGR01612 1646 KENGDNLNSLQEFLESLKDQKKNIEDK------------KKELDELDSEIEKIEIDVD-QHKKNYE 1698
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1683-1930 |
1.24e-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: 60.19 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1683 LQAELEELRAVVEQteRSRKLaEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEavQECRNAEEKAKKAIT 1762
Cdd:pfam01576 55 LCAEAEEMRARLAA--RKQEL-EEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE--EEAARQKLQLEKVTT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1763 DAAM--MAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlKGGKKQLQKLEARVRELEGELEAEQKRNAESVK 1840
Cdd:pfam01576 130 EAKIkkLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA-KSLSKLKNKHEAMISDLEERLKKEEKGRQELEK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1841 GMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVN 1920
Cdd:pfam01576 209 AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN 288
|
250
....*....|
gi 124376530 1921 KLRAKSRDIG 1930
Cdd:pfam01576 289 KAEKQRRDLG 298
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1417-1922 |
1.60e-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: 59.65 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1417 EKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKnAYEESLEH 1496
Cdd:TIGR04523 137 KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK-KKIQKNKS 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1497 LET----FKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKA 1572
Cdd:TIGR04523 216 LESqiseLKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1573 EIE----RKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSL 1648
Cdd:TIGR04523 296 EISdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1649 QSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQ 1728
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1729 KKKMESDLTQLQSEVEEAVQECRNAEEKAKKaitdaamMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALK 1808
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQ-------KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1809 GGKKQLQKlEARVRELEGELEAEQKRNAESV--KGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEE 1886
Cdd:TIGR04523 529 LESEKKEK-ESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
490 500 510
....*....|....*....|....*....|....*.
gi 124376530 1887 AEEQANTNLSKFRKVQHELDEAEERADIAESQVNKL 1922
Cdd:TIGR04523 608 KEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1199-1415 |
1.87e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1199 ADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQ 1278
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1279 RAKLQTENGELARQLEEKEAL-----------ISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLRE 1347
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124376530 1348 QYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSS 1415
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1568-1896 |
2.44e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.26 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1568 NQIKAEIE----RKLAEK-------DEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLrvkkkmegdlnemEIQLSHANr 1636
Cdd:COG3206 81 SPLETQIEilksRPVLERvvdklnlDEDPLGEEASREAAIERLRKNLTVEPVKGSNVI-------------EISYTSPD- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1637 mAAEAQKQVKSLQSLLKDTQIQLddavranddlkeNIAIVERRNNLLQAELEELRAVVEQTERSRK--LAEQELIETSER 1714
Cdd:COG3206 147 -PELAAAVANALAEAYLEQNLEL------------RREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1715 VQLLHSQNTSLINQKKKMESDLTQLQSEVEeAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK--------- 1785
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLA-ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpd 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1786 -KNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRnaesVKGMRKSERRIKELTYQTEEDKKNll 1864
Cdd:COG3206 293 vIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVAREL-- 366
|
330 340 350
....*....|....*....|....*....|..
gi 124376530 1865 rLQDLVDKLQlkvkaykrQAEEAEEQANTNLS 1896
Cdd:COG3206 367 -YESLLQRLE--------EARLAEALTVGNVR 389
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
849-1697 |
3.06e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 849 KEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQliKNKIQ--------LEAK 920
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQ--QEKIEryqadleeLEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 921 VKEMNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDL-------------------------------ELTLAKVEKE 969
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYqqaldvqqtraiqyqqavqalerakqlcglpDLTADNAEDW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 970 KHATENKVKNLTEEMAGL-------DEIIAKLTKEKKALQ---------EAHQQALDDL-QVEEDKVnsLSKSKVKLEQQ 1032
Cdd:PRK04863 444 LEEFQAKEQEATEELLSLeqklsvaQAAHSQFEQAYQLVRkiagevsrsEAWDVARELLrRLREQRH--LAEQLQQLRMR 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1033 VDDLEGSLEQEKkvrmDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKkkefDINQQnskIEDEQVLALQLQKKLKE 1112
Cdd:PRK04863 522 LSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE----SLSES---VSEARERRMALRQQLEQ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1113 NQARIEELEEELEAERTARAKVEKLRSDLSRELEEiSERLEEAggatsvqiemnkkreaeFQKMRRDLEEATLQHEATAA 1192
Cdd:PRK04863 591 LQARIQRLAARAPAWLAAQDALARLREQSGEEFED-SQDVTEY-----------------MQQLLERERELTVERDELAA 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1193 ALRkkhadsvaELGEQIDNLQ--------RVKQKLEKEKSEFKLEL-DDVtsnmeqiikakanlekvsrTLEDqANEYRV 1263
Cdd:PRK04863 653 RKQ--------ALDEEIERLSqpggsedpRLNALAERFGGVLLSEIyDDV-------------------SLED-APYFSA 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1264 KLEEAQRSL--NDFTTQRAKLQTENGeLARQLEEKEALISQLTRGKLSYTQQMEDL-----KRQLEEEG---------KA 1327
Cdd:PRK04863 705 LYGPARHAIvvPDLSDAAEQLAGLED-CPEDLYLIEGDPDSFDDSVFSVEELEKAVvvkiaDRQWRYSRfpevplfgrAA 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1328 KNALAHALQSARhdcDLLREQYEEETEAKAELQRVLSKANSEVA-------QWRTKYETDAIQRT--------EELEEAK 1392
Cdd:PRK04863 784 REKRIEQLRAER---EELAERYATLSFDVQKLQRLHQAFSRFIGshlavafEADPEAELRQLNRRrveleralADHESQE 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1393 KKLAQRLQDAEEAVEAVN--AKCSSLEKTKHrLQNEIEDLMVDVERSNAAAAALDKKQRNFDKI-------------LAE 1457
Cdd:PRK04863 861 QQQRSQLEQAKEGLSALNrlLPRLNLLADET-LADRVEEIREQLDEAEEAKRFVQQHGNALAQLepivsvlqsdpeqFEQ 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1458 WKQKYEESQSELESSQKEARSLsTELFKLKN--AYEESLEHLetfkrenknlqEEISDLTEQLgeggknvheleKVR-KQ 1534
Cdd:PRK04863 940 LKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAhfSYEDAAEML-----------AKNSDLNEKL-----------RQRlEQ 996
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1535 LEVEKLELQSALEEAEAslEHEEGKILRAQLE-----FNQIKAEIERKLAE----KDEEMEQAKRNHQrvvDSLQTSLDA 1605
Cdd:PRK04863 997 AEQERTRAREQLRQAQA--QLAQYNQVLASLKssydaKRQMLQELKQELQDlgvpADSGAEERARARR---DELHARLSA 1071
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1606 ETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQV----KSLQSLLKdtqiqlddAVRANDdlkeniaiVERRnn 1681
Cdd:PRK04863 1072 NRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVvnakAGWCAVLR--------LVKDNG--------VERR-- 1133
|
970 980
....*....|....*....|.
gi 124376530 1682 LLQAEL-----EELRAVVEQT 1697
Cdd:PRK04863 1134 LHRRELaylsaDELRSMSDKA 1154
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1065-1292 |
3.11e-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: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1065 QESIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRE 1144
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1145 LEEISERLEE-------AGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRkkhadsvaelgEQIDNLQRVKQ 1217
Cdd:COG4942 99 LEAQKEELAEllralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR-----------ADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124376530 1218 KLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQ 1292
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
833-1085 |
3.23e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 833 KLYFKIKPLLKSAETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIK 912
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 913 NKIQLEAKVKEMNERLEDEEEMNAELTAKKRK-LEDECSELKKdIDDLELTLAKVEKEKHATENKVKNLTEEmagLDEII 991
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKELEP-FYNEYLELKDAEKELEREEKELKKLEEE---LDKAF 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 992 AKLTKEKKALQEAHQQaLDDLQVE--EDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIM 1069
Cdd:PRK03918 633 EELAETEKRLEELRKE-LEELEKKysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
250
....*....|....*...
gi 124376530 1070 DLENDKLQLE--EKLKKK 1085
Cdd:PRK03918 712 ELEKLEKALErvEELREK 729
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1216-1443 |
3.67e-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: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1216 KQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEE 1295
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1296 KEALISQLTRG--KLSYTQQMEDLKRQleeegKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQW 1373
Cdd:COG4942 102 QKEELAELLRAlyRLGRQPPLALLLSP-----EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1374 RTKYETDAIQRtEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAA 1443
Cdd:COG4942 177 EALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
844-1569 |
3.87e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 58.68 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 844 SAETEKEMATMKEEFGRIKEtleksearrkeLEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKE 923
Cdd:pfam10174 38 SPELKKERALRKEEAARISV-----------LKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGED 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 924 MNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELtlaKVEKEKHATENKvknlteemaglDEIIAKLtkekkaLQE 1003
Cdd:pfam10174 107 KFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMEL---RIETQKQTLGAR-----------DESIKKL------LEM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1004 AHQQALDDLQVEEDkvNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDL-ERAKRKLEG--------------DLKLTQESI 1068
Cdd:pfam10174 167 LQSKGLPKKSGEED--WERTRRIAEAEMQLGHLEVLLDQKEKENIHLrEELHRRNQLqpdpaktkalqtviEMKDTKISS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1069 MDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENqarieeleeeleaertaraKVEKLRSDLSR---EL 1145
Cdd:pfam10174 245 LERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKN-------------------KIDQLKQELSKkesEL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1146 EEISERLEEAGGATS---VQIEMNKKREAEfqkmrRDLEEATLQHEATAAALRKKHADSVaeLGEQIDNLQRvkqkLEKE 1222
Cdd:pfam10174 306 LALQTKLETLTNQNSdckQHIEVLKESLTA-----KEQRAAILQTEVDALRLRLEEKESF--LNKKTKQLQD----LTEE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1223 KSEFKLELDDVtSNMEQIIKAKAN-LEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALIS 1301
Cdd:pfam10174 375 KSTLAGEIRDL-KDMLDVKERKINvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1302 QLtrgklsyTQQMEDLKRQLEEEgkaKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDA 1381
Cdd:pfam10174 454 RL-------KEQREREDRERLEE---LESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLE 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1382 IQRTEELEEAKK-----KLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILA 1456
Cdd:pfam10174 524 IAVEQKKEECSKlenqlKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIA 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1457 EWKQKYEESQSELESSQKEARSLSTELfKLKNAYEESLEHLETFKRENKNLQEEISDLTEqlgeggknvhELEKVRKQLE 1536
Cdd:pfam10174 604 ELESLTLRQMKEQNKKVANIKHGQQEM-KKKGAQLLEEARRREDNLADNSQQLQLEELMG----------ALEKTRQELD 672
|
730 740 750
....*....|....*....|....*....|....*....
gi 124376530 1537 VEKLEL---QSALEEAEA---SLEHEEGKILRAQLEFNQ 1569
Cdd:pfam10174 673 ATKARLsstQQSLAEKDGhltNLRAERRKQLEEILEMKQ 711
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1649-1899 |
5.60e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1649 QSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQllhsqntSLINQ 1728
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1729 KKKMESDLTQLQSEVEEAVqecRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQI--A 1806
Cdd:COG4942 92 IAELRAELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALraE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1807 LKGGKKQLQKLEARVRELEGELEAEQKRNAESVKgmrKSERRIKELTYQTEEDKKNLLRLQDLVDKLQlkvkayKRQAEE 1886
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLE------AEAAAA 239
|
250
....*....|...
gi 124376530 1887 AEEQANTNLSKFR 1899
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
837-1329 |
6.40e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 837 KIKPLLKSAETEKEMATMK---EEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQ----DNLNDAEE--RC 907
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAkkkaDEAKKAEEakKA 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 908 DQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVknltEEMAGL 987
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI----EEVMKL 1600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 988 DEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDlKLTQES 1067
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED-KKKAEE 1679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1068 IMDLENDKLQLEEKLKKKEfdinqqNSKIEDEQVLALQLQKKLKENQARIEELEEELeaertaraKVEKLRsdlsRELEE 1147
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEA------EEAKKAEELKKKEAEEKKKAEELKKAEEENKI--------KAEEAK----KEAEE 1741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1148 ISERLEEAggatsvqiemnKKREAEFQKMRRDLEEatlqhEATAAALRKKHADSVAELGeqidnlqrVKQKLEKEKSEFK 1227
Cdd:PTZ00121 1742 DKKKAEEA-----------KKDEEEKKKIAHLKKE-----EEKKAEEIRKEKEAVIEEE--------LDEEDEKRRMEVD 1797
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1228 LELDDVTSNMEQIIK-----------AKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEK 1296
Cdd:PTZ00121 1798 KKIKDIFDNFANIIEggkegnlvindSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLK 1877
|
490 500 510
....*....|....*....|....*....|...
gi 124376530 1297 EALISQLTRGKLSYTQQMEDLKRQLEEEGKAKN 1329
Cdd:PTZ00121 1878 EDDEEEIEEADEIEKIDKDDIEREIPNNNMAGK 1910
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
837-1186 |
7.13e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.82 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 837 KIKPLLKSAETEKEM-ATMKEEFGRIKETLEKSE-------------ARRKELEEKMVSLLQEKNDLQLQ----VQAEQD 898
Cdd:pfam15921 462 KVSSLTAQLESTKEMlRKVVEELTAKKMTLESSErtvsdltaslqekERAIEATNAEITKLRSRVDLKLQelqhLKNEGD 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 899 NLNDAEERCDQLiknKIQLEAK---VKEMNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATEN 975
Cdd:pfam15921 542 HLRNVQTECEAL---KLQMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 976 KVKNLTEEMAGLDEIIAKLT-------KEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQ-EKKVR 1047
Cdd:pfam15921 619 KIRELEARVSDLELEKVKLVnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETtTNKLK 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1048 MDLERAKRKLE---GDLKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSKI---EDEQVLALQLQKKLKENQARIEELE 1121
Cdd:pfam15921 699 MQLKSAQSELEqtrNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIqflEEAMTNANKEKHFLKEEKNKLSQEL 778
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124376530 1122 EELEAERTARA-KVEKLRSDlSRELEEISERLEEAGGATSVQ------IEMNKKREAEFQKMRRDLEEATLQ 1186
Cdd:pfam15921 779 STVATEKNKMAgELEVLRSQ-ERRLKEKVANMEVALDKASLQfaecqdIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1351-1911 |
8.39e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.42 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1351 EETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEE------AKKKLAQRLQDAEEAV----EAVNAKCSSLEKTK 1420
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQEnrkiieAQRKAIQELQFENEKVslklEEEIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1421 HRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTEL-FKLKNAYEEsLEHLET 1499
Cdd:pfam05483 151 NATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMhFKLKEDHEK-IQHLEE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1500 -FKRENKNLQEEIS--------------DLTEQLGEGGKNVHELEKVRK-------QLEVEKLELQSALEEAEASLEHEE 1557
Cdd:pfam05483 230 eYKKEINDKEKQVSllliqitekenkmkDLTFLLEESRDKANQLEEKTKlqdenlkELIEKKDHLTKELEDIKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1558 GKILRAQLEFNQIKAEIERKLAEKDEEMEQ---AKRNHQRVVdslqTSLDAETRSRNEVLRV-KKKMEGDLNEMEIqlsh 1633
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLTEEKEAQMEElnkAKAAHSFVV----TEFEATTCSLEELLRTeQQRLEKNEDQLKI---- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1634 anrMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERrNNLLQAELEELRAVVEQTERSRKLAEQELIETSE 1713
Cdd:pfam05483 382 ---ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDE-KKQFEKIAEELKGKEQELIFLLQAREKEIHDLEI 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1714 RVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIK 1793
Cdd:pfam05483 458 QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIE 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1794 DLQHR---LDEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNllrlqdlV 1870
Cdd:pfam05483 538 NLEEKemnLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN-------I 610
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 124376530 1871 DKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEER 1911
Cdd:pfam05483 611 EELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK 651
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
833-1326 |
8.85e-08 |
|
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: 57.75 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 833 KLYFKIKPLLKSAETEKEMATMKEEFGRIKETLEKSE--ARRKELEEKMVSLLQEKNDL------QLQVQAEQDNLNDAE 904
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLdrklrkLDQEMEQLNHHTTTR 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 905 ERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKV 977
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 978 KNLTEEMAGLDEIIAKLTKekkalQEAHQQALDDLQVEEDKVnslSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKL 1057
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCG-----SQDEESDLERLKEEIEKS---SKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRV 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1058 EGDLKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIeeleeeleaeRTARAKVEKL 1137
Cdd:TIGR00606 687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEI----------PELRNKLQKV 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1138 RSDLSRELEEISERlEEAGGATSVQIEMNKKREAEFQKMRRdLEEATLQHEataaalrKKHADSVAELgeQIDNLQRVKQ 1217
Cdd:TIGR00606 757 NRDIQRLKNDIEEQ-ETLLGTIMPEEESAKVCLTDVTIMER-FQMELKDVE-------RKIAQQAAKL--QGSDLDRTVQ 825
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1218 KLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANE---YRVKLEEAQRSLNDFTTQRAKLQTENGELARQLE 1294
Cdd:TIGR00606 826 QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElksEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIK 905
|
490 500 510
....*....|....*....|....*....|..
gi 124376530 1295 EKEALISQLTRGKLSYTQQMEDLKRQLEEEGK 1326
Cdd:TIGR00606 906 DAKEQDSPLETFLEKDQQEKEELISSKETSNK 937
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
835-1285 |
9.59e-08 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 57.15 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 835 YFKIKPLLKSAE-----TEKEMATMKEEFGRIKETLEKSEARRKELEEKMvsllqekNDLQLQVQAEQDNLNDAEErcdq 909
Cdd:PRK04778 100 FRKAKHEINEIEslldlIEEDIEQILEELQELLESEEKNREEVEQLKDLY-------RELRKSLLANRFSFGPALD---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 910 liknkiQLEAKVKEMNERLEDEEEMNAE---LTAKK--RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN----L 980
Cdd:PRK04778 169 ------ELEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 981 TEEMAGLDEIiaKLTKEKKALQEAHQQALDDLqvEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGD 1060
Cdd:PRK04778 243 VEEGYHLDHL--DIEKEIQDLKEQIDENLALL--EELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1061 LKLTQEsimdlENDKLQLEEKLKKKEFDINqqnskiEDEQVLALQLQKKLKENQARIEELEEELeaertarAKVEKLRSD 1140
Cdd:PRK04778 319 LEHAKE-----QNKELKEEIDRVKQSYTLN------ESELESVRQLEKQLESLEKQYDEITERI-------AEQEIAYSE 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1141 LSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsvaelgeqidnLQRVKQKLE 1220
Cdd:PRK04778 381 LQEELEEILKQLEEI-----------EKEQEKLSEMLQGLRKDELEAREKLERYRNK--------------LHEIKRYLE 435
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1221 KEK-----SEFKLELDDVTSNMEQiikakanlekvsrtLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTE 1285
Cdd:PRK04778 436 KSNlpglpEDYLEMFFEVSDEIEA--------------LAEELEEKPINMEAVNRLLEEATEDVETLEEE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1670-1911 |
1.12e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1670 KENIAIVERRNNLLQAELEELRAVVEQTERSRKlaeqELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQE 1749
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1750 CRNAEEKAKKaitdaammAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLE---ARVRELEG 1826
Cdd:PRK03918 275 IEELEEKVKE--------LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEE-EINGIEERIKELEekeERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1827 ELEaEQKRNAESVKGMRKSERRIKELTYQTEEDKKNL--LRLQDLVDKLQLKVKAyKRQAEEAEEQANTNLSKFRKVQHE 1904
Cdd:PRK03918 346 KLK-ELEKRLEELEERHELYEEAKAKKEELERLKKRLtgLTPEKLEKELEELEKA-KEEIEEEISKITARIGELKKEIKE 423
|
....*..
gi 124376530 1905 LDEAEER 1911
Cdd:PRK03918 424 LKKAIEE 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1047-1282 |
1.72e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1047 RMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEA 1126
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1127 ERTARAKVEKLRSDLSR--ELEEI--SERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEatlqheatAAALRKKHADSV 1202
Cdd:COG4942 102 QKEELAELLRALYRLGRqpPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE--------LAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1203 AELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSL--NDFTTQRA 1280
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTpaAGFAALKG 253
|
..
gi 124376530 1281 KL 1282
Cdd:COG4942 254 KL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1474-1699 |
2.22e-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: 55.16 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1474 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASL 1553
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1554 EhEEGKILRAQLEFNQIKAEIER-KLAEKDEEMEQAKRN---HQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEI 1629
Cdd:COG4942 100 E-AQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1630 QLshanrmaAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTER 1699
Cdd:COG4942 179 LL-------AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1237-1452 |
2.49e-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: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1237 MEQIIKAK-ANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQR--AKLQTENGELARQLEEKEALISQLTRGKLSYTQQ 1313
Cdd:COG3206 162 LEQNLELRrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1314 MEDLKRQLEEEGKAKNALAHALQSARhdcdlLREQYEEETEAKAELQRVLSKANSEVAQWRtkyetdaiqrtEELEEAKK 1393
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALR-----------AQIAALRA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124376530 1394 KLAQRLQDAEEAVEAVNAkcsSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFD 1452
Cdd:COG3206 306 QLQQEAQRILASLEAELE---ALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1001-1451 |
2.49e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1001 LQEAHQQALDDlQVEEDKVNSLSKSKVKLEQQVDDLEgSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEE 1080
Cdd:COG4717 39 LLAFIRAMLLE-RLEKEADELFKPQGRKPELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1081 KLKKKEFDINQQNSKIEDEQvlalqLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATS 1160
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEA-----LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1161 VQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELgeqidNLQRVKQKLEKEKSEFKL---------ELD 1231
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARLLLLIaaallallgLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1232 DVTSNMEQIIKA--------------KANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKE 1297
Cdd:COG4717 267 SLLSLILTIAGVlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1298 ALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREqYEEETEAKAELQRVLSKANSEVAQWRTKY 1377
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1378 ETDAI-QRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKT---------KHRLQNEIEDLMVDVERSNAAAAALDKK 1447
Cdd:COG4717 426 DEEELeEELEELEEELEELEEELEELREELAELEAELEQLEEDgelaellqeLEELKAELRELAEEWAALKLALELLEEA 505
|
....
gi 124376530 1448 QRNF 1451
Cdd:COG4717 506 REEY 509
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1393-1898 |
3.17e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1393 KKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESS 1472
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1473 QKEARSLSTELFKLKNAYEESLehLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEAS 1552
Cdd:TIGR04523 287 EKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1553 LEHEEGKILRAQLEFNQIKAEIErKLAEKDEEMEQAKRNHQRVVDSLQTSLDaetrsrnevlrvKKKMEGDLNEMEIQLS 1632
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIK------------KLQQEKELLEKEIERL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1633 HANRmaAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETS 1712
Cdd:TIGR04523 432 KETI--IKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1713 ERVQLLHSQNTSLINQKKKMESDLTQLQSEVeeavqecRNAEEKAKKaitdaamMAEELKKEQdtsahLERMKKNMEQTI 1792
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKIEKLESEKKEKESKI-------SDLEDELNK-------DDFELKKEN-----LEKEIDEKNKEI 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1793 KDLQHrldeaEQIALKGGKKQLQKLEArvrelegELEAEQKrnaESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDK 1872
Cdd:TIGR04523 571 EELKQ-----TQKSLKKKQEEKQELID-------QKEKEKK---DLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
490 500
....*....|....*....|....*.
gi 124376530 1873 LQLKVKAYKRQAEEAEEQANTNLSKF 1898
Cdd:TIGR04523 636 IKSKKNKLKQEVKQIKETIKEIRNKW 661
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1543-1939 |
3.23e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1543 QSALEEAEASLEHEEGKILRAQL-EFNQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQTSldAETRSRNEVLrvkkkmE 1621
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEIERYEEQREQARETRDEADEVLEEH--EERREELETL------E 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1622 GDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSR 1701
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1702 KLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVE---EAVQECRNAEEKAKKAITDAAmmaEELKKEQDTS 1778
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEdrrEEIEELEEEIEELRERFGDAP---VDLGNAEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1779 AHLERMKKNMEQTIKDLqhrldEAEqialkggkkqLQKLEARVRELEGELEA-------EQKRNAESVKGMRKSERRIKE 1851
Cdd:PRK02224 415 EELREERDELREREAEL-----EAT----------LRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1852 LTYQTEEDKKNLLRLQDLVDKLQlkvkaykrQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGA 1931
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
|
....*...
gi 124376530 1932 KQKMHDEE 1939
Cdd:PRK02224 552 EAEEKREA 559
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1258-1930 |
3.35e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.73 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1258 ANEYRVKLEEA---QRSLNDFTTQRAKLQTENGELARQLEEKEALISQLtrgklsyTQQMEDLKRQLEeegKAKNALAHA 1334
Cdd:PRK04863 278 ANERRVHLEEAlelRRELYTSRRQLAAEQYRLVEMARELAELNEAESDL-------EQDYQAASDHLN---LVQTALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1335 LQSARHDCDL--LREQYEEETEAKAElqrvlskANSEVAQWRTKYEtdaiQRTEELEEAKKKLA---QRL---------- 1399
Cdd:PRK04863 348 EKIERYQADLeeLEERLEEQNEVVEE-------ADEQQEENEARAE----AAEEEVDELKSQLAdyqQALdvqqtraiqy 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1400 QDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKE---- 1475
Cdd:PRK04863 417 QQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSeawd 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1476 -ARSLSTELFKLKN------AYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEE 1548
Cdd:PRK04863 497 vARELLRRLREQRHlaeqlqQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSE 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1549 AeasleHEEGKILRAQLEfnQIKAEIER-------------KLAEKDEEMEQAKRNHQRVVDSLQTSLDAE---TRSRNE 1612
Cdd:PRK04863 577 A-----RERRMALRQQLE--QLQARIQRlaarapawlaaqdALARLREQSGEEFEDSQDVTEYMQQLLERErelTVERDE 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1613 VLRVKKKMEGDLNEmeiqLSHAN-----RMAAEAQKQVKSLQSLLKDtQIQLDDA---------------VR-------- 1664
Cdd:PRK04863 650 LAARKQALDEEIER----LSQPGgsedpRLNALAERFGGVLLSEIYD-DVSLEDApyfsalygparhaivVPdlsdaaeq 724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1665 --ANDDLKENIAIVER-----RNNLLQAELEElRAVV----------------------------EQTERSRKLAEQELI 1709
Cdd:PRK04863 725 laGLEDCPEDLYLIEGdpdsfDDSVFSVEELE-KAVVvkiadrqwrysrfpevplfgraarekriEQLRAEREELAERYA 803
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1710 ETSERVQL---LHSQNTSLINQKKKM------ESDLTQLQ---SEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT 1777
Cdd:PRK04863 804 TLSFDVQKlqrLHQAFSRFIGSHLAVafeadpEAELRQLNrrrVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPR 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1778 SAHLERmkKNMEQTIKDLQHRLDEAEQ----IALKGGK-KQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKEL 1852
Cdd:PRK04863 884 LNLLAD--ETLADRVEEIREQLDEAEEakrfVQQHGNAlAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL 961
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1853 TYQTE-------EDKKNLL-RLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRA 1924
Cdd:PRK04863 962 TEVVQrrahfsyEDAAEMLaKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQ 1041
|
....*.
gi 124376530 1925 KSRDIG 1930
Cdd:PRK04863 1042 ELQDLG 1047
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1617-1819 |
3.75e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1617 KKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQ 1696
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1697 TERSRKLAE--------QELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQEcrnAEEKAKKAITDAAMMA 1768
Cdd:COG3883 98 SGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 124376530 1769 EELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEA 1819
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1479-1697 |
3.78e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1479 LSTELFKLKNAYEESLEHLETFKRENK--NLQEEISDLTEQLGEggknvheLEKVRKQLEVEKLELQSALEEAEASLEHE 1556
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE-------LESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1557 EGKI--LRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQRVVdSLQTSLDA-ETRSRNEVLRVKKKMEGDLNEMEIQLSH 1633
Cdd:COG3206 253 PDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVI-ALRAQIAAlRAQLQQEAQRILASLEAELEALQAREAS 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124376530 1634 ANRMAAEAQKQVKSLQSLlkdtQIQLddavranDDLKENIAIVERRNNLLQAELEELRAVVEQT 1697
Cdd:COG3206 332 LQAQLAQLEARLAELPEL----EAEL-------RRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
653-677 |
4.31e-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: 51.96 E-value: 4.31e-07
10 20
....*....|....*....|....*
gi 124376530 653 HRENLNKLMTNLRTTHPHFVRCIIP 677
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1128-1870 |
4.90e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1128 RTARAKVEKLRSDLSRELEEISER---LEEAGGATS--VQIEMNKKREAE-FQKMRRDLEEATLQHEATAAAlrkkhads 1201
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELAELNEAesdLEQDYQAASdhLNLVQTALRQQEkIERYQADLEELEERLEEQNEV-------- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1202 VAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNME-------QIIKAKANLEKVSR----------TLEDQANEYRVK 1264
Cdd:PRK04863 371 VEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDvqqtraiQYQQAVQALERAKQlcglpdltadNAEDWLEEFQAK 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1265 LEEAQRSLNDFTT-----QRAKLQTENG---------------------ELARQLEEKEALISQLT--RGKLSytqqmeD 1316
Cdd:PRK04863 451 EQEATEELLSLEQklsvaQAAHSQFEQAyqlvrkiagevsrseawdvarELLRRLREQRHLAEQLQqlRMRLS------E 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1317 LKRQLEEEGKAKNALAHALQSARHDCDLlREQYEEETEAKAELQRVLSKANSEVAQWRTKYEtdaiQRTEELEEAKKKLA 1396
Cdd:PRK04863 525 LEQRLRQQQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEARLESLSESVSEARERRMALR----QQLEQLQARIQRLA 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1397 QR---LQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLmvdVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQ 1473
Cdd:PRK04863 600 ARapaWLAAQDALARLREQSGEEFEDSQDVTEYMQQL---LERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLN 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1474 KEARSLSTELfkLKNAYEE-SLEH-------------------LETFKRENKNLQEEISDL------TEQLGEGGKNVHE 1527
Cdd:PRK04863 677 ALAERFGGVL--LSEIYDDvSLEDapyfsalygparhaivvpdLSDAAEQLAGLEDCPEDLyliegdPDSFDDSVFSVEE 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1528 LEK------VRKQLEVEKLELQSALEEA--EASLEheegkILRAQLEfnqikaEIERKLAEKDEEMEQAKRNHQR----V 1595
Cdd:PRK04863 755 LEKavvvkiADRQWRYSRFPEVPLFGRAarEKRIE-----QLRAERE------ELAERYATLSFDVQKLQRLHQAfsrfI 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1596 VDSLQTSLDAETRSRNEVLRVKK-KMEGDLNEMEIQLSHANRMAAEAQKQVKSLQ------SLLKDTQI---------QL 1659
Cdd:PRK04863 824 GSHLAVAFEADPEAELRQLNRRRvELERALADHESQEQQQRSQLEQAKEGLSALNrllprlNLLADETLadrveeireQL 903
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1660 DDAVRANDDLKEN---IAIVERRNNLLQA---ELEELRAVVEQTERSRKLAEQELIETSERVQLLH----SQNTSLINQk 1729
Cdd:PRK04863 904 DEAEEAKRFVQQHgnaLAQLEPIVSVLQSdpeQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyEDAAEMLAK- 982
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1730 kkmESDLT-QLQSEVEEAVQECRNAEEKAKKA---ITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHRLDEAEQI 1805
Cdd:PRK04863 983 ---NSDLNeKLRQRLEQAEQERTRAREQLRQAqaqLAQYNQVLASLKSSYDA---KRQMLQELKQELQDLGVPADSGAEE 1056
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124376530 1806 ALKGGKKQLQK-----------LEARVRELEGELEAEQKRnaesvkgMRKSERRIKELTYQTEEDKKNLLRLQDLV 1870
Cdd:PRK04863 1057 RARARRDELHArlsanrsrrnqLEKQLTFCEAEMDNLTKK-------LRKLERDYHEMREQVVNAKAGWCAVLRLV 1125
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
842-1058 |
4.96e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 842 LKSAETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLlqeknDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKV 921
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 922 KEMNERLEDEEEMNAELTAkkrklEDECSELKKDIDDLELTLAkvEKEKHATEN--KVKNLTEEMAGLdeiiakltkeKK 999
Cdd:COG3206 243 AALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL----------RA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124376530 1000 ALQEAHQQALDDLQVEedkVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLE 1058
Cdd:COG3206 306 QLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
835-1305 |
4.99e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.91 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 835 YFKIKPLLKSAETE-KEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQA---EQDNLNDAEERCDQL 910
Cdd:PRK01156 168 YDKLKDVIDMLRAEiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNamdDYNNLKSALNELSSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 911 IKNKIQLEAKVKEMNERLEDEEEMNAELTA--------------KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENK 976
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYKEleerhmkiindpvyKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 977 VKNLTEEMAGLDEIIakltkEKKALQEAHQQALDDLQVEEDKVNSLSKS----KVKLE---------------------- 1030
Cdd:PRK01156 328 IKKLSVLQKDYNDYI-----KKKSRYDDLNNQILELEGYEMDYNSYLKSieslKKKIEeyskniermsafiseilkiqei 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1031 ----------------QQVDDLEGSLEQEKKV----RMDLERAKRKLEGDLK-------LTQESIMDL----ENDKLQLE 1079
Cdd:PRK01156 403 dpdaikkelneinvklQDISSKVSSLNQRIRAlrenLDELSRNMEMLNGQSVcpvcgttLGEEKSNHIinhyNEKKSRLE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1080 EKLKKKEFDINQQNSKIEDEQVLALQLQK-----------KLKENQARIEELEEELEAERTARAKVEKLRSDL-SRELEE 1147
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYLESeeinksineynKIESARADLEDIKIKINELKDKHDKYEEIKNRYkSLKLED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1148 ISERLEEAGGATSV----QIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEK 1223
Cdd:PRK01156 563 LDSKRTSWLNALAVisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1224 SEFKlELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQL 1303
Cdd:PRK01156 643 ILIE-KLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDI 721
|
..
gi 124376530 1304 TR 1305
Cdd:PRK01156 722 NE 723
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1217-1707 |
6.58e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1217 QKLEKEKSE-FKLELDDVTSNMEQIIKAKANLekvsRTLEDQANEYRvkleEAQRSLNDFTTQRAKLQTENGELARQLEE 1295
Cdd:COG4717 49 ERLEKEADElFKPQGRKPELNLKELKELEEEL----KEAEEKEEEYA----ELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1296 KEALISQLtrgklSYTQQMEDLKRQLEEEGKAKNALAHALQSARHdcdlLREQYEEETEAKAELQRVLSKANSEVAQWRT 1375
Cdd:COG4717 121 LEKLLQLL-----PLYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1376 KYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTK--HRLQNEIEDLMVDVERSNAAAAALDKKQRNFDK 1453
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEARLLLLIAAALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1454 ILAEWKQKYEESQSELEssqkearsLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLG-EGGKNVHELEKVR 1532
Cdd:COG4717 272 ILTIAGVLFLVLGLLAL--------LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1533 KQLEvEKLELQSALEEAEASLEHEEGKILRAQLeFNQIKAEIERKLAEKDEEMEQAKRNHQRVvDSLQTSLDAETRSRNE 1612
Cdd:COG4717 344 DRIE-ELQELLREAEELEEELQLEELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQELKEEL-EELEEQLEELLGELEE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1613 VLRvkkkmEGDLNEMEIQLSHANRMAAEAQKQVKSLQsllkdtqiqlddavranddlkeniaiverrnnllqAELEELRA 1692
Cdd:COG4717 421 LLE-----ALDEEELEEELEELEEELEELEEELEELR-----------------------------------EELAELEA 460
|
490
....*....|....*
gi 124376530 1693 VVEQTERSRKLAEQE 1707
Cdd:COG4717 461 ELEQLEEDGELAELL 475
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
855-1057 |
6.84e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 855 KEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEM 934
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 935 NAELTAKKRKLEDECS-------------------------ELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDE 989
Cdd:COG4942 106 LAELLRALYRLGRQPPlalllspedfldavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 990 IIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQ--EKKVRMDLERAKRKL 1057
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAaaERTPAAGFAALKGKL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
863-1095 |
8.08e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 863 ETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLedeeemnAELTAKK 942
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------AELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 943 RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSL 1022
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124376530 1023 SKSKVKLEQQVDDLEGSLEQEKKVRmdlERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSK 1095
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1258-1938 |
9.15e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1258 ANEYRVKLEEAQRSLNDFTTQRAKLQTEN---GELARQLEEKEALISQLTrgklsytqqmEDLKRQLEEEGKAKNALAHA 1334
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQyrlVEMARELEELSARESDLE----------QDYQAASDHLNLVQTALRQQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1335 LQSARHDCDLlreqyEEETEAKAELQRVLSKANSEVAQwrtkYETDAIQRTEELEEAKKKLA--QRLQDAEE--AV---E 1407
Cdd:COG3096 347 EKIERYQEDL-----EELTERLEEQEEVVEEAAEQLAE----AEARLEAAEEEVDSLKSQLAdyQQALDVQQtrAIqyqQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1408 AVNAkcssLEKTKHRLQneIEDLMVDversNAAA--AALDKKQRNFDKILAEWKQKyeesqselESSQKEARSLSTELFK 1485
Cdd:COG3096 418 AVQA----LEKARALCG--LPDLTPE----NAEDylAAFRAKEQQATEEVLELEQK--------LSVADAARRQFEKAYE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1486 L----------KNAYEESLEHLETFkRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQ-----------------LEVE 1538
Cdd:COG3096 480 LvckiageverSQAWQTARELLRRY-RSQQALAQRLQQLRAQLAELEQRLRQQQNAERLleefcqrigqqldaaeeLEEL 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1539 KLELQSALEEAEASL-EHEEGKI-LRAQLEfnQIKAEIER-------------KLAEKDEEMEQAKRNHQRVVDSLQTSL 1603
Cdd:COG3096 559 LAELEAQLEELEEQAaEAVEQRSeLRQQLE--QLRARIKElaarapawlaaqdALERLREQSGEALADSQEVTAAMQQLL 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1604 DAE---TRSRNEVLRVKKKMEGDLNEmeiqLSHAN-----RMAAEAQKQVKSLQSLLKDtQIQLDDA------------- 1662
Cdd:COG3096 637 EREreaTVERDELAARKQALESQIER----LSQPGgaedpRLLALAERLGGVLLSEIYD-DVTLEDApyfsalygparha 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1663 ------------VRANDDLKENIAIVERR-----NNLLQAELEELRAVVEQTERS-------------RKLAEQELIETS 1712
Cdd:COG3096 712 ivvpdlsavkeqLAGLEDCPEDLYLIEGDpdsfdDSVFDAEELEDAVVVKLSDRQwrysrfpevplfgRAAREKRLEELR 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1713 ERVQLLHSQNTSLINQKKKME--------------------------SDLTQLQSEVEEAVQECRNAEEKAKKAITDAAM 1766
Cdd:COG3096 792 AERDELAEQYAKASFDVQKLQrlhqafsqfvgghlavafapdpeaelAALRQRRSELERELAQHRAQEQQLRQQLDQLKE 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1767 MAEELKKEQDTSAHLErmKKNMEQTIKDLQHRLDEAEQ----IALKGgkKQLQKLEARVRELEG-------------ELE 1829
Cdd:COG3096 872 QLQLLNKLLPQANLLA--DETLADRLEELREELDAAQEaqafIQQHG--KALAQLEPLVAVLQSdpeqfeqlqadylQAK 947
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1830 AEQKRNAESVKGMRKSERRIKELTYQTEEDKknLLRLQDLVDKLQLKVkaykRQAEEAEEQANTNLskfRKVQHELDEAE 1909
Cdd:COG3096 948 EQQRRLKQQIFALSEVVQRRPHFSYEDAVGL--LGENSDLNEKLRARL----EQAEEARREAREQL---RQAQAQYSQYN 1018
|
810 820
....*....|....*....|....*....
gi 124376530 1910 ERADIAESqvnklrakSRDigAKQKMHDE 1938
Cdd:COG3096 1019 QVLASLKS--------SRD--AKQQTLQE 1037
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1141-1793 |
1.06e-06 |
|
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: 54.06 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1141 LSRELEEISERLEEaggaTSVQIEMNKKR-EAEFQKMRRDLEeaTLQHEATAAALRKKHADSVAELGE---QIDNLQRVK 1216
Cdd:pfam10174 128 QAKELFLLRKTLEE----MELRIETQKQTlGARDESIKKLLE--MLQSKGLPKKSGEEDWERTRRIAEaemQLGHLEVLL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1217 QKLEKEKSEFKLEL---------DDVTSNMEQIIKAK----ANLEKVSRTLEDQAN-------------EYRVKLEEAQR 1270
Cdd:pfam10174 202 DQKEKENIHLREELhrrnqlqpdPAKTKALQTVIEMKdtkiSSLERNIRDLEDEVQmlktngllhtedrEEEIKQMEVYK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1271 SLNDFttqrakLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLE---EEGKAKNALAHALQSarhDCDLLRE 1347
Cdd:pfam10174 282 SHSKF------MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEvlkESLTAKEQRAAILQT---EVDALRL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1348 QYEEEteakaelQRVLSKansevaqwrtkyETDAIQRteeLEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEI 1427
Cdd:pfam10174 353 RLEEK-------ESFLNK------------KTKQLQD---LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1428 EDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKyEESQSELESSQKEARSLSTElfklknayeESLEHLETFKRENKNL 1507
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEA-LSEKERIIERLKEQREREDR---------ERLEELESLKKENKDL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1508 QEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEH--EEGKILRAQLEFNQIKAEIERKLAEKDEEM 1585
Cdd:pfam10174 481 KEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQkkEECSKLENQLKKAHNAEEAVRTNPEINDRI 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1586 EQAKRNHQRVVDS---LQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQ-LDD 1661
Cdd:pfam10174 561 RLLEQEVARYKEEsgkAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQlLEE 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1662 AVRANDDLKENIAiverrnnllQAELEELRAVVEQTersrklaEQELIETSERV----QLLHSQNTSLINQKKKMESDLt 1737
Cdd:pfam10174 641 ARRREDNLADNSQ---------QLQLEELMGALEKT-------RQELDATKARLsstqQSLAEKDGHLTNLRAERRKQL- 703
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 124376530 1738 qlqSEVEEAVQECRNAEEKAKKA-ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIK 1793
Cdd:pfam10174 704 ---EEILEMKQEALLAAISEKDAnIALLELSSSKKKKTQEEVMALKREKDRLVHQLK 757
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1527-1743 |
1.07e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1527 ELEKVRKQLEVEKLELQSALEEAEASLEH-----------EEGKILRAQLefnqikAEIERKLAEKDEEMEQAKRNHQRV 1595
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlsEEAKLLLQQL------SELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1596 VDSLQTSLDAETR-SRNEVLRvkkKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAV-RANDDLKENI 1673
Cdd:COG3206 246 RAQLGSGPDALPElLQSPVIQ---QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAqRILASLEAEL 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1674 AIVERRNNLLQAELEELRAVVEQTERsrklAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEV 1743
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
923-1341 |
1.17e-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: 53.15 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 923 EMNERLEDEEEMNAELTAKKRKLEDECSEL---KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKK 999
Cdd:pfam19220 14 EMADRLEDLRSLKADFSQLIEPIEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1000 ALQEAHQQAldDLQVEEDKVNSLSKskvklEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLE 1079
Cdd:pfam19220 94 KLEAALREA--EAAKEELRIELRDK-----TAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1080 EKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARieeleeeleaERTARAKVEKLRSDLSRELEEiSERLEEAggat 1159
Cdd:pfam19220 167 ERLALLEQENRRLQALSEEQAAELAELTRRLAELETQ----------LDATRARLRALEGQLAAEQAE-RERAEAQ---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1160 svQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQ 1239
Cdd:pfam19220 232 --LEEAVEAHRAERASLRMKLEALTARAAATEQLLAEA-RNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1240 IIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKealisqltrgKLSYTQQMEDLKR 1319
Cdd:pfam19220 309 RTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVE----------RAALEQANRRLKE 378
|
410 420
....*....|....*....|...
gi 124376530 1320 QLEEEgKAKNALAH-ALQSARHD 1341
Cdd:pfam19220 379 ELQRE-RAERALAQgALEIARES 400
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
865-1021 |
1.34e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 865 LEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLE-DEEEMNAELTAKkr 943
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYEEQLGNVRNNK-- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124376530 944 kledECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNS 1021
Cdd:COG1579 90 ----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1242-1923 |
1.37e-06 |
|
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: 53.69 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1242 KAKANLEKVSRTLED-QA----NEYRVKLEEAQRSLNDFTTQRAKLQTENGEL-------ARQLEEKEALISQLTRGKLS 1309
Cdd:pfam12128 215 KSRLNRQQVEHWIRDiQAiagiMKIRPEFTKLQQEFNTLESAELRLSHLHFGYksdetliASRQEERQETSAELNQLLRT 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1310 YTQQMEDLKRQLEEEGKAKNAlahALQSARHDCDLLREQYEEETEAKAElqrVLSKANSEVAQWRTKyetdaiqrTEELE 1389
Cdd:pfam12128 295 LDDQWKEKRDELNGELSAADA---AVAKDRSELEALEDQHGAFLDADIE---TAAADQEQLPSWQSE--------LENLE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1390 EAKKKLAQRLQDAEEAVEAVNAKCSSlektkhRLQNEIEDLMVDVERSNAAAAALDKKQRN-FDKILAEWKQKYEESQSE 1468
Cdd:pfam12128 361 ERLKALTGKHQDVTAKYNRRRSKIKE------QNNRDIAGIKDKLAKIREARDRQLAVAEDdLQALESELREQLEAGKLE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1469 LESSQKEARSLSTELFKLKN---AYEESLEHLETFkrenknlQEEISDLTEQLGEGGKNVHELEKVRKQL---------- 1535
Cdd:pfam12128 435 FNEEEYRLKSRLGELKLRLNqatATPELLLQLENF-------DERIERAREEQEAANAEVERLQSELRQArkrrdqasea 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1536 ----EVEKLELQSALEEAEASLEHEEGKIL-----RAQLEFNQIKAEIERKLAEK---DEEMEQAKRNHQRVVDSLQtsL 1603
Cdd:pfam12128 508 lrqaSRRLEERQSALDELELQLFPQAGTLLhflrkEAPDWEQSIGKVISPELLHRtdlDPEVWDGSVGGELNLYGVK--L 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1604 DAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRAnddLKENIAIVERRNNLL 1683
Cdd:pfam12128 586 DLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA---LKNARLDLRRLFDEK 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1684 QAELeelRAVVEQTERSRKLAEqelietsERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAiTD 1763
Cdd:pfam12128 663 QSEK---DKKNKALAERKDSAN-------ERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDA-QL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1764 AAMMAEELKKEQDTSAHLERMKKNMEqtiKDLQHRLDEAEQIAlkggkkqlqKLEARVRELEGELEAEQKRNAESVKGMR 1843
Cdd:pfam12128 732 ALLKAAIAARRSGAKAELKALETWYK---RDLASLGVDPDVIA---------KLKREIRTLERKIERIAVRRQEVLRYFD 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1844 KSERRI----KELTYQTEEDKKNLLRLQDLVDKLQLKVKAyKRQAEEAEEQANtnlskfRKVQHELDEAEERADIAESQV 1919
Cdd:pfam12128 800 WYQETWlqrrPRLATQLSNIERAISELQQQLARLIADTKL-RRAKLEMERKAS------EKQQVRLSENLRGLRCEMSKL 872
|
....
gi 124376530 1920 NKLR 1923
Cdd:pfam12128 873 ATLK 876
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1256-1457 |
1.39e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1256 DQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHAL 1335
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1336 QSARHD-CDLLREQYEEETEAKAELqrVLSKANSEVAQWRTKY----------ETDAIQRT-EELEEAKKKLAQRLQDAE 1403
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYlkylaparreQAEELRADlAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124376530 1404 EAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAE 1457
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
837-1012 |
1.42e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 837 KIKPLLKSAETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLiKNKIQ 916
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY-EEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 917 LEAKVKEMnERLEDEEEMnaeLTAKKRKLEDECSELKKDIDDLELTLAKVEKEKhatENKVKNLTEEMAGLDEIIAKLTK 996
Cdd:COG1579 84 NVRNNKEY-EALQKEIES---LKRRISDLEDEILELMERIEELEEELAELEAEL---AELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*.
gi 124376530 997 EKKALQEAHQQALDDL 1012
Cdd:COG1579 157 ELEELEAEREELAAKI 172
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1483-1929 |
1.68e-06 |
|
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: 52.93 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1483 LFKLKNAYEEsLEHLETFKRE--NKNLQEEISDLtEQLGEGGKNVHELEKVRKQ----LEVEKLELQSALEEAEASLEhe 1556
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1557 egkilraqlEFNQIKAEieRKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKK----------------- 1619
Cdd:pfam06160 78 ---------KYRFKKAK--KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKyrelrktllanrfsygp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1620 ----MEGDLNEMEIQLSHA-NRMAA----EAQKQVKSLQSLLKDTQIQLDDavranddlkenI-AIVERRNNLLQAELEE 1689
Cdd:pfam06160 147 aideLEKQLAEIEEEFSQFeELTESgdylEAREVLEKLEEETDALEELMED-----------IpPLYEELKTELPDQLEE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1690 LRAVVEQTERSR-KLAEQELIETSERVQLLHSQNTSLINQK--KKMESDLTQLQSEVEEaVQECRNAEEKAKKaitdaam 1766
Cdd:pfam06160 216 LKEGYREMEEEGyALEHLNVDKEIQQLEEQLEENLALLENLelDEAEEALEEIEERIDQ-LYDLLEKEVDAKK------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1767 maeELKKEQDT-SAHLERMKKNMEQTIKDLQH-----RLDEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVK 1840
Cdd:pfam06160 288 ---YVEKNLPEiEDYLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1841 GMRKSERRIKELTYQTEEDKKNL-------LRLQDLVDKLQLKVKAYKRQAE----------------EAEEQANTNLSK 1897
Cdd:pfam06160 365 ELEEILEQLEEIEEEQEEFKESLqslrkdeLEAREKLDEFKLELREIKRLVEksnlpglpesyldyffDVSDEIEDLADE 444
|
490 500 510
....*....|....*....|....*....|..
gi 124376530 1898 FRKVQHELDEAEERADIAESQVNKLRAKSRDI 1929
Cdd:pfam06160 445 LNEVPLNMDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
957-1369 |
1.95e-06 |
|
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: 53.30 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 957 DDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLsksKVKLEQQVDDL 1036
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSE---KDKKNKALAER 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1037 EGSLEQEkkvRMDLERAKRKLEGDLKLTQESIMD-LENDKLQLEEKLKKKEFDINQQNSKIeDEQVLALQLQKKlkenqA 1115
Cdd:pfam12128 677 KDSANER---LNSLEAQLKQLDKKHQAWLEEQKEqKREARTEKQAYWQVVEGALDAQLALL-KAAIAARRSGAK-----A 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1116 RIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHE----ATA 1191
Cdd:pfam12128 748 ELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERI-----------AVRRQEVLRYFDWYQETWLQRRprlaTQL 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1192 AALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEqiiKAKANLEKVSRTLEDQ-ANEYRVKLEEAQR 1270
Cdd:pfam12128 817 SNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLR---GLRCEMSKLATLKEDAnSEQAQGSIGERLA 893
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1271 SLNDFttqRAKLQTENGELARQLEEKEALISQLTRGKLSYTqqMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYE 1350
Cdd:pfam12128 894 QLEDL---KLKRDYLSESVKKYVEHFKNVIADHSGSGLAET--WESLREEDHYQNDKGIRLLDYRKLVPYLEQWFDVRVP 968
|
410
....*....|....*....
gi 124376530 1351 EETEAKAELQRVLSKANSE 1369
Cdd:pfam12128 969 QSIMVLREQVSILGVDLTE 987
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1280-1699 |
1.98e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.59 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1280 AKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAEL 1359
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1360 qrvlskanSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSna 1439
Cdd:pfam07888 114 --------SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT-- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1440 aaaaldkkqrnfdkilaewkqkyeesqselessQKEARSLSTELFKLKNAYEESLEHLETfkrenknLQEEISDLTEQLG 1519
Cdd:pfam07888 184 ---------------------------------EEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1520 EGGKNVHELEKVRKQLEV--EKLE--------LQSALEEAEASLEHEEGKILRAQLEfnqiKAEIERKLAEKDEEMEQAK 1589
Cdd:pfam07888 224 TAHRKEAENEALLEELRSlqERLNaserkvegLGEELSSMAAQRDRTQAELHQARLQ----AAQLTLQLADASLALREGR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1590 RNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEmeiqlshaNRMaaEAQKQVKSLQSLLKDTQIQLDDAVRANDDL 1669
Cdd:pfam07888 300 ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE--------ERM--EREKLEVELGREKDCNRVQLSESRRELQEL 369
|
410 420 430
....*....|....*....|....*....|
gi 124376530 1670 KENIAIVERRNNLLQAELEELRAVVEQTER 1699
Cdd:pfam07888 370 KASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1353-1589 |
2.17e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1353 TEAKAELQRVLSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMv 1432
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE--------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1433 dvERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEIS 1512
Cdd:COG4942 90 --KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124376530 1513 DLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAK 1589
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1187-1911 |
2.90e-06 |
|
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: 52.53 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1187 HEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLe 1266
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDEL- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1267 eaqrslndfttqRAKLQTENGELARQLEEKEALisqltrgklsytqqmEDLKRQLEEEGKAKNAL-AHALQSARHDCDLL 1345
Cdd:pfam12128 307 ------------NGELSAADAAVAKDRSELEAL---------------EDQHGAFLDADIETAAAdQEQLPSWQSELENL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1346 REQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEA-----VNAKCSSLEKTK 1420
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESelreqLEAGKLEFNEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1421 HRLQNEIEDLMVdveRSNAAAAALDKK--QRNFDKILAEWKQKyeesqseLESSQKEARSLSTELFKLKNAYEESLEHLe 1498
Cdd:pfam12128 440 YRLKSRLGELKL---RLNQATATPELLlqLENFDERIERAREE-------QEAANAEVERLQSELRQARKRRDQASEAL- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1499 tfKRENKNLQEEISdlteqlgeggknvhELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLefnqikaeierkL 1578
Cdd:pfam12128 509 --RQASRRLEERQS--------------ALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPEL------------L 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1579 AEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQ 1658
Cdd:pfam12128 561 HRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASRE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1659 LDDAVRAnddLKENIAIVERRNNLLQAeleELRAVVEQTERSRKLAEQELIE-TSERVQLLHSQNTSLINQKKKMESDLT 1737
Cdd:pfam12128 641 ETFARTA---LKNARLDLRRLFDEKQS---EKDKKNKALAERKDSANERLNSlEAQLKQLDKKHQAWLEEQKEQKREART 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1738 QLQS---EVEEA-------VQECRNAEEKAKKAITDA--AMMAEELKK---EQDTSAHLERMKKNMEQTIKDLQHRLDEA 1802
Cdd:pfam12128 715 EKQAywqVVEGAldaqlalLKAAIAARRSGAKAELKAleTWYKRDLASlgvDPDVIAKLKREIRTLERKIERIAVRRQEV 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1803 EQ----------IALKGGKKQLQKLEARVRELEGELeaeqKRNAESVKGMRKS-ERRIKELTYQTEEDKKNLLRLQDLVD 1871
Cdd:pfam12128 795 LRyfdwyqetwlQRRPRLATQLSNIERAISELQQQL----ARLIADTKLRRAKlEMERKASEKQQVRLSENLRGLRCEMS 870
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 124376530 1872 KL-QLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEER 1911
Cdd:pfam12128 871 KLaTLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKK 911
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1670-1939 |
3.17e-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: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1670 KENIAIVE--RRNNLLQAELEELRAVVEQ-------TERsRKLAEQELIETSERVQLLHSQNTSLINQKKKMesdltQLQ 1740
Cdd:TIGR02168 135 KRSYSIIEqgKISEIIEAKPEERRAIFEEaagiskyKER-RKETERKLERTRENLDRLEDILNELERQLKSL-----ERQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1741 SEVEEAVQECRNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEAR 1820
Cdd:TIGR02168 209 AEKAERYKELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEELRLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1821 VRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLV-------DKLQLKVKAYKRQAEEAEEQANT 1893
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLeelesklDELAEELAELEEKLEELKEELES 355
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 124376530 1894 NLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKQKMHDEE 1939
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1505-1929 |
4.92e-06 |
|
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: 51.75 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1505 KNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALE-EAEASLEHEEGKILRAQLEFNQIK-AEIERKLAEKD 1582
Cdd:pfam10174 174 KKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHrRNQLQPDPAKTKALQTVIEMKDTKiSSLERNIRDLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1583 EEmeqakrnhqrvVDSLQTSLDAETRSRNEvlrvkkkmegDLNEMEIQLSHANRMA-------AEAQK---QVKSLQSLL 1652
Cdd:pfam10174 254 DE-----------VQMLKTNGLLHTEDREE----------EIKQMEVYKSHSKFMKnkidqlkQELSKkesELLALQTKL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1653 KDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQ-----TERSRKLAE---------------QELIETS 1712
Cdd:pfam10174 313 ETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEkesflNKKTKQLQDlteekstlageirdlKDMLDVK 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1713 ER-VQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEekakkaiTDAAMMAEELKKEQDTsahLERMKknmEQT 1791
Cdd:pfam10174 393 ERkINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTD-------TALTTLEEALSEKERI---IERLK---EQR 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1792 IKDLQHRLDEAEQI--ALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDL 1869
Cdd:pfam10174 460 EREDRERLEELESLkkENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQ 539
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1870 VDKLQlkvkaykrQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1929
Cdd:pfam10174 540 LKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREV 591
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1155-1384 |
5.14e-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: 50.92 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1155 AGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAAlRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVT 1234
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1235 SNMEQIIKA----KANLEKVSRTLEDQANEYRVKL-------EEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQL 1303
Cdd:COG4942 90 KEIAELRAEleaqKEELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1304 TRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQ 1383
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
.
gi 124376530 1384 R 1384
Cdd:COG4942 250 A 250
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
931-1426 |
8.25e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 931 EEEMNAELTAKKRKLEDECSELKKDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALqEAHQQALD 1010
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1011 DLQVEEDKVNSLSKSKVKLEQqvddlegsLEQEKKVRMDLERAKRKLEGDLKLTQESI-MDLENDKLQLEEKLKKKEFDI 1089
Cdd:COG4717 130 LYQELEALEAELAELPERLEE--------LEERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1090 NQQNSKIEDEQVLALQLQKKLKENQARIEELeeeleaertaraKVEKLRSDLSRELEEISERLeeAGGATSVQIEMNKKR 1169
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQL------------ENELEAAALEERLKEARLLL--LIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1170 EAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVK----QKLEKEKSEFKLELDDVTSNMEQIIKAKA 1245
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEeleeEELEELLAALGLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1246 NLEKVSRTLEDQANEYRVKLEEAQRSlNDFTTQRAKLQTENGELARQLEEKEALisqltrgklsyTQQMEDLKRQLEEEG 1325
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEEYQEL-----------KEELEELEEQLEELL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1326 KAKNALAhalqsARHDCDLLREQYEEETEAKAELQRVLSKANSEVAqwRTKYETDAIQRTEELEEAKKKLAQRLQDAEEA 1405
Cdd:COG4717 416 GELEELL-----EALDEEELEEELEELEEELEELEEELEELREELA--ELEAELEQLEEDGELAELLQELEELKAELREL 488
|
490 500
....*....|....*....|....
gi 124376530 1406 VEAVNAKC---SSLEKTKHRLQNE 1426
Cdd:COG4717 489 AEEWAALKlalELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
971-1225 |
8.29e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 971 HATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQekkvrmdL 1050
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1051 ERAKRKLEGDLKLTQESIMDLeNDKLQLEEKLKKKEFDINQQNSkieDEQVLALQLQKKLkeNQARieeleeeleaerta 1130
Cdd:COG4942 89 EKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDF---LDAVRRLQYLKYL--APAR-------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1131 RAKVEKLRSDLsRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsVAELGEQID 1210
Cdd:COG4942 149 REQAEELRADL-AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE----LAELQQEAE 223
|
250
....*....|....*
gi 124376530 1211 NLQRVKQKLEKEKSE 1225
Cdd:COG4942 224 ELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1439-1679 |
8.51e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1439 AAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQl 1518
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1519 geggknvheLEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERklaekdeeMEQAKRNHQRVVDS 1598
Cdd:COG4942 92 ---------IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY--------LKYLAPARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1599 LQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVER 1678
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
.
gi 124376530 1679 R 1679
Cdd:COG4942 235 E 235
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
938-1410 |
1.54e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 938 LTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT---KEKKALQEAHQQALDDLQV 1014
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSsleDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1015 EEDKVNSLSKSKVKLEQQVDD--------------LEGSLEQEKKVRMDLERAKRKLEGDLKltqeSIMDLENDKLQLEE 1080
Cdd:PRK01156 268 ELEKNNYYKELEERHMKIINDpvyknrnyindyfkYKNDIENKKQILSNIDAEINKYHAIIK----KLSVLQKDYNDYIK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1081 KLKKKEfDINQQNSKIEDEQVLALQL-----QKKLKENQARIEELEEELEAERTARaKVEKLRSDLSRELEEISERLEE- 1154
Cdd:PRK01156 344 KKSRYD-DLNNQILELEGYEMDYNSYlksieSLKKKIEEYSKNIERMSAFISEILK-IQEIDPDAIKKELNEINVKLQDi 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1155 AGGATSVQIEMNKKREAEfQKMRRDLEE----------ATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKS 1224
Cdd:PRK01156 422 SSKVSSLNQRIRALRENL-DELSRNMEMlngqsvcpvcGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIV 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1225 EFKLELDDVTSN--------MEQIIKAKANLEKVSRTL----------EDQANEYR-VKLEE------------AQRSLN 1273
Cdd:PRK01156 501 DLKKRKEYLESEeinksineYNKIESARADLEDIKIKInelkdkhdkyEEIKNRYKsLKLEDldskrtswlnalAVISLI 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1274 DFTTQRAKLQTENGEL---ARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYE 1350
Cdd:PRK01156 581 DIETNRSRSNEIKKQLndlESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIA 660
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124376530 1351 EETEAKAELQRV-----------------LSKANSEVAQWRTKYETDaIQRTEELEEAKKKLAQRLQDAEEAVEAVN 1410
Cdd:PRK01156 661 EIDSIIPDLKEItsrindiednlkksrkaLDDAKANRARLESTIEIL-RTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
936-1160 |
1.70e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 936 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQVE 1015
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1016 EDKVNSL-----SKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEfdin 1090
Cdd:COG3883 99 GGSVSYLdvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE---- 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1091 qqnSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATS 1160
Cdd:COG3883 175 ---AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1383-1613 |
1.72e-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: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1383 QRTEELEEAKKKLAQ---RLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWK 1459
Cdd:COG4942 24 EAEAELEQLQQEIAElekELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1460 QKYeesQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLgeggknvHELEKVRKQLEVEK 1539
Cdd:COG4942 104 EEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-------AELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124376530 1540 LELQSALEEAEAslehEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEV 1613
Cdd:COG4942 174 AELEALLAELEE----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
845-1008 |
1.86e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 845 AETEKEMATMKEEfgrIKETLEKSEARRKELEEKMVSLLQEKNDLQ-LQVQAEQDNLNDAEERCDQLikNKIqleakVKE 923
Cdd:COG3883 61 EALQAEIDKLQAE---IAEAEAEIEERREELGERARALYRSGGSVSyLDVLLGSESFSDFLDRLSAL--SKI-----ADA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 924 MNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQE 1003
Cdd:COG3883 131 DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
....*
gi 124376530 1004 AHQQA 1008
Cdd:COG3883 211 AAAAA 215
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
856-1408 |
1.87e-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: 50.05 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 856 EEFGRIKETLEKSEarrKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNK--IQLEAKVKEMNERLEDEEE 933
Cdd:TIGR01612 1111 DEINKIKDDIKNLD---QKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDdpEEIEKKIENIVTKIDKKKN 1187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 934 MNAELtakkRKLEDECSELKKDIDDLE---------------LTLAKVEKEKHATENKVKNLTEEMAGLDEIiakltKEK 998
Cdd:TIGR01612 1188 IYDEI----KKLLNEIAEIEKDKTSLEevkginlsygknlgkLFLEKIDEEKKKSEHMIKAMEAYIEDLDEI-----KEK 1258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 999 KALQEAHQQALDDLQVEEDKVNsLSKSKVK---LEQQVDDLEGSLEQEKKVRM--------DLERAKRKLEGDLKLTQE- 1066
Cdd:TIGR01612 1259 SPEIENEMGIEMDIKAEMETFN-ISHDDDKdhhIISKKHDENISDIREKSLKIiedfseesDINDIKKELQKNLLDAQKh 1337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1067 ---------------SIMDLENDKlQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKEN------QARIEELEEELE 1125
Cdd:TIGR01612 1338 nsdinlylneianiyNILKLNKIK-KIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDinleecKSKIESTLDDKD 1416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1126 AERTARaKVEKLRSDLSRELEEISERLEEAGGATS------VQIEMNKKREAEFQKMRRDleEATLQHEATAAALrKKHA 1199
Cdd:TIGR01612 1417 IDECIK-KIKELKNHILSEESNIDTYFKNADENNEnvlllfKNIEMADNKSQHILKIKKD--NATNDHDFNINEL-KEHI 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1200 DSVAELGEQIDnlqRVKQKLEKEKSEFKLELDDVTSNMEQ---------IIKAKANLEKVSRTLEDQANEYRVKLEEAQR 1270
Cdd:TIGR01612 1493 DKSKGCKDEAD---KNAKAIEKNKELFEQYKKDVTELLNKysalaiknkFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQ 1569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1271 SLNDFTTQRAKLQTENGELARQ-------------LEEKEALISQLTRGKLSYTQQMEDLKRQ------------LEEEG 1325
Cdd:TIGR01612 1570 KIKEIKKEKFRIEDDAAKNDKSnkaaidiqlslenFENKFLKISDIKKKINDCLKETESIEKKissfsidsqdteLKENG 1649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1326 KAKNALAHALQSarhdcdlLREQYEEETEAKAELQRVLSKANS---EVAQWRTKYETDAIQRTEELEEAKKklaQRLQDA 1402
Cdd:TIGR01612 1650 DNLNSLQEFLES-------LKDQKKNIEDKKKELDELDSEIEKieiDVDQHKKNYEIGIIEKIKEIAIANK---EEIESI 1719
|
....*.
gi 124376530 1403 EEAVEA 1408
Cdd:TIGR01612 1720 KELIEP 1725
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1474-1603 |
1.88e-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: 48.00 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1474 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDL-------TEQLGEGGKN------VHELEKVRKQ---LEV 1537
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearikkyEEQLGNVRNNkeyealQKEIESLKRRisdLED 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124376530 1538 EKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQTSL 1603
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1145-1580 |
1.88e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1145 LEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQRVKQKLEK--- 1221
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEKllq 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1222 ------EKSEFKLELDDVTSNMEQI---IKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAK-LQTENGELAR 1291
Cdd:COG4717 127 llplyqELEALEAELAELPERLEELeerLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQdLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1292 QLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGK----AKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKAN 1367
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALeerlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1368 SEVAQWRTKYETDAIQRTEELE--EAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALD 1445
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQalPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1446 KKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKREN--KNLQEEISDLTEQLgeggk 1523
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEEL----- 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 124376530 1524 nvHELEKVRKQLEVEKLELQSALEEAEaslehEEGKILRAQLEFNQIKAEIERKLAE 1580
Cdd:COG4717 442 --EELEEELEELREELAELEAELEQLE-----EDGELAELLQELEELKAELRELAEE 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1434-1836 |
2.20e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1434 VERSNAAAAALDKKQRNFDKILAEwKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEhLETFKRENKNLQEEISD 1513
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1514 LTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQ 1593
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1594 RVVDSLQTSLDAETRSRNEVL------------RVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDD 1661
Cdd:COG4717 231 QLENELEAAALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1662 AVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQ--ELIETSERVQLLHSQNTSLINQKKKMESDLTQL 1739
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1740 QSEVEEAVQ---ECRNAEEKAKKAITDAAMMAEELKKEQ--DTSAHLERMKKNMEQTIKDLQHRLDEAE-QIALKGGKKQ 1813
Cdd:COG4717 391 LEQAEEYQElkeELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEELEEELEELREELAELEaELEQLEEDGE 470
|
410 420
....*....|....*....|...
gi 124376530 1814 LQKLEARVRELEGELEAEQKRNA 1836
Cdd:COG4717 471 LAELLQELEELKAELRELAEEWA 493
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1253-1411 |
2.24e-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: 48.00 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1253 TLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAK--NA 1330
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1331 LAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVN 1410
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
.
gi 124376530 1411 A 1411
Cdd:COG1579 174 P 174
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1134-1426 |
2.51e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.35 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1134 VEKLRSDLSRELEEISERLEEAggatsvQIEMNKKREAEFQKMRRDLEEATLQHEAT---AAALRKKHADSVAELGEQID 1210
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQE------RLRQEKEEKAREVERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERERELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1211 NLQRVKQKLEKEK---SEFKLELDDVTSNMEQIIKAKANLEKVSRTLEdQANEYRVKLEEAQRSLNDFTTQRAKLQTENg 1287
Cdd:pfam17380 352 RIRQEERKRELERirqEEIAMEISRMRELERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIRAEQ- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1288 ELARQL------EEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAE--- 1358
Cdd:pfam17380 430 EEARQRevrrleEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQami 509
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124376530 1359 --------LQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNE 1426
Cdd:pfam17380 510 eeerkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESE 585
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1131-1430 |
2.87e-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: 49.57 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1131 RAKVEKLRSDLSRELEEISERLEEAggATSVQiemnkkreaEFQKMRRDLEEATLQH---------EATAAALRKKHADS 1201
Cdd:COG3096 780 RAAREKRLEELRAERDELAEQYAKA--SFDVQ---------KLQRLHQAFSQFVGGHlavafapdpEAELAALRQRRSEL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1202 VAELGEQIDNLQRVKQKLEKEKSEFKL------------------ELDDVTSNMEQIIKAKANLEKVSRTLEdqaneyrv 1263
Cdd:COG3096 849 ERELAQHRAQEQQLRQQLDQLKEQLQLlnkllpqanlladetladRLEELREELDAAQEAQAFIQQHGKALA-------- 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1264 KLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLT-----RGKLSYtqqmEDLKRQLEEEGKAKNALAHALQSA 1338
Cdd:COG3096 921 QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSevvqrRPHFSY----EDAVGLLGENSDLNEKLRARLEQA 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1339 RHDCDLLREQYEEETEAKAELQRVLSKANSevaQWRTKYET--DAIQRTEELE-----EAKKKLAQRLQDAEEAVEAVNA 1411
Cdd:COG3096 997 EEARREAREQLRQAQAQYSQYNQVLASLKS---SRDAKQQTlqELEQELEELGvqadaEAEERARIRRDELHEELSQNRS 1073
|
330
....*....|....*....
gi 124376530 1412 KCSSLEKTKHRLQNEIEDL 1430
Cdd:COG3096 1074 RRSQLEKQLTRCEAEMDSL 1092
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1380-1925 |
3.16e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1380 DAIQRTEELEEAKKKLaqrlqdaEEAVEAVNAKCSSLEKTKHRLQNEIEDlmvdVERSNAAAAALDKKQRNFDKILAEWK 1459
Cdd:PRK01156 156 DEILEINSLERNYDKL-------KDVIDMLRAEISNIDYLEEKLKSSNLE----LENIKKQIADDEKSHSITLKEIERLS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1460 QKYEESQSELESSQKEARSLSTeLFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKN--------VHELEKV 1531
Cdd:PRK01156 225 IEYNNAMDDYNNLKSALNELSS-LEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDpvyknrnyINDYFKY 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1532 RKQLEveklELQSALEEAEASLEHEEGKILRAQlEFNQIKAEIERKLAEKDE------EMEQAKRNHQRVVDSLQTSLDA 1605
Cdd:PRK01156 304 KNDIE----NKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKKSRYDDlnnqilELEGYEMDYNSYLKSIESLKKK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1606 ETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRN----- 1680
Cdd:PRK01156 379 IEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvc 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1681 -------------NLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTS-LINQKKKMESDLTQLQsEVEEA 1746
Cdd:PRK01156 459 gttlgeeksnhiiNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADLE-DIKIK 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1747 VQECRNAEEKAKKAITDAAMMAEELKKEQDTSaHLERMKKNMEQTIKDLQHRLDEAeqialkggKKQLQKLEARVRELEG 1826
Cdd:PRK01156 538 INELKDKHDKYEEIKNRYKSLKLEDLDSKRTS-WLNALAVISLIDIETNRSRSNEI--------KKQLNDLESRLQEIEI 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1827 ELEAEQKRNAESVkgmrkseRRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQA---EEAEEQANTNLSKFRKVQH 1903
Cdd:PRK01156 609 GFPDDKSYIDKSI-------REIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIaeiDSIIPDLKEITSRINDIED 681
|
570 580
....*....|....*....|..
gi 124376530 1904 ELDEAEERADIAESQVNKLRAK 1925
Cdd:PRK01156 682 NLKKSRKALDDAKANRARLEST 703
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1587-1809 |
3.19e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1587 QAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRAN 1666
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1667 DDLKENIAIVER------RNNLLQ--------AELEELRAVVEQTERSRKLAEQELIETSERvqlLHSQNTSLINQKKKM 1732
Cdd:COG4942 100 EAQKEELAELLRalyrlgRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAE---LAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124376530 1733 ESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKG 1809
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1238-1886 |
3.24e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.03 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1238 EQIIKAKANLEKvsrtLEDQANEYRVKLEEAQRSLNdfTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQ--ME 1315
Cdd:PRK10246 191 EQHKSARTELEK----LQAQASGVALLTPEQVQSLT--ASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASrrQQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1316 DLKRQLEEEGKAKNALAhALQSARHDCDL--LREQYEEETEAKAELQRVLSKANS---EVAQWRTKYETDAIQRTEELEE 1390
Cdd:PRK10246 265 ALQQALAAEEKAQPQLA-ALSLAQPARQLrpHWERIQEQSAALAHTRQQIEEVNTrlqSTMALRARIRHHAAKQSAELQA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1391 AKKKLAQRLQDAE------EAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNA------------AAAALDK--KQRN 1450
Cdd:PRK10246 344 QQQSLNTWLAEHDrfrqwnNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltadeVAAALAQhaEQRP 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1451 FDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKnayeeslEHLETFKRENKNLQEEISDLteqlgeggKNVHELEK 1530
Cdd:PRK10246 424 LRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRN-------AALNEMRQRYKEKTQQLADV--------KTICEQEA 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1531 VRKQLEVEKLELQS-------------------------------ALEEAEASLEhEEGKILRAQLEFNQIKAEIERKLA 1579
Cdd:PRK10246 489 RIKDLEAQRAQLQAgqpcplcgstshpaveayqalepgvnqsrldALEKEVKKLG-EEGAALRGQLDALTKQLQRDESEA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1580 EKDEEMEQA-KRNHQRVVDSLQTSLDAEtRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAeAQKQVKSLQSLLKDTQIQ 1658
Cdd:PRK10246 568 QSLRQEEQAlTQQWQAVCASLNITLQPQ-DDIQPWLDAQEEHERQLRLLSQRHELQGQIAA-HNQQIIQYQQQIEQRQQQ 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1659 LDDAVRA-----NDDLKENIAIVER------------RNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQ 1721
Cdd:PRK10246 646 LLTALAGyaltlPQEDEEASWLATRqqeaqswqqrqnELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQ 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1722 NTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEK---AKKAITDAAMMAEElkkeqdTSAHLERMKKNMEQTIKDLQHR 1798
Cdd:PRK10246 726 CLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQAsvfDDQQAFLAALLDEE------TLTQLEQLKQNLENQRQQAQTL 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1799 LDEAEQialkggkKQLQKLEARVRELEGELEAE--QKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVdklqLK 1876
Cdd:PRK10246 800 VTQTAQ-------ALAQHQQHRPDGLDLTVTVEqiQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALM----QQ 868
|
730
....*....|
gi 124376530 1877 VKAYKRQAEE 1886
Cdd:PRK10246 869 IAQATQQVED 878
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1286-1804 |
3.24e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.31 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1286 NGELARQLEEKEALISQ--LTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQsarhdcdlLREQYEEETEAKAE--LQR 1361
Cdd:COG5022 779 HGFRLRRLVDYELKWRLfiKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKK--------LRETEEVEFSLKAEvlIQK 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1362 VLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLaQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIE-DLMVDVERSNAA 1440
Cdd:COG5022 851 FGRSLKAKKRFSLLKKETIYLQSAQRVELAERQL-QELKIDVKSISSLKLVNLELESEIIELKKSLSsDLIENLEFKTEL 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1441 AAALDKKQRNFDKILAEWKQKYEESQSELESSQKeaRSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGE 1520
Cdd:COG5022 930 IARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVE--SKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQ 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1521 GGKNVHELEKVrKQLEVEKLELQSAleEAEASLEHEEGKILR--AQLEFNQIKAeiERKLAEKDEEMEQAKRNhqRVVDS 1598
Cdd:COG5022 1008 YGALQESTKQL-KELPVEVAELQSA--SKIISSESTELSILKplQKLKGLLLLE--NNQLQARYKALKLRREN--SLLDD 1080
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1599 LQTSLDAETRSrnevlrvkkkMEGDLNEMEIQLSHANRMAAEAQKQVKSLQsllkdtQIQLDDAVRANDDLKENIAIVER 1678
Cdd:COG5022 1081 KQLYQLESTEN----------LLKTINVKDLEVTNRNLVKPANVLQFIVAQ------MIKLNLLQEISKFLSQLVNTLEP 1144
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1679 RNNLLQAELEELRAVVEQTERSRKLAEQELIETSERvqlLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKA- 1757
Cdd:COG5022 1145 VFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEK---RLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGd 1221
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 124376530 1758 --KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQ 1804
Cdd:COG5022 1222 klKKLISEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDN 1270
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
971-1338 |
3.25e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 48.86 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 971 HATENKVKNLTEEMAGLDEIiakLTKEKKALQEAHQQALDDLQVEEDK---------VNSLSKSKVKLEQQVDDLEGSLE 1041
Cdd:NF033838 36 HAEEVRGGNNPTVTSSGNES---QKEHAKEVESHLEKILSEIQKSLDKrkhtqnvalNKKLSDIKTEYLYELNVLKEKSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1042 QE--KKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKK---------------------EFDINQQNSKIED 1098
Cdd:NF033838 113 AEltSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQkeedrrnyptntyktleleiaESDVEVKKAELEL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1099 EQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKlrsdlsrelEEISERLEEAGGATSVQIEMNKKREAEFQKMRR 1178
Cdd:NF033838 193 VKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDR---------EKAEEEAKRRADAKLKEAVEKNVATSEQDKPKR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1179 DLEEATLQHEATAAALRKKHADSVAELGEQidNLQRVKQKLEKEKSEFKLELDDVTSnmeqiiKAKANLEKVSR------ 1252
Cdd:NF033838 264 RAKRGVLGEPATPDKKENDAKSSDSSVGEE--TLPSPSLKPEKKVAEAEKKVEEAKK------KAKDQKEEDRRnyptnt 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1253 --TLEDQANEYRVKLEEAQRSLndfTTQRAKlQTENGELARQ----LEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGK 1326
Cdd:NF033838 336 ykTLELEIAESDVKVKEAELEL---VKEEAK-EPRNEEKIKQakakVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDK 411
|
410
....*....|..
gi 124376530 1327 AKNALAHALQSA 1338
Cdd:NF033838 412 VKEKPAEQPQPA 423
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
845-1028 |
3.45e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 845 AETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQ---------LQVQAEQDNLN--DAEERCDQLIKN 913
Cdd:COG4942 58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeelaellraLYRLGRQPPLAllLSPEDFLDAVRR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 914 KIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAK 993
Cdd:COG4942 138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
170 180 190
....*....|....*....|....*....|....*
gi 124376530 994 LTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVK 1028
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
873-1225 |
3.45e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 873 KELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSEL 952
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 953 KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQ 1032
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1033 VDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKE 1112
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1113 NQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1192
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350
....*....|....*....|....*....|...
gi 124376530 1193 ALRKKHADSVAELGEQIDNLQRVKQKLEKEKSE 1225
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1735-1929 |
3.97e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1735 DLTQLQSEVEEAvQECRNAEEKAKKAitdaammAEELKKEQDTSAHLERMKK-----NMEQTIKDLQHRLDEAEQiALKG 1809
Cdd:COG4913 236 DLERAHEALEDA-REQIELLEPIREL-------AERYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRA-ELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1810 GKKQLQKLEARVRELEGEL-EAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAE 1888
Cdd:COG4913 307 LEAELERLEARLDALREELdELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 124376530 1889 EQANTNLSKFRKVQHELDEAEERADIAESQVNK-LRAKSRDI 1929
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRReLRELEAEI 428
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1746-1931 |
4.07e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1746 AVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELE 1825
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-ELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1826 GELEAEQKRNAESVKGMRKSERR---------------IKELTY----------QTEEDKKNLLRLQDLVDKLQLKVKAY 1880
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQpplalllspedfldaVRRLQYlkylaparreQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 124376530 1881 KRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGA 1931
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1755-1934 |
4.30e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1755 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIalkggkKQLQKLEARVRELEGELEAEQKR 1834
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1835 naesVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQA-EEAEEQANTNLSKFRKVQHELDEAEERAD 1913
Cdd:COG4717 148 ----LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180
....*....|....*....|.
gi 124376530 1914 IAESQVNKLRAKSRDIGAKQK 1934
Cdd:COG4717 224 ELEEELEQLENELEAAALEER 244
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
893-1115 |
4.66e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 893 VQAEqDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEdeeemnaELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHA 972
Cdd:COG3883 12 AFAD-PQIQAKQKELSELQAELEAAQAELDALQAELE-------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 973 TENKVKNLTEEM----------------AGLDEIIAKLTKEKKaLQEAHQQALDDLQveedkvnslsKSKVKLEQQVDDL 1036
Cdd:COG3883 84 RREELGERARALyrsggsvsyldvllgsESFSDFLDRLSALSK-IADADADLLEELK----------ADKAELEAKKAEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124376530 1037 EGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQA 1115
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1424-1924 |
4.95e-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: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1424 QNEIEDLMVDVERSNAAAAALDKKQRNFDKILAewKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLEtfkRE 1503
Cdd:pfam05557 20 QMELEHKRARIELEKKASALKRQLDRESDRNQE--LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL---NE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1504 NKNLQEEISDLTEQLGEggknvhELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQlEFNQIKAEIERKLAEKDE 1583
Cdd:pfam05557 95 KESQLADAREVISCLKN------ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS-EAEQLRQNLEKQQSSLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1584 EMEQAKRNHQRVvdSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMaaeaqkqvKSLQSLLKDTQIQLDDAV 1663
Cdd:pfam05557 168 AEQRIKELEFEI--QSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNEN--------IENKLLLKEEVEDLKRKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1664 RANDDLKENIAIVERRNNLLQAELEELravvEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEV 1743
Cdd:pfam05557 238 EREEKYREEAATLELEKEKLEQELQSW----VKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1744 EEAVQECRNAEEKakkaITDAAMMAEELK--------------KEQD-TSAHLERMKK--NMEQTIKDLQHRLDEAEQIA 1806
Cdd:pfam05557 314 RELEQELAQYLKK----IEDLNKKLKRHKalvrrlqrrvllltKERDgYRAILESYDKelTMSNYSPQLLERIEEAEDMT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1807 LKgGKKQLQKLEARVRELEGELEAEQKRNA--ESVKGMRKSERRIKELTYQTEEDKKNLLRLQDL---VDKLQLKVKAYK 1881
Cdd:pfam05557 390 QK-MQAHNEEMEAQLSVAEEELGGYKQQAQtlERELQALRQQESLADPSYSKEEVDSLRRKLETLeleRQRLREQKNELE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 124376530 1882 RQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRA 1924
Cdd:pfam05557 469 MELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQA 511
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
845-1449 |
8.79e-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: 47.64 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 845 AETEKEMATMKEEFGRIKETLEKSEARRKELEEKmvslLQEKND-LQLQVQAEQdnLNDAEERCDQLIKnkiQLEAKVKE 923
Cdd:COG3096 295 FGARRQLAEEQYRLVEMARELEELSARESDLEQD----YQAASDhLNLVQTALR--QQEKIERYQEDLE---ELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 924 MNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDL-------------------------------ELTLAKVEKEKHA 972
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYqqaldvqqtraiqyqqavqalekaralcglpDLTPENAEDYLAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 973 TENKVKNLTEEMAGLDE--IIAKLTKEK--KALQ------------EAHQQALDDLQVEEDKVNsLSKSKVKLEQQVDDL 1036
Cdd:COG3096 446 FRAKEQQATEEVLELEQklSVADAARRQfeKAYElvckiageversQAWQTARELLRRYRSQQA-LAQRLQQLRAQLAEL 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1037 EGSLEQEKKVRMDLERAKRKLEGDLkltqESIMDLENDKLQLEEKLKKKEfdiNQQNSKIEDeqvlALQLQKKLKENQAR 1116
Cdd:COG3096 525 EQRLRQQQNAERLLEEFCQRIGQQL----DAAEELEELLAELEAQLEELE---EQAAEAVEQ----RSELRQQLEQLRAR 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1117 IEELEEELEAERTARAKVEKLRsdlsrelEEISERLEEAGGATS-VQIEMNKKREAEFQKmrrdlEEATLQHEATAAALR 1195
Cdd:COG3096 594 IKELAARAPAWLAAQDALERLR-------EQSGEALADSQEVTAaMQQLLEREREATVER-----DELAARKQALESQIE 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1196 KKHADSVAE------LGEQ---------------------------------IDNLQRVKQKL----------------- 1219
Cdd:COG3096 662 RLSQPGGAEdprllaLAERlggvllseiyddvtledapyfsalygparhaivVPDLSAVKEQLagledcpedlyliegdp 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1220 ------------------------------------------EKEKSEFKLELDDVTsnmEQIIKAKANLEKVSRTLED- 1256
Cdd:COG3096 742 dsfddsvfdaeeledavvvklsdrqwrysrfpevplfgraarEKRLEELRAERDELA---EQYAKASFDVQKLQRLHQAf 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1257 ------------------QANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTrgkL----SYTQQM 1314
Cdd:COG3096 819 sqfvgghlavafapdpeaELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAN---LladeTLADRL 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1315 EDLKRQLEEEGKAKNALAH-------------ALQSARHDCDLLREQYEeetEAKAELQRVLSK--ANSEVAQWRT--KY 1377
Cdd:COG3096 896 EELREELDAAQEAQAFIQQhgkalaqleplvaVLQSDPEQFEQLQADYL---QAKEQQRRLKQQifALSEVVQRRPhfSY 972
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1378 EtDAIQRTEELEEAKKKLAQRLQDAE-------EAVEAVNAKCS-------SLeKTKHR--------LQNEIEDLMVDVE 1435
Cdd:COG3096 973 E-DAVGLLGENSDLNEKLRARLEQAEearrearEQLRQAQAQYSqynqvlaSL-KSSRDakqqtlqeLEQELEELGVQAD 1050
|
810
....*....|....
gi 124376530 1436 rSNAAAAALDKKQR 1449
Cdd:COG3096 1051 -AEAEERARIRRDE 1063
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1345-1606 |
9.62e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.45 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1345 LREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEeLEEAKKKLAQRLQDAEEAVEAVNAKCSSLE------K 1418
Cdd:pfam00038 59 LRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTS-AENDLVGLRKDLDEATLARVDLEAKIESLKeelaflK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1419 TKHR-----LQNEIEDLMVDVERSNAaaaaldkKQRNFDKILAEWKQKYEEsqselessqkearslstelfkLKNAYEES 1493
Cdd:pfam00038 138 KNHEeevreLQAQVSDTQVNVEMDAA-------RKLDLTSALAEIRAQYEE---------------------IAAKNREE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1494 LEhlETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAE 1573
Cdd:pfam00038 190 AE--EWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISE 267
|
250 260 270
....*....|....*....|....*....|...
gi 124376530 1574 IERKLAEKDEEMEQAKRNHQRVVDsLQTSLDAE 1606
Cdd:pfam00038 268 LEAELQETRQEMARQLREYQELLN-VKLALDIE 299
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1475-1831 |
1.04e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.98 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1475 EARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLE 1554
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1555 HEEGKILRAQLEFNQ---IKAEIERKLAEKDEEME------QAKRNHQRVVDSLQTSLDAETRSRNEVLRV----KKKME 1621
Cdd:pfam19220 101 EAEAAKEELRIELRDktaQAEALERQLAAETEQNRaleeenKALREEAQAAEKALQRAEGELATARERLALleqeNRRLQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1622 GDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAV----RANDDLKENIAIVERRNNLLQAELEELRAVVEQT 1697
Cdd:pfam19220 181 ALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQaereRAEAQLEEAVEAHRAERASLRMKLEALTARAAAT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1698 ERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQEcRNAEEKAKKAITD-AAMMAEELKkeqD 1776
Cdd:pfam19220 261 EQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQ-FQEMQRARAELEErAEMLTKALA---A 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 124376530 1777 TSAHLERMkknmEQTIKDLQHRLDEAEQIALKggkkQLQKLEARVRELEGELEAE 1831
Cdd:pfam19220 337 KDAALERA----EERIASLSDRIAELTKRFEV----ERAALEQANRRLKEELQRE 383
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
861-1096 |
1.40e-04 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 47.07 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 861 IKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAeqdnlNDAEERCDQLIKNKIQLEAKVKEMNERLEDeeeMNAELTA 940
Cdd:pfam18971 619 LEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQA-----NSQKDEIFALINKEANRDARAIAYTQNLKG---IKRELSD 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 941 KKRKLEDECSELKKDIDDLE----LTLAKVEKEKHATENKVKNLteemaGLD-EIIAKLTKEKKALQEAHQQALDDL--- 1012
Cdd:pfam18971 691 KLEKISKDLKDFSKSFDEFKngknKDFSKAEETLKALKGSVKDL-----GINpEWISKVENLNAALNEFKNGKNKDFskv 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1013 -QVEEDKVNSLskSKVKLEQQVDDLEGSLEQEKKVrmdlerakRKLEGDLKLTQESIMDLEN-DKLQLEEKLKKKEfDIN 1090
Cdd:pfam18971 766 tQAKSDLENSV--KDVIINQKVTDKVDNLNQAVSV--------AKAMGDFSRVEQVLADLKNfSKEQLAQQAQKNE-DFN 834
|
....*..
gi 124376530 1091 Q-QNSKI 1096
Cdd:pfam18971 835 TgKNSEL 841
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
845-1003 |
1.43e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.81 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 845 AETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEM 924
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 925 NER-------LEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAK---L 994
Cdd:pfam07888 156 KERakkagaqRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEneaL 235
|
....*....
gi 124376530 995 TKEKKALQE 1003
Cdd:pfam07888 236 LEELRSLQE 244
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
913-1182 |
1.64e-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: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 913 NKIQLEAKVKEM-NERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDeiI 991
Cdd:pfam17380 285 SERQQQEKFEKMeQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRE--L 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 992 AKLTKEKKALQEAHQQALDDLQVEEDKVN--------SLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAK----RKLEG 1059
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELERLQMERQQKNervrqeleAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARqrevRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1060 DLKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQvlalqLQKKLKENQARiEELEEELEAERTARAKVEKLRS 1139
Cdd:pfam17380 443 ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK-----RDRKRAEEQRR-KILEKELEERKQAMIEEERKRK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 124376530 1140 DLSRELEEIS------ERLEEAGGATSVQIEMNKKREAEfQKMRRDLEE 1182
Cdd:pfam17380 517 LLEKEMEERQkaiyeeERRREAEEERRKQQEMEERRRIQ-EQMRKATEE 564
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
889-1095 |
1.77e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 889 LQLQVQAEQDNLNDAEER--------CDQLIKNkiqLEAKVKEMNERLEDEEEMNAELTAKKR----KLEDECSELKKDI 956
Cdd:PHA02562 160 LDISVLSEMDKLNKDKIRelnqqiqtLDMKIDH---IQQQIKTYNKNIEEQRKKNGENIARKQnkydELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 957 DDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAH-----QQALDDlqvEEDKVNSLSKSKVKLEQ 1031
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGvcptcTQQISE---GPDRITKIKDKLKELQH 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124376530 1032 QVDDLEGSLEQEKKVRMDLERAKRKL----------EGDLKLTQESIMDLEN--DKLQLEEKLKKKEFDINQQNSK 1095
Cdd:PHA02562 314 SLEKLDTAIDELEEIMDEFNEQSKKLlelknkistnKQSLITLVDKAKKVKAaiEELQAEFVDNAEELAKLQDELD 389
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1058-1302 |
1.87e-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: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1058 EGDLKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSKIEdeqvlalQLQKKLKENQARIEeleeeleaerTARAKVEKL 1137
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-------ELQAELEALQAEID----------KLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1138 RSDLSRELEEISERLeeaggatsvqiemnkkREAEFQKMRRDLEEATLQHEATAAALRKkhADSVAELGEQ----IDNLQ 1213
Cdd:COG3883 78 EAEIEERREELGERA----------------RALYRSGGSVSYLDVLLGSESFSDFLDR--LSALSKIADAdadlLEELK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1214 RVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKvsrtledqaneyrvKLEEAQRSLNDFTTQRAKLQTENGELARQL 1293
Cdd:COG3883 140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEA--------------QQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
....*....
gi 124376530 1294 EEKEALISQ 1302
Cdd:COG3883 206 AAAEAAAAA 214
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1298-1590 |
2.12e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 46.16 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1298 ALISQLTRGKLSYTQQMEDLKRQLEEE--GKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRvlsKANSEVAQWRT 1375
Cdd:NF033838 88 ALNKKLSDIKTEYLYELNVLKEKSEAEltSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEK---KAKDQKEEDRR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1376 KYETDAIqRTEELEEAKKKLaqRLQDAEEAVEAVNAKCSSLEKTkhrlqneIEDLMVDVERSNAAAAALDKKQRnfDKIL 1455
Cdd:NF033838 165 NYPTNTY-KTLELEIAESDV--EVKKAELELVKEEAKEPRDEEK-------IKQAKAKVESKKAEATRLEKIKT--DREK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1456 AEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQL-----------GEGGKN 1524
Cdd:NF033838 233 AEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSVGEETLpspslkpekkvAEAEKK 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1525 VHELEK----------------VRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAE-------- 1580
Cdd:NF033838 313 VEEAKKkakdqkeedrrnyptnTYKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEatrlekik 392
|
330
....*....|..
gi 124376530 1581 --KDEEMEQAKR 1590
Cdd:NF033838 393 tdRKKAEEEAKR 404
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1637-1831 |
2.20e-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: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1637 MAAEAQKQVKSLQSLLKdtqiQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQ 1716
Cdd:COG1579 1 AMPEDLRALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1717 LLHSQNTSLINQKkkmesDLTQLQSEVEEAVQECRNAEEKAKkaitdAAMMAEELKKEQdtsahLERMKKNMEQTIKDLQ 1796
Cdd:COG1579 77 KYEEQLGNVRNNK-----EYEALQKEIESLKRRISDLEDEIL-----ELMERIEELEEE-----LAELEAELAELEAELE 141
|
170 180 190
....*....|....*....|....*....|....*
gi 124376530 1797 HRLDEAEQIaLKGGKKQLQKLEARVRELEGELEAE 1831
Cdd:COG1579 142 EKKAELDEE-LAELEAELEELEAEREELAAKIPPE 175
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1196-1702 |
2.66e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1196 KKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVtsnMEQIIKAKANLEKVSrTLEDQANEYRVKLEEAQRSLNDF 1275
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNA---MDDYNNLKSALNELS-SLEDMKNRYESEIKTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1276 TTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLE------EEGKAKNALAHALQSARHDCDLLREQY 1349
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSnidaeiNKYHAIIKKLSVLQKDYNDYIKKKSRY 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1350 EEETEAKAELQRVLSKANSEV------AQWRTKYETDAIQRTEELEEAKKK-------LAQRLQDAEEAVEAVNAKCSSL 1416
Cdd:PRK01156 349 DDLNNQILELEGYEMDYNSYLksieslKKKIEEYSKNIERMSAFISEILKIqeidpdaIKKELNEINVKLQDISSKVSSL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1417 EKTKHRLQNEIEDLMVDVE----RSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYE- 1491
Cdd:PRK01156 429 NQRIRALRENLDELSRNMEmlngQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEy 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1492 ---ESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLE-----------------------LQSA 1545
Cdd:PRK01156 509 lesEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEdldskrtswlnalavislidietNRSR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1546 LEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEME--QAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGD 1623
Cdd:PRK01156 589 SNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANnlNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPD 668
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124376530 1624 LNEMEIQLSHANrmaaeaqkqvkslqSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRK 1702
Cdd:PRK01156 669 LKEITSRINDIE--------------DNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1363-1907 |
2.85e-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: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1363 LSKANSEVAQWRTKY-ETDAIQRTEElEEAKkklaQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVER----S 1437
Cdd:TIGR01612 781 LNKYKSKISEIKNHYnDQINIDNIKD-EDAK----QNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKfinfE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1438 NAAAAALDKKQRNFDKILAEWKQKYEESQSEL-ESSQKEARSLSTELfklKNAYEESLEHLETFKREN------KNLQEE 1510
Cdd:TIGR01612 856 NNCKEKIDSEHEQFAELTNKIKAEISDDKLNDyEKKFNDSKSLINEI---NKSIEEEYQNINTLKKVDeyikicENTKES 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1511 ISD-------LTEQLGEGGKNVHELEKVRK----QLEVEKLELQSALEEA--EASLEHEEGKILRAQLEFNQIKAEI--- 1574
Cdd:TIGR01612 933 IEKfhnkqniLKEILNKNIDTIKESNLIEKsykdKFDNTLIDKINELDKAfkDASLNDYEAKNNELIKYFNDLKANLgkn 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1575 -ERKLAEKDEEMEQAKRN-HQRVVDSLQTSLDAETRSRNEVLRVKKKMEGD------------LNEMEIQLSHANRMaaE 1640
Cdd:TIGR01612 1013 kENMLYHQFDEKEKATNDiEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEigkniellnkeiLEEAEINITNFNEI--K 1090
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1641 AQKQVKSLQSLLKDTQIQLDDAV-RANDDLK-------ENIAIVERRNNLLQAELEELRAVVEQTER-SRKLAEQELIET 1711
Cdd:TIGR01612 1091 EKLKHYNFDDFGKEENIKYADEInKIKDDIKnldqkidHHIKALEEIKKKSENYIDEIKAQINDLEDvADKAISNDDPEE 1170
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1712 SERVQllhsQN-TSLINQKKKMESDLTQLQSEVEE------AVQECRNAEEKAKKAItdAAMMAEELKKEQDTSAHlerM 1784
Cdd:TIGR01612 1171 IEKKI----ENiVTKIDKKKNIYDEIKKLLNEIAEiekdktSLEEVKGINLSYGKNL--GKLFLEKIDEEKKKSEH---M 1241
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1785 KKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELEGELEAE----QKRNAESVKGMRKSERRI----------- 1849
Cdd:TIGR01612 1242 IKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDhhiiSKKHDENISDIREKSLKIiedfseesdin 1321
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124376530 1850 ---KEL-TYQTEEDKKN------LLRLQDLVDKLQL--------KVKAYKRQAEEAEEQANTNLSKFRKVQHELDE 1907
Cdd:TIGR01612 1322 dikKELqKNLLDAQKHNsdinlyLNEIANIYNILKLnkikkiidEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD 1397
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1675-1813 |
2.88e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1675 IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESdltQLQSEVEEAVQECRNAE 1754
Cdd:PRK00409 503 IIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQE---EEDKLLEEAEKEAQQAI 579
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 124376530 1755 EKAKKAITDAAMMAEELKKEQDTSAHLermkKNMEQTIKDLQHRLDEAEQIALKGGKKQ 1813
Cdd:PRK00409 580 KEAKKEADEIIKELRQLQKGGYASVKA----HELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
869-1336 |
2.94e-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: 45.90 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 869 EARRKELEEKMVSLLQEKNDLQLQVQAEQDNLndaeercdQLIKNKIQLEAkvKEMNERLEDEEEMNAELTAKKRKLede 948
Cdd:pfam07111 241 ELERQELLDTMQHLQEDRADLQATVELLQVRV--------QSLTHMLALQE--EELTRKIQPSDSLEPEFPKKCRSL--- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 949 cseLKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSL------ 1022
Cdd:pfam07111 308 ---LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLqmelsr 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1023 -SKSKVKLEQQVDDLEgslEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKefdinqqnskiedeQV 1101
Cdd:pfam07111 385 aQEARRRQQQQTASAE---EQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKV--------------HT 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1102 LALQLQKKLKENQARIEELEEELEaertarakVEKLRSDLSRELEEISE---RL--EEAGGATSVQIEMNKKREaEFQKM 1176
Cdd:pfam07111 448 IKGLMARKVALAQLRQESCPPPPP--------APPVDADLSLELEQLREernRLdaELQLSAHLIQQEVGRARE-QGEAE 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1177 RRDLEEATLQHEATAaalrKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELddvtsNMEQIIKAKANLEKVSRT--- 1253
Cdd:pfam07111 519 RQQLSEVAQQLEQEL----QRAQESLASVGQQLEVARQGQQESTEEAASLRQEL-----TQQQEIYGQALQEKVAEVetr 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1254 LEDQANEYRVKLEEAQR-------SLNDFTTQRAKLQTENGELARQLEEkealisqltrgklSYTQQMEDLKRQLEEEGK 1326
Cdd:pfam07111 590 LREQLSDTKRRLNEARReqakavvSLRQIQHRATQEKERNQELRRLQDE-------------ARKEEGQRLARRVQELER 656
|
490
....*....|
gi 124376530 1327 AKNALAHALQ 1336
Cdd:pfam07111 657 DKNLMLATLQ 666
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1050-1204 |
2.97e-04 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 45.90 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1050 LERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKkefdINQQNSKIEDEQVLALQLQKKLKENQARIeeleeeleaERT 1129
Cdd:COG1193 502 IERARELLGEESIDVEKLIEELERERRELEEEREE----AERLREELEKLREELEEKLEELEEEKEEI---------LEK 568
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124376530 1130 ARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAE 1204
Cdd:COG1193 569 AREEAEEILREARKEAEELIRELREA-----------QAEEEELKEARKKLEELKQELEEKLEKPKKKAKPAKPP 632
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1327-1461 |
2.98e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1327 AKNALAHALQSARHDCDLLREqyEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAV 1406
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 124376530 1407 EAVNAKCSSLEKTKHRLQNEIEDlmvdversnaaaaaLDKKQRNFDKILAEWKQK 1461
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQE--------------LEKKEEELEELIEEQLQE 143
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1270-1797 |
3.24e-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: 46.10 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1270 RSLNDFttqrakLQTENGELARQLEEKEALI--SQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHAlqsaRHdcdllRE 1347
Cdd:COG3096 214 RSLRDY------LLPENSGVRKAFQDMEAALreNRMTLEAIRVTQSDRDLFKHLITEATNYVAADYM----RH-----AN 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1348 QYEEETEAKAELQRVLSKANSEVA--QWRTKYETDAIqrtEELEEAKKKLAQRLQDAEEAVEAVnakcssleKTKHRLQN 1425
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAeeQYRLVEMAREL---EELSARESDLEQDYQAASDHLNLV--------QTALRQQE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1426 EIEDLMVDVErsnAAAAALDKKQrnfdKILAEWKQKYEESQSELESSQKEARSLSTELFKlknaYEESLEHLETfkrenK 1505
Cdd:COG3096 348 KIERYQEDLE---ELTERLEEQE----EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD----YQQALDVQQT-----R 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1506 NLQEEisdlteqlgeggKNVHELEKVRKQLEVEKLELQSALEEAEASLEHEEgkilraqlEFNQIKAEIERKLAEKDEem 1585
Cdd:COG3096 412 AIQYQ------------QAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQ--------QATEEVLELEQKLSVADA-- 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1586 eqAKRNHQRVVDSLQTSLDAETRSR-----NEVLRV---KKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQI 1657
Cdd:COG3096 470 --ARRQFEKAYELVCKIAGEVERSQawqtaRELLRRyrsQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQ 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1658 QLDDAvranDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHsqntslinqkkKMESDLT 1737
Cdd:COG3096 548 QLDAA----EELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL-----------AAQDALE 612
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124376530 1738 QLQSEVEEAVQECRnaeekakkAITDAamMAEELKKEQDTSA---HLERMKKNMEQTIKDLQH 1797
Cdd:COG3096 613 RLREQSGEALADSQ--------EVTAA--MQQLLEREREATVerdELAARKQALESQIERLSQ 665
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1342-1554 |
3.39e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1342 CDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKH 1421
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1422 RLQNEIEDLM------VDVER----SNAAAAALDKKQRNFDKILAEWKQKYEESQSELESS-------QKEARSLSTELF 1484
Cdd:PRK05771 118 ELEQEIERLEpwgnfdLDLSLllgfKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvvLKELSDEVEEEL 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124376530 1485 KlKNAYEE-SLEHLETFKRENKNLQEEISDLTEQLGEggkNVHELEKVRKQLEVEKL----ELQSALEEAEASLE 1554
Cdd:PRK05771 198 K-KLGFERlELEEEGTPSELIREIKEELEEIEKERES---LLEELKELAKKYLEELLalyeYLEIELERAEALSK 268
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1022-1172 |
3.47e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1022 LSKSKVKLEQQVDDLEGSLEQEKK-----VRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSKI 1096
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKealleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1097 EDEQVLALQLQKKLKENQARIEELEEEleaertARAKVEKLrSDLSRE------LEEISERLEEAGGATSVQIEMNKKRE 1170
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEE------QLQELERI-SGLTAEeakeilLEKVEEEARHEAAVLIKEIEEEAKEE 185
|
..
gi 124376530 1171 AE 1172
Cdd:PRK12704 186 AD 187
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1477-1912 |
3.47e-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: 45.73 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1477 RSLSTELFKLKNAYEESLEHLEtfkrenKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSALEEAEASLEHE 1556
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLT------LRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1557 EGKiLRAQLEFNQIKAEIERKLA-EKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEiQLSHAN 1635
Cdd:TIGR00618 253 EEQ-LKKQQLLKQLRARIEELRAqEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRA-KLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1636 RMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQ----------AELEELRAVVEQTERSRKLAE 1705
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhihtlqqqktTLTQKLQSLCKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1706 QELIETSE----RVQLLHSQNTSLINQKKK------MESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQ 1775
Cdd:TIGR00618 411 TIDTRTSAfrdlQGQLAHAKKQQELQQRYAelcaaaITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1776 DTSAHLERMKKN----MEQTIKDLQHRLD----EAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSER 1847
Cdd:TIGR00618 491 VVLARLLELQEEpcplCGSCIHPNPARQDidnpGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ 570
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124376530 1848 RIKELTYQTEEDK-------KNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERA 1912
Cdd:TIGR00618 571 SFSILTQCDNRSKedipnlqNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA 642
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1003-1187 |
4.04e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1003 EAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQekkvrmdLERAKRKLEGDLKLTQESIMDLENDKLQLEEKL 1082
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1083 KKKEfdiNQQNSKIEDEQVLALQ-----LQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGG 1157
Cdd:COG1579 76 KKYE---EQLGNVRNNKEYEALQkeiesLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180 190
....*....|....*....|....*....|
gi 124376530 1158 ATSVQIEmnkKREAEFQKMRRDLEEATLQH 1187
Cdd:COG1579 153 ELEAELE---ELEAEREELAAKIPPELLAL 179
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1495-1933 |
4.56e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.90 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1495 EHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQSAL--------EEAEASLEHEEGKILRAQLE 1566
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1567 FNQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVK 1646
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1647 SLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLI 1726
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1727 NQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIA 1806
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1807 LKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEE 1886
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 124376530 1887 AEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKQ 1933
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
994-1251 |
5.00e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 994 LTKEKKALQEAhQQALDDLQVEEDKVNSLSKSKVkLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLEN 1073
Cdd:COG3206 184 LPELRKELEEA-EAALEEFRQKNGLVDLSEEAKL-LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1074 DklQLEEKLKKKEFDINQQnskiedeqvLAlQLQKKLKENQARIeeleeeleaeRTARAKVEKLRSDLSRELEEISERLE 1153
Cdd:COG3206 262 S--PVIQQLRAQLAELEAE---------LA-ELSARYTPNHPDV----------IALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1154 eaggatsVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRkkhadsvaELGEQIDNLQRVKQKLEKEKSEFKLELDDV 1233
Cdd:COG3206 320 -------AELEALQAREASLQAQLAQLEARLAELPELEAELR--------RLEREVEVARELYESLLQRLEEARLAEALT 384
|
250
....*....|....*...
gi 124376530 1234 TSNMEQIIKAKANLEKVS 1251
Cdd:COG3206 385 VGNVRVIDPAVVPLKPVS 402
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
870-1013 |
5.08e-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: 43.80 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 870 ARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQL---------------IKNKI--------QLEAKVKEMNE 926
Cdd:pfam15934 41 ENKNEQEQQLKEFTVQNQRLACQIDNLHETLKDRDHQIKQLqsmitgysdisennrLKEEIhdlkqkncVQARVVRKMGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 927 RLEDEEEMNAELTAKKRKL----EDECSELK---KDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLdeiiakltKEKK 999
Cdd:pfam15934 121 ELKGQEEQRVELCDKYESLlgsfEEQCQELKranRRVQSLQTRLSQVEKLQEELRTERKILREEVIAL--------KEKD 192
|
170
....*....|....
gi 124376530 1000 ALQEAHQQALDDLQ 1013
Cdd:pfam15934 193 AKSNGRERALQDQL 206
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1189-1372 |
5.28e-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: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1189 ATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELD----DVTSNMEQIIKAKANLEKVSRTLEDQANEYRVK 1264
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelqaELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1265 LEEAQR---------------SLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKN 1329
Cdd:COG3883 92 ARALYRsggsvsyldvllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 124376530 1330 ALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQ 1372
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
959-1339 |
5.52e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 959 LELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEG 1038
Cdd:COG5185 217 SESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1039 SLeQEKKVRMDLERAKRKLEGDLKLTQEsimdlendKLQLEEKLKKKEFDINQQNSKIEdeqvlalQLQKKLKENQARIE 1118
Cdd:COG5185 297 KI-AEYTKSIDIKKATESLEEQLAAAEA--------EQELEESKRETETGIQNLTAEIE-------QGQESLTENLEAIK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1119 ELEEELEAERTARAKVEKLRSdLSRELEEISERLEEAGGATSVQIEMNKKREA--------EFQKMRRDLEEATLQHEAT 1190
Cdd:COG5185 361 EEIENIVGEVELSKSSEELDS-FKDTIESTKESLDEIPQNQRGYAQEILATLEdtlkaadrQIEELQRQIEQATSSNEEV 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1191 AAALRKKHADSVAELGEQIDNLQ-RVKQKLEKEKSEFKLELDDVTSNMEQIIKA----KANLEKVSRTLEDQANEYRVKL 1265
Cdd:COG5185 440 SKLLNELISELNKVMREADEESQsRLEEAYDEINRSVRSKKEDLNEELTQIESRvstlKATLEKLRAKLERQLEGVRSKL 519
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124376530 1266 EEAQRSLNDFttqrakLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLK-RQLEEEGKAKNALAHALQSAR 1339
Cdd:COG5185 520 DQVAESLKDF------MRARGYAHILALENLIPASELIQASNAKTDGQAANLRtAVIDELTQYLSTIESQQARED 588
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1029-1285 |
5.59e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1029 LEQQVDDLEGSL----EQEKKVRMDLERAKRKLEgDLKlTQESIMDLENDKLQLEEKLKkkefdinqqnskiedeqvlal 1104
Cdd:COG3206 166 LELRREEARKALefleEQLPELRKELEEAEAALE-EFR-QKNGLVDLSEEAKLLLQQLS--------------------- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1105 QLQKKLKENQARIeeleeeleaeRTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnkkreaEFQKMRRDLEEAT 1184
Cdd:COG3206 223 ELESQLAEARAEL----------AEAEARLAALRAQLGSGPDALPELLQSP----------------VIQQLRAQLAELE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1185 LQHEATAAALRKKHADsVAELGEQIDNL-QRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRV 1263
Cdd:COG3206 277 AELAELSARYTPNHPD-VIALRAQIAALrAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
250 260
....*....|....*....|....*
gi 124376530 1264 ---KLEEAQRSLNDFTTQRAKLQTE 1285
Cdd:COG3206 356 lerEVEVARELYESLLQRLEEARLA 380
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1583-1870 |
5.71e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1583 EEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGdLNEMeiqLSHANRMAAEaqkqvkSLQSLLKDTQIQLDDA 1662
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQL-LNKL---LPQANLLADE------TLADRLEELREELDAA 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1663 VRANDDLKEN---IAIVERRNNLLQ---AELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDL 1736
Cdd:COG3096 906 QEAQAFIQQHgkaLAQLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSDL 985
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1737 T-QLQSEVEEAVQECRNAEEKAKKA---ITDAAMMAEELKKEQDTSAhleRMKKNMEQTIKDLQHRLD-EAEQIAlKGGK 1811
Cdd:COG3096 986 NeKLRARLEQAEEARREAREQLRQAqaqYSQYNQVLASLKSSRDAKQ---QTLQELEQELEELGVQADaEAEERA-RIRR 1061
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124376530 1812 KQLQK----LEARVRELEGEL---EAEQKrnaESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLV 1870
Cdd:COG3096 1062 DELHEelsqNRSRRSQLEKQLtrcEAEMD---SLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLA 1124
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
853-1938 |
6.22e-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: 45.04 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 853 TMKEEFGRIKETLEKSEARRKeLEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIK--NKIQLEAKVKEMNerLED 930
Cdd:TIGR01612 538 LYKEIEAGLKESYELAKNWKK-LIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIyiNKLKLELKEKIKN--ISD 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 931 EEEMNAELTAKKRKLEDECSElkkdIDDleltLAKVEKEKhatenkvknLTEEMAGLDEIIAKLTKEkkaLQEAHQQALD 1010
Cdd:TIGR01612 615 KNEYIKKAIDLKKIIENNNAY----IDE----LAKISPYQ---------VPEHLKNKDKIYSTIKSE---LSKIYEDDID 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1011 DLQ------VEEDKVNSlSKSKVKLeqqvDDLEGSLEQEKKVRMDLERAKRKLegdlkltqeSIMDLENDKLQLEEKLKK 1084
Cdd:TIGR01612 675 ALYnelssiVKENAIDN-TEDKAKL----DDLKSKIDKEYDKIQNMETATVEL---------HLSNIENKKNELLDIIVE 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1085 KEFDI-----NQQNSKIEDeqvlalqLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGAT 1159
Cdd:TIGR01612 741 IKKHIhgeinKDLNKILED-------FKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNY 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1160 SVQIEMNKK---REAEFQKM---RRDLEEATLQHEATAAALRKKHADSVAELGEQIDNL-QRVKQKLEKEK--------S 1224
Cdd:TIGR01612 814 DKSKEYIKTisiKEDEIFKIineMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELtNKIKAEISDDKlndyekkfN 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1225 EFKLELDDVTSNMEQIIKAKANLEKVSRTLE--DQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEK--EALI 1300
Cdd:TIGR01612 894 DSKSLINEINKSIEEEYQNINTLKKVDEYIKicENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKfdNTLI 973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1301 SQLTRGKLSYTQ-QMEDLKRQLEEEGKAKNALAHALQSARHdcDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYET 1379
Cdd:TIGR01612 974 DKINELDKAFKDaSLNDYEAKNNELIKYFNDLKANLGKNKE--NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHT 1051
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1380 DAIQRTEELEEAKKKLAQRLQdaEEAVEAVNAKCSSLEKTKHRLQ----------------NEIEDLMVDVErsnaaaaA 1443
Cdd:TIGR01612 1052 SIYNIIDEIEKEIGKNIELLN--KEILEEAEINITNFNEIKEKLKhynfddfgkeenikyaDEINKIKDDIK-------N 1122
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1444 LDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKN--AYEESLEHLETFKRENKNLQEEISDLTEQLGEG 1521
Cdd:TIGR01612 1123 LDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDpeEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEI 1202
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1522 GKNVHELEKVR---------------KQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKlaekdEEME 1586
Cdd:TIGR01612 1203 EKDKTSLEEVKginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIK-----AEME 1277
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1587 QAKRNHQRVVDSLQTSLDAE---TRSRNEVLRVKKKM--EGDLNEMEIQLshaNRMAAEAQKQVKSLQSLLKDTQ----- 1656
Cdd:TIGR01612 1278 TFNISHDDDKDHHIISKKHDeniSDIREKSLKIIEDFseESDINDIKKEL---QKNLLDAQKHNSDINLYLNEIAniyni 1354
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1657 IQLDDAVRANDDLKENIAIVERRNNLLQAE----------------LEELRAVVEQTERSRKLAE--QELIETSERVQLL 1718
Cdd:TIGR01612 1355 LKLNKIKKIIDEVKEYTKEIEENNKNIKDEldkseklikkikddinLEECKSKIESTLDDKDIDEciKKIKELKNHILSE 1434
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1719 HSQNTSLINQKKKMESDLTQLQSEVEEAVQECRN-AEEKAKKAITDAAMMAEELKKEQDTS-----------AHLERMKK 1786
Cdd:TIGR01612 1435 ESNIDTYFKNADENNENVLLLFKNIEMADNKSQHiLKIKKDNATNDHDFNINELKEHIDKSkgckdeadknaKAIEKNKE 1514
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1787 NMEQTIKDLQHRLDEAEQIALKGG----KKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKN 1862
Cdd:TIGR01612 1515 LFEQYKKDVTELLNKYSALAIKNKfaktKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKA 1594
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1863 LLRLQDLVDKLQ---LKVKAYKRQAEEA---EEQANTNLSKFR--KVQHELDEAEERADIAESQVNKLRAKSRDIGAKQK 1934
Cdd:TIGR01612 1595 AIDIQLSLENFEnkfLKISDIKKKINDClkeTESIEKKISSFSidSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKK 1674
|
....
gi 124376530 1935 MHDE 1938
Cdd:TIGR01612 1675 ELDE 1678
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1671-1919 |
6.71e-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: 44.37 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1671 ENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQEC 1750
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1751 RNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEaeqialkggkkqLQKLEARVRELEG 1826
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEE------------LRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1827 ELEAEQKrnaesvkgmrkserrikELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELD 1906
Cdd:COG4942 168 ELEAERA-----------------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
250
....*....|...
gi 124376530 1907 EAEERADIAESQV 1919
Cdd:COG4942 231 RLEAEAAAAAERT 243
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
845-1000 |
6.82e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 845 AETEKEMATMKEEfgRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEErcdQLIKNKIQLEAKVKEM 924
Cdd:PRK12704 45 EEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE---LLEKREEELEKKEKEL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 925 NERLEDEEEMNAELTAKKRKLEDE---CSELKKDiDDLELTLAKVEKE-KHATENKVKNLTEEmagldeiiAKLTKEKKA 1000
Cdd:PRK12704 120 EQKQQELEKKEEELEELIEEQLQElerISGLTAE-EAKEILLEKVEEEaRHEAAVLIKEIEEE--------AKEEADKKA 190
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1573-1902 |
6.95e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.96 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1573 EIERKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLshANRMAAEAQKQVKSLQSLL 1652
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL--YLDYLKLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1653 KDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKM 1732
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1733 ESDLTQLQS-----EVEEAVQECRNAEEKAKKaitdAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAL 1807
Cdd:pfam02463 327 EKELKKEKEeieelEKELKELEIKREAEEEEE----EELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1808 KGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEA 1887
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
330
....*....|....*
gi 124376530 1888 EEQANTNLSKFRKVQ 1902
Cdd:pfam02463 483 QEQLELLLSRQKLEE 497
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1644-1928 |
7.24e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.51 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1644 QVKSLQSLLKDTQ---IQLDDA-VRANDDLKEniaiVERRNNLLQAELEELRAVVEQTERSRKLAEQELIetseRVQLLH 1719
Cdd:PLN02939 129 QLEDLVGMIQNAEkniLLLNQArLQALEDLEK----ILTEKEALQGKINILEMRLSETDARIKLAAQEKI----HVEILE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1720 SQntsLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTS---AHLERMKKNMEQTIKDLQ 1796
Cdd:PLN02939 201 EQ---LEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEervFKLEKERSLLDASLRELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1797 HRLDEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESV---KGMRKSERRIKELTYQTEEDKKNLLRLQdLVDKL 1873
Cdd:PLN02939 278 SKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAAlvlDQNQDLRDKVDKLEASLKEANVSKFSSY-KVELL 356
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 124376530 1874 QLKVKAYKRQAEEAEEQANTnlskfrKVQHELDEAEERADIAESQVNKLRAKSRD 1928
Cdd:PLN02939 357 QQKLKLLEERLQASDHEIHS------YIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1543-1922 |
7.44e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1543 QSALEEAEASLEHEEGKILRAQLEFNQIKaEIERKLaekDEEMEQAKRNHQrvvdSLQTSLDAETRSRNEVLrvkKKMEG 1622
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQELL-ESEEKN---REEVEQLKDLYR----ELRKSLLANRFSFGPAL---DELEK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1623 DLNEMEIQLSHANRMAA-----EAQKQVKSLQSLLKDTQIQLDDavranddlkenI-AIVERRNNLLQAELEELRAVVEQ 1696
Cdd:PRK04778 173 QLENLEEEFSQFVELTEsgdyvEAREILDQLEEELAALEQIMEE-----------IpELLKELQTELPDQLQELKAGYRE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1697 -TERSRKLAEQELIETSERVQLLHSQNTSLINQK--KKMESDLTQLQSEVE------EAVQECRNAEEKAKKAITDAAMM 1767
Cdd:PRK04778 242 lVEEGYHLDHLDIEKEIQDLKEQIDENLALLEELdlDEAEEKNEEIQERIDqlydilEREVKARKYVEKNSDTLPDFLEH 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1768 AEELKKEqdTSAHLERMKKN-------------MEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELEGEL---EAE 1831
Cdd:PRK04778 322 AKEQNKE--LKEEIDRVKQSytlneselesvrqLEKQLESLEKQYDEITE-RIAEQEIAYSELQEELEEILKQLeeiEKE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1832 QKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRlqdLVDKLQL-----KVKAYKRQAEEAEEQANTNLSKFR----KVQ 1902
Cdd:PRK04778 399 QEKLSEMLQGLRKDELEAREKLERYRNKLHEIKR---YLEKSNLpglpeDYLEMFFEVSDEIEALAEELEEKPinmeAVN 475
|
410 420
....*....|....*....|
gi 124376530 1903 HELDEAEERADIAESQVNKL 1922
Cdd:PRK04778 476 RLLEEATEDVETLEEETEEL 495
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
875-1179 |
7.66e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 875 LEEKMVSLLQEKNDLQLqVQAEQDNLNDAEERcdqlIKNKIQLEAKVKEMNERLEDEeeMNAELTAKKRKLEDECSELKK 954
Cdd:PRK05771 14 LKSYKDEVLEALHELGV-VHIEDLKEELSNER----LRKLRSLLTKLSEALDKLRSY--LPKLNPLREEKKKVSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 955 DIDDLELTLAKVEKEkhatenkVKNLTEEMAGLDEIIAKLTKEKKALqeahqQALDDLQVEEDKVNSLSKSKVKLEQQVD 1034
Cdd:PRK05771 87 LIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERL-----EPWGNFDLDLSLLLGFKYVSVFVGTVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1035 DLEGSLEQEKKVRMDLERAKRKLEGDLkltqeSIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLAlQLQKKLKEnq 1114
Cdd:PRK05771 155 DKLEELKLESDVENVEYISTDKGYVYV-----VVVVLKELSDEVEEELKKLGFERLELEEEGTPSELIR-EIKEELEE-- 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124376530 1115 arieeleeeleaertarakVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRD 1179
Cdd:PRK05771 227 -------------------IEKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSKFLKT 272
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1386-1933 |
7.68e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.25 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1386 EELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKhrlqNEIEDLMVDVERsnaaaAALDKKQRNFDKILAEWKQKyees 1465
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTK----RLIEELKLNLER-----AQTEEAQAKQDSELAKLRVE---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1466 QSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVH-------ELEKVRKQLEVE 1538
Cdd:pfam05701 109 EMEQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEeavsaskEIEKTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1539 KLELQSALEEAEAS-LEHEEGKIlRAQLEFNQIKAEIERKLAEKDEEMEQAkRNHQRVVDSLQTSLDAetrsrNEVLRVK 1617
Cdd:pfam05701 189 LIATKESLESAHAAhLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-----ASALLLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1618 KK------MEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDdavRANDDLKENIAIVERrnnlLQAELEELR 1691
Cdd:pfam05701 262 LKaelaayMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIE---KAKDEVNCLRVAAAS----LRSELEKEK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1692 AVVEQTERSRKLA-------EQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDa 1764
Cdd:pfam05701 335 AELASLRQREGMAsiavsslEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEE- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1765 ammAEELKKEQDT-SAHLERMKKNMEQTIkdlqhrldEAEQIALkggkkqlqkleARVRELEgelEAEQKRNAESVKGMR 1843
Cdd:pfam05701 414 ---AEQAKAAASTvESRLEAVLKEIEAAK--------ASEKLAL-----------AAIKALQ---ESESSAESTNQEDSP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1844 KSerrikeLTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKlr 1923
Cdd:pfam05701 469 RG------VTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIALEKAEK-- 540
|
570
....*....|
gi 124376530 1924 AKSRDIGAKQ 1933
Cdd:pfam05701 541 AKEGKLAAEQ 550
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1025-1450 |
7.78e-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: 44.35 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1025 SKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDINQQ-----NSKIEDE 1099
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQaelnrLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1100 QVLALQLQKKLKENQARiEELEEELEAERTARAKVEKLRSDLSR---ELEEISERLEEAGGATSvqiEMNKKREaEFQKM 1176
Cdd:pfam05557 87 ALNKKLNEKESQLADAR-EVISCLKNELSELRRQIQRAELELQStnsELEELQERLDLLKAKAS---EAEQLRQ-NLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1177 RRDLEEATLQHEATAAALRKKHADSV------AELgEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKV 1250
Cdd:pfam05557 162 QSSLAEAEQRIKELEFEIQSQEQDSEivknskSEL-ARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1251 SRTLEDQANeYRVKLEEAQRSLNDFTtqraKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNA 1330
Cdd:pfam05557 241 EKYREEAAT-LELEKEKLEQELQSWV----KLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1331 LAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEelEEAKKKLAQRLQDAEEAVEAVN 1410
Cdd:pfam05557 316 LEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTM--SNYSPQLLERIEEAEDMTQKMQ 393
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 124376530 1411 AKCSSLEktkHRLQNEIEDLMVDVERSNAAAAALDKKQRN 1450
Cdd:pfam05557 394 AHNEEME---AQLSVAEEELGGYKQQAQTLERELQALRQQ 430
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
863-1036 |
7.92e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 44.54 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 863 ETLEKSEARRKELEEKMVSLLQEkndLQLQVQAEQDNLN------DAEERCDQLIKNKIQLEAK-VKEMNERLEDEEEMN 935
Cdd:PLN03188 1047 KKLEQERLRWTEAESKWISLAEE---LRTELDASRALAEkqkhelDTEKRCAEELKEAMQMAMEgHARMLEQYADLEEKH 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 936 AELTAKKRKLEDECSELKKD-------------IDDL--ELTLAKVEKEKHAT----ENK-----VKNLTEEMAGLDEII 991
Cdd:PLN03188 1124 IQLLARHRRIQEGIDDVKKAaaragvrgaeskfINALaaEISALKVEREKERRylrdENKslqaqLRDTAEAVQAAGELL 1203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 124376530 992 AKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDL 1036
Cdd:PLN03188 1204 VRLKEAEEALTVAQKRAMDAEQEAAEAYKQIDKLKRKHENEISTL 1248
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1235-1449 |
8.07e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1235 SNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTrgklsytQQM 1314
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR-------EEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1315 EDLKRQLEEEGKAKNALAhALQSARHDCDLLReqyeeeteaKAELQRVLSKANSEVAQwrtkyetDAIQRTEELEEAKKK 1394
Cdd:COG3883 89 GERARALYRSGGSVSYLD-VLLGSESFSDFLD---------RLSALSKIADADADLLE-------ELKADKAELEAKKAE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 124376530 1395 LAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQR 1449
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1527-1798 |
8.48e-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: 44.34 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1527 ELEKVRkqLEVEKLELQSALEEaEASLEHEEGKIL-RAQLEFNQ----IKAEIERKLAEKDEEMEQAKRNHQRVVDSLQT 1601
Cdd:pfam17380 349 ELERIR--QEERKRELERIRQE-EIAMEISRMRELeRLQMERQQknerVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1602 SLDAETRSRNEVLRVKKKMEgdlNEMEiqlshanRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNN 1681
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERA---REME-------RVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1682 LLQAELEELRAVVEQTERSRKLAEQELIEtservqllhSQNTSLINQKKKMESDLTQLQSEVEEavqecrnaeekaKKAI 1761
Cdd:pfam17380 496 ILEKELEERKQAMIEEERKRKLLEKEMEE---------RQKAIYEEERRREAEEERRKQQEMEE------------RRRI 554
|
250 260 270
....*....|....*....|....*....|....*..
gi 124376530 1762 TDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHR 1798
Cdd:pfam17380 555 QEQMRKATEERSRLEA---MEREREMMRQIVESEKAR 588
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1498-1853 |
9.32e-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: 44.12 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1498 ETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLELQsalEEAEASLEHEEGKILRAQLEFNQIKAEIERK 1577
Cdd:pfam07888 69 EQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS---EEKDALLAQRAAHEARIRELEEDIKTLTQRV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1578 LaEKDEEMEQAKRNHQRVvdslqtsldaeTRSRNEVLRVKKKMEGDLNEMEIQLshaNRMAAEAQKQVKSLQSllKDTQI 1657
Cdd:pfam07888 146 L-ERETELERMKERAKKA-----------GAQRKEEEAERKQLQAKLQQTEEEL---RSLSKEFQELRNSLAQ--RDTQV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1658 -QLDDAVRAnddLKENIAIVERRNNLLQAELEELRAVveqtersrklaeQELIETSER-VQLLHSQNTSLINQKKKMESD 1735
Cdd:pfam07888 209 lQLQDTITT---LTQKLTTAHRKEAENEALLEELRSL------------QERLNASERkVEGLGEELSSMAAQRDRTQAE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1736 LTQLQSEVEE----------AVQECRNAEEKAKKAITDAAMMAEElkKEQDTSAHLERMKKNMEQTIKDLQH------RL 1799
Cdd:pfam07888 274 LHQARLQAAQltlqladaslALREGRARWAQERETLQQSAEADKD--RIEKLSAELQRLEERLQEERMEREKlevelgRE 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 124376530 1800 DEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELT 1853
Cdd:pfam07888 352 KDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1247-1448 |
9.57e-04 |
|
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: 44.07 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1247 LEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGK 1326
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1327 AKNALAHALQSARHdcdllREQYEEETEAKAELQRVLSKANSevaqwrtkyeTDAI-QRTEELEEAKKKLAQRLQDAEEA 1405
Cdd:pfam09726 480 ARASAEKQLAEEKK-----RKKEEEATAARAVALAAASRGEC----------TESLkQRKRELESEIKKLTHDIKLKEEQ 544
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 124376530 1406 VEAVNAKCSSLEKTKHRlQNEIEDLMvdversNAAAAALDKKQ 1448
Cdd:pfam09726 545 IRELEIKVQELRKYKES-EKDTEVLM------SALSAMQDKNQ 580
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1599-1924 |
1.01e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1599 LQTSLDAETRSRNEVLR----VKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIA 1674
Cdd:pfam07888 32 LQNRLEECLQERAELLQaqeaANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1675 IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNae 1754
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRS-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1755 ekakkaitdaamMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQ--IALKGGKKQLQKLEARVRELEGELEAeQ 1832
Cdd:pfam07888 190 ------------LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeAENEALLEELRSLQERLNASERKVEG-L 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1833 KRNAESVKGMRksERRIKELTYQTEEDKKNLLRLQDLvdKLQLKVKAYKRQAEEAEEQANTNLSKFR--KVQHELDEAEE 1910
Cdd:pfam07888 257 GEELSSMAAQR--DRTQAELHQARLQAAQLTLQLADA--SLALREGRARWAQERETLQQSAEADKDRieKLSAELQRLEE 332
|
330
....*....|....
gi 124376530 1911 RADIAESQVNKLRA 1924
Cdd:pfam07888 333 RLQEERMEREKLEV 346
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1329-1889 |
1.01e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1329 NALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYE--TDAIQRTEELEEAKKKLAQRLQDAEEAV 1406
Cdd:PRK01156 186 DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDMKNRYESEIKTAESDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1407 EAVNAKCSSLEKTKHRLqNEIEDLMVDVERSNAAAAALDKKQ-RNFDKILAEWK---QKYEESQSELEssqkEARSLSTE 1482
Cdd:PRK01156 266 SMELEKNNYYKELEERH-MKIINDPVYKNRNYINDYFKYKNDiENKKQILSNIDaeiNKYHAIIKKLS----VLQKDYND 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1483 LFKLKNAYEE---SLEHLETFKRENKNLQEEISDLTEQLGEGGKNVH----ELEKVRKQLEVEKLELQSALEEAEASLEH 1555
Cdd:PRK01156 341 YIKKKSRYDDlnnQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIErmsaFISEILKIQEIDPDAIKKELNEINVKLQD 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1556 EEGKILraqlEFNQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHAN 1635
Cdd:PRK01156 421 ISSKVS----SLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDID 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1636 rmaaEAQKQVKSLQSLLkdtqiqlddavrANDDLKENIAiVERRNNLLQAELEELRaVVEQTERSRKLAEQELIE--TSE 1713
Cdd:PRK01156 497 ----EKIVDLKKRKEYL------------ESEEINKSIN-EYNKIESARADLEDIK-IKINELKDKHDKYEEIKNryKSL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1714 RVQLLHSQNTSLINQKKKMES-DLTQLQSEVEEAVQECRNAEEKakkaitdaamMAEELKKEQDTSAHLERMKKNMEQTI 1792
Cdd:PRK01156 559 KLEDLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESR----------LQEIEIGFPDDKSYIDKSIREIENEA 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1793 KDLQHRLDEAEqiALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDK 1872
Cdd:PRK01156 629 NNLNNKYNEIQ--ENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEI 706
|
570
....*....|....*..
gi 124376530 1873 LQLKVKAYKRQAEEAEE 1889
Cdd:PRK01156 707 LRTRINELSDRINDINE 723
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1624-1765 |
1.05e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1624 LNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQA---------ELEELRAVV 1694
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124376530 1695 EQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAA 1765
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1130-1363 |
1.08e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1130 ARAKVEKLRSDLSRELEEISERLEEaggatsvqiEMNKKR--EAEFQKMRRDLEEATLQH---EATA-------AALRKK 1197
Cdd:pfam00038 69 ERARLQLELDNLRLAAEDFRQKYED---------ELNLRTsaENDLVGLRKDLDEATLARvdlEAKIeslkeelAFLKKN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1198 HADSVAELGEQIDNLQRVkqklekeksefkLELDDVTS-NMEQIIK-AKANLEKVSRTLEDQANE-YRVKLEEAQRSLND 1274
Cdd:pfam00038 140 HEEEVRELQAQVSDTQVN------------VEMDAARKlDLTSALAeIRAQYEEIAAKNREEAEEwYQSKLEELQQAAAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1275 FTTQRAKLQTENGELARQLEEKEALISQLTRgklsytqQMEDLKRQLEEegkAKNALAHALQSARhdcDLLREQYEEETE 1354
Cdd:pfam00038 208 NGDALRSAKEEITELRRTIQSLEIELQSLKK-------QKASLERQLAE---TEERYELQLADYQ---ELISELEAELQE 274
|
....*....
gi 124376530 1355 AKAELQRVL 1363
Cdd:pfam00038 275 TRQEMARQL 283
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
767-1112 |
1.13e-03 |
|
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: 44.17 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 767 FKAGLLGLLEEMR---------DERLSRIITRMQaqargqlmRIEFKKIVERRDALLVIQWNIRAFMGVKNWPWMKLYF- 836
Cdd:pfam15818 5 FKTSLLEALEELRmrreaetqyEEQIGKIIVETQ--------ELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCAl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 837 ---KIKPLLKSAETEKEMATMKEefgrikeTLEKSEARRKELEEKmVSLLQEKndLQLQVQAEQD---NLNDAEeRCDQL 910
Cdd:pfam15818 77 eeeKGKYQLATEIKEKEIEGLKE-------TLKALQVSKYSLQKK-VSEMEQK--LQLHLLAKEDhhkQLNEIE-KYYAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 911 IKNKIQLeakVKEMNERLE----DEEEMNAELTAKKRKLEDECSELKKDIDDL--ELTLAKVEKEKHATENKVkNLTEEM 984
Cdd:pfam15818 146 ITGQFGL---VKENHGKLEqnvqEAIQLNKRLSALNKKQESEICSLKKELKKVtsDLIKSKVTCQYKMGEENI-NLTIKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 985 AGLDEIIAKLTKEKkALQEAHQQALDDLQVE-EDKVNSLSKSKVKLEQQVD---DLEGSLEQEKKVRMDLERAKRKLEGD 1060
Cdd:pfam15818 222 QKFQELQERLNMEL-ELNKKINEEITHIQEEkQDIIISFQHMQQLLQQQTQantEMEAELKALKENNQTLERDNELQREK 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 124376530 1061 LKLTQESIMDLENDKLQLEEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKE 1112
Cdd:pfam15818 301 VKENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1513-1795 |
1.18e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.91 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1513 DLTEQLGEGGKNVHELEKVRKQLEveklELQSALEEAEASLEheegkILRAQLEfnqikaEIER-KLAEKDEE--MEQAK 1589
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELE----ELRADEAERARELD-----LLRFQLE------ELEAaALQPGEEEelEEERR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1590 R--NHQRVVDSLQTSLDAetrsrnevlrvkkkmegdLNEMEI----QLSHANRM---AAEAQKQVKSLQSLLKDTQIQLD 1660
Cdd:COG0497 217 RlsNAEKLREALQEALEA------------------LSGGEGgaldLLGQALRAlerLAEYDPSLAELAERLESALIELE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1661 DAVRanddlkeniaiverrnnllqaeleELRAVVEQTErsrkLAEQELIETSERVQLLHS-------QNTSLINQKKKME 1733
Cdd:COG0497 279 EAAS------------------------ELRRYLDSLE----FDPERLEEVEERLALLRRlarkygvTVEELLAYAEELR 330
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124376530 1734 SDLTQLQSeVEEAVQECRNAEEKAKKAITDAammAEEL-KKEQDTSAHLErmkKNMEQTIKDL 1795
Cdd:COG0497 331 AELAELEN-SDERLEELEAELAEAEAELLEA---AEKLsAARKKAAKKLE---KAVTAELADL 386
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1630-1835 |
1.36e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 42.32 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1630 QLSHANRMAAEAQKQVKSLQSLLKDTQIQLDdavRANDDLKENiaiverrnnllQAELEELRAVVEQTERSRKLAEQELI 1709
Cdd:pfam00261 23 KLEEAEKRAEKAEAEVAALNRRIQLLEEELE---RTEERLAEA-----------LEKLEEAEKAADESERGRKVLENRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1710 ETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLE------- 1782
Cdd:pfam00261 89 KDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEaseekas 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 124376530 1783 RMKKNMEQTIKDLQHRLDEAEQIALKGgKKQLQKLEARVRELEGELEAEQKRN 1835
Cdd:pfam00261 169 EREDKYEEQIRFLTEKLKEAETRAEFA-ERSVQKLEKEVDRLEDELEAEKEKY 220
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
978-1114 |
1.37e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 978 KNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEgsLEQEKKVRMDLERAKRKL 1057
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLL--EEAEKEAQQAIKEAKKEA 586
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 124376530 1058 EGDLK-LTQESIMDLENDKLQ-LEEKLKKkefdINQQNSKIEDEQVLALQLQKKLKENQ 1114
Cdd:PRK00409 587 DEIIKeLRQLQKGGYASVKAHeLIEARKR----LNKANEKKEKKKKKQKEKQEELKVGD 641
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1133-1396 |
1.39e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1133 KVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKmrrDLEEATLQHEataaalrkkhaDSVAELGEQIDNL 1212
Cdd:PRK05771 47 KLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIK---DVEEELEKIE-----------KEIKELEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1213 QRVKQKLEKEKSE------FKLELDDVTSN-MEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTE 1285
Cdd:PRK05771 113 ENEIKELEQEIERlepwgnFDLDLSLLLGFkYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1286 NGELARQLEEKEALISqlTRGKLSytQQMEDLKRQLEEEGKAKNALAHALqsarhdCDLLREQYEEETEAKAELQRVLSK 1365
Cdd:PRK05771 193 VEEELKKLGFERLELE--EEGTPS--ELIREIKEELEEIEKERESLLEEL------KELAKKYLEELLALYEYLEIELER 262
|
250 260 270
....*....|....*....|....*....|....*..
gi 124376530 1366 ANSEVAQWRTKYeTDAIQ------RTEELEEAKKKLA 1396
Cdd:PRK05771 263 AEALSKFLKTDK-TFAIEgwvpedRVKKLKELIDKAT 298
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
861-997 |
1.46e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 861 IKETLEKSEARRKELEEKmvsllqeknDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTA 940
Cdd:COG2433 378 IEEALEELIEKELPEEEP---------EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124376530 941 KKRKL----------EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLtEEMAGLDE--------IIAKLTKE 997
Cdd:COG2433 449 ELSEArseerreirkDREISRLDREIERLERELEEERERIEELKRKLERL-KELWKLEHsgelvpvkVVEKFTKE 522
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1143-1412 |
1.62e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1143 RELEEISERLEEAggatsvqiemnKKR-EAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELgeqidnLQRVKQKLEK 1221
Cdd:PRK05035 439 RAIEQEKKKAEEA-----------KARfEARQARLEREKAAREARHKKAAEARAAKDKDAVAAA------LARVKAKKAA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1222 EKSEFKLELDDVTSNMEQIIKAKAnlekvsrtledqaneyrVKLEEAQRslndfttqRAKLQTENGELARqleeKEALIS 1301
Cdd:PRK05035 502 ATQPIVIKAGARPDNSAVIAAREA-----------------RKAQARAR--------QAEKQAAAAADPK----KAAVAA 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1302 QLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALqsARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDA 1381
Cdd:PRK05035 553 AIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAI--ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAE 630
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 124376530 1382 IQRTEELEE---------------AKKKLAQRLQDAEEAVEAVNAK 1412
Cdd:PRK05035 631 QQANAEPEEpvdprkaavaaaiarAKARKAAQQQANAEPEEAEDPK 676
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1689-1873 |
1.77e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1689 ELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKK---AITDAA 1765
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1766 MMAEELKKE--------------QDTSAHLERMKKNMEQtIKDLQHRLDEAE--QIALKGGKKQLQKLEARVRELEGELE 1829
Cdd:PHA02562 269 SKIEQFQKVikmyekggvcptctQQISEGPDRITKIKDK-LKELQHSLEKLDtaIDELEEIMDEFNEQSKKLLELKNKIS 347
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 124376530 1830 AEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKL 1873
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
841-1091 |
1.79e-03 |
|
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: 42.74 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 841 LLKSAETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQ---------EKNDLQLQVQAEQDNLNDAEERCDQLI 911
Cdd:pfam15742 99 VLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQQKLEHAHKvcltdtcilEKKQLEERIKEASENEAKLKQQYQEEQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 912 KNKIQLEAKVKEMNERLEDeeemnaeLTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEemagLDEII 991
Cdd:pfam15742 179 QKRKLLDQNVNELQQQVRS-------LQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQE----LSEKL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 992 AKLTKEKKALQEAHQQALDDLQVEEDKVNslskskvkleqqvddlegslEQEKKVRMDLERAKRKLEGDLKLTQESIMDL 1071
Cdd:pfam15742 248 SSLQQEKEALQEELQQVLKQLDVHVRKYN--------------------EKHHHHKAKLRRAKDRLVHEVEQRDERIKQL 307
|
250 260
....*....|....*....|
gi 124376530 1072 ENDKLQLEEKLKKKEFDINQ 1091
Cdd:pfam15742 308 ENEIGILQQQSEKEKAFQKQ 327
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1779-1925 |
1.82e-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: 42.22 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1779 AHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELEGELEAEQKRNAESVK--GMRKSERRIKELTYQT 1856
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124376530 1857 EEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1925
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1383-1591 |
1.82e-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: 42.22 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1383 QRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKilaewkqky 1462
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1463 eesqselessQKEARSLSTElfklknayeeslehLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEVEKLEL 1542
Cdd:COG1579 88 ----------NKEYEALQKE--------------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 124376530 1543 QSALEEAEASLEhEEGKILRAQLEfnQIKAEIERKLAEKDEEMEQAKRN 1591
Cdd:COG1579 144 KAELDEELAELE-AELEELEAERE--ELAAKIPPELLALYERIRKRKNG 189
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
904-1079 |
2.03e-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: 42.31 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 904 EERCDQLIKNKIQLEAKVKEMNErleDEEEMNAELTakkrkledECSELKKDIDDLELTL-AKVEKEKHATENKVKNLTE 982
Cdd:smart00787 136 EWRMKLLEGLKEGLDENLEGLKE---DYKLLMKELE--------LLNSIKPKLRDRKDALeEELRQLKQLEDELEDCDPT 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 983 EMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKV-RMDLERAKRKLEGDL 1061
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFtFKEIEKLKEQLKLLQ 284
|
170
....*....|....*...
gi 124376530 1062 KLTQESIMDLENDKLQLE 1079
Cdd:smart00787 285 SLTGWKITKLSGNTLSMT 302
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
962-1172 |
2.11e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 962 TLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLE 1041
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1042 ------QEKKVRMD--------------LERA---KRKLEGDLKLTQEsimdLENDKLQLEEKLKKKEFDINQQNSKIED 1098
Cdd:COG3883 90 eraralYRSGGSVSyldvllgsesfsdfLDRLsalSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124376530 1099 EQVLALQLQKKLKENQARIeelEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAE 1172
Cdd:COG3883 166 LEAAKAELEAQQAEQEALL---AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1434-1707 |
2.15e-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: 43.02 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1434 VERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARslstelFKLKNAYEESLEHLETfkrENKNLQEEISD 1513
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAA------AEAEQELEESKRETET---GIQNLTAEIEQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1514 LTEQLGEGgknvheLEKVRKqlEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQ 1593
Cdd:COG5185 348 GQESLTEN------LEAIKE--EIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1594 RVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEiQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENI 1673
Cdd:COG5185 420 RQIEELQRQIEQATSSNEEVSKLLNELISELNKVM-READEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLK 498
|
250 260 270
....*....|....*....|....*....|....
gi 124376530 1674 AIVERRNNLLQAELEELRAVVEQTERSRKLAEQE 1707
Cdd:COG5185 499 ATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
867-1016 |
2.22e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 867 KSEARRKELEEKMVSLLQEKNdlqlqvqaeqdnlNDAEErcdqlIKNKIQLEAKVKEMNERLEDEEE---MNAELTAKKR 943
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAK-------------KEAEA-----IKKEALLEAKEEIHKLRNEFEKElreRRNELQKLEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 944 KLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAK----------LTKEkkalqEAHQQALDdlQ 1013
Cdd:PRK12704 90 RLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEqlqelerisgLTAE-----EAKEILLE--K 162
|
...
gi 124376530 1014 VEE 1016
Cdd:PRK12704 163 VEE 165
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1549-1779 |
2.24e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1549 AEASLEHEEGKILRAQLEfnqiKAEIERKLAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVlrvkKKMEGDLNEME 1628
Cdd:COG3883 14 ADPQIQAKQKELSELQAE----LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI----AEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1629 IQLSHANRMAAEAQKQVKSLQSLLKDTQIqlDDAVRANDDLKeniAIVERRNNLL------QAELEELRAVVEQTERSRK 1702
Cdd:COG3883 86 EELGERARALYRSGGSVSYLDVLLGSESF--SDFLDRLSALS---KIADADADLLeelkadKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1703 LAEQELIETSERVQLLHSQNTSLIN----QKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTS 1778
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAqlsaEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
.
gi 124376530 1779 A 1779
Cdd:COG3883 241 A 241
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
843-1585 |
2.27e-03 |
|
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: 43.12 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 843 KSAETEKEMATMKEEFGRIKETL-----EKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERcdqLIKNKIQL 917
Cdd:TIGR01612 994 KNNELIKYFNDLKANLGKNKENMlyhqfDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEK---EIGKNIEL 1070
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 918 ---------EAKVKEMNERLEDEEEMNAELTAKKR--KLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAG 986
Cdd:TIGR01612 1071 lnkeileeaEINITNFNEIKEKLKHYNFDDFGKEEniKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKA 1150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 987 LDEIIAKLTKEKKALQ--EAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEG---SLEQEKKVRMD------------ 1049
Cdd:TIGR01612 1151 QINDLEDVADKAISNDdpEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKdktSLEEVKGINLSygknlgklflek 1230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1050 LERAKRKLEGDLKLTQESIMDLENdklqleeklkkkefdINQQNSKIEDEQVLALQLQKKLKEnqarIEELEEELEAERT 1129
Cdd:TIGR01612 1231 IDEEKKKSEHMIKAMEAYIEDLDE---------------IKEKSPEIENEMGIEMDIKAEMET----FNISHDDDKDHHI 1291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1130 ARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMnKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVaelgeqI 1209
Cdd:TIGR01612 1292 ISKKHDENISDIREKSLKIIEDFSEESDINDIKKEL-QKNLLDAQKHNSDINLYLNEIANIYNILKLNKIKKI------I 1364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1210 DNLQRVKQKLEKEKSEFKLELDDvTSNMEQIIKAKANLE----KVSRTLEDQ-ANEYRVKLEE------AQRSLNDFTTQ 1278
Cdd:TIGR01612 1365 DEVKEYTKEIEENNKNIKDELDK-SEKLIKKIKDDINLEecksKIESTLDDKdIDECIKKIKElknhilSEESNIDTYFK 1443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1279 RAK-------LQTENGELARQlEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNAlAHALQSARHDCDLLREQYee 1351
Cdd:TIGR01612 1444 NADennenvlLLFKNIEMADN-KSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDE-ADKNAKAIEKNKELFEQY-- 1519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1352 eteaKAELQRVLSKANS-EVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEaveavnaKCSSLEKTKHRlqneIEDL 1430
Cdd:TIGR01612 1520 ----KKDVTELLNKYSAlAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQ-------KIKEIKKEKFR----IEDD 1584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1431 MVDVERSNAAAAALDKKQRNFDKIL---AEWKQKYEESQSELESSQKEARSLS-----TELFKLKNAYEESLEHLETFKR 1502
Cdd:TIGR01612 1585 AAKNDKSNKAAIDIQLSLENFENKFlkiSDIKKKINDCLKETESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKD 1664
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1503 ENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLE---VEKLE--LQSALEEAEASLEHEEGKILRAQLEFNQIKAE---I 1574
Cdd:TIGR01612 1665 QKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEigiIEKIKeiAIANKEEIESIKELIEPTIENLISSFNTNDLEgidP 1744
|
810
....*....|.
gi 124376530 1575 ERKLAEKDEEM 1585
Cdd:TIGR01612 1745 NEKLEEYNTEI 1755
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1760-1939 |
2.30e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1760 AITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELEGELEAEQKRNAESV 1839
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1840 KGMRKSERRIKELT-----YQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADI 1914
Cdd:COG3883 93 RALYRSGGSVSYLDvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180
....*....|....*....|....*
gi 124376530 1915 AESQVNKLRAKSRDIGAKQKMHDEE 1939
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQ 197
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
852-1175 |
2.32e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 852 ATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDE 931
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 932 EEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAH-QQALD 1010
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1011 DLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDIN 1090
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1091 QQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKRE 1170
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
....*
gi 124376530 1171 AEFQK 1175
Cdd:COG4372 347 LVGLL 351
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1575-1838 |
2.40e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.12 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1575 ERKLAEKDEEMEQAKRNHQ-RVVDSLQTSLDAetrsrnevlrvkkkmegdLNEMEIqlshANRMAAEAQKQVKSLQSLLK 1653
Cdd:PRK10929 25 EKQITQELEQAKAAKTPAQaEIVEALQSALNW------------------LEERKG----SLERAKQYQQVIDNFPKLSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1654 DTQIQLDDAVRANDDLKENIAIVERRNNLLQAE---LEELRAVVEQTERSRKLAE-------------QELIETSERVQL 1717
Cdd:PRK10929 83 ELRQQLNNERDEPRSVPPNMSTDALEQEILQVSsqlLEKSRQAQQEQDRAREISDslsqlpqqqtearRQLNEIERRLQT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1718 LHSQNTSLinqkkkMESDLTQLQseveeavqecrnAEEKAKKAITDaammaeELKkeqdtsahLERMKKNMEQTIKDLQH 1797
Cdd:PRK10929 163 LGTPNTPL------AQAQLTALQ------------AESAALKALVD------ELE--------LAQLSANNRQELARLRS 210
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 124376530 1798 RLdeaeqialkgGKKQLQKLEARVRELEGELEAEQKRNAES 1838
Cdd:PRK10929 211 EL----------AKKRSQQLDAYLQALRNQLNSQRQREAER 241
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
898-1756 |
2.47e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 898 DNLNDAEERcDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATEnKV 977
Cdd:COG3096 272 DYMRHANER-RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQE-KI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 978 KNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKL 1057
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1058 EGDlKLTQESIMDLENDKLQLEEKLKKKEFDINQQNS-----KIEDEQvlALQLQKKLKENQARIEELEEELEAERTARA 1132
Cdd:COG3096 430 GLP-DLTPENAEDYLAAFRAKEQQATEEVLELEQKLSvadaaRRQFEK--AYELVCKIAGEVERSQAWQTARELLRRYRS 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1133 KVEKL--RSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKmRRDLEEatlqHEATAAALRKKHADSVAELGEQID 1210
Cdd:COG3096 507 QQALAqrLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEE----LLAELEAQLEELEEQAAEAVEQRS 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1211 NLQRvkqklekeksefklELDDVTsnmeQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKL-------Q 1283
Cdd:COG3096 582 ELRQ--------------QLEQLR----ARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLlerereaT 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1284 TENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEE---------------------GKAKNAL--------AHA 1334
Cdd:COG3096 644 VERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGGVllseiyddvtledapyfsalyGPARHAIvvpdlsavKEQ 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1335 LQsARHDC--DLLREQYEEET------EAKAELQRVLSKanSEVAQWR-TKYETDAI-------QRTEELEEAKKKLAQR 1398
Cdd:COG3096 724 LA-GLEDCpeDLYLIEGDPDSfddsvfDAEELEDAVVVK--LSDRQWRySRFPEVPLfgraareKRLEELRAERDELAEQ 800
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1399 LQDAEEAVEavnaKCSSLEKTKHRLQNE------IEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESqseless 1472
Cdd:COG3096 801 YAKASFDVQ----KLQRLHQAFSQFVGGhlavafAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQL------- 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1473 qKEARSLsteLFKLknayeesLEHLETFKRENknLQEEISDLTEQLGEGGKNVHELEKVRKQLEveKLE-LQSALEEAEA 1551
Cdd:COG3096 870 -KEQLQL---LNKL-------LPQANLLADET--LADRLEELREELDAAQEAQAFIQQHGKALA--QLEpLVAVLQSDPE 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1552 SLEHEEGKILRAQLEFNQIKAEIErklaekdeEMEQ--AKRNHQRVVDSLQtsLDAETRSRNEVLRVKkkmegdLNEMEI 1629
Cdd:COG3096 935 QFEQLQADYLQAKEQQRRLKQQIF--------ALSEvvQRRPHFSYEDAVG--LLGENSDLNEKLRAR------LEQAEE 998
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1630 QLSHANRMAAEAQKQVKSLQSLLKDtqiqLDDAVRA-NDDLKEniaiverrnnlLQAELEEL--RAVVEQTERSRklaeq 1706
Cdd:COG3096 999 ARREAREQLRQAQAQYSQYNQVLAS----LKSSRDAkQQTLQE-----------LEQELEELgvQADAEAEERAR----- 1058
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 124376530 1707 elietsERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEK 1756
Cdd:COG3096 1059 ------IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERD 1102
|
|
| ycf1 |
CHL00204 |
Ycf1; Provisional |
827-999 |
2.52e-03 |
|
Ycf1; Provisional
Pssm-ID: 214395 [Multi-domain] Cd Length: 1832 Bit Score: 43.17 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 827 KNWPWMKLYFKIKPLLKSAETEKE------MATMKEE--FGRIKETLEKSEARRKELEEKMVSLlQEKNDLQLQVQAEQD 898
Cdd:CHL00204 866 KPWHRSKLRSSHKDRMKKKKKKKNdfcfltVWGMETElpFGSPRKRPSFFEPIFKELKKKIRKF-KKKYFLVLKILKERT 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 899 N--LNDAEERCDQLIKNKIQLEAKVKEMNERledeeemNAELTAKKRKLeDECSELKKDIDDL-------ELTLAKVEKE 969
Cdd:CHL00204 945 KlfLKVSKETKKWIIKSFLFLKRIIKELSKR-------NPILLFGLREI-YELNETKKEKDSIisnqmihESSVQIRSME 1016
|
170 180 190
....*....|....*....|....*....|...
gi 124376530 970 ---KHATENKVKNLTEEMAGLDEIIAKLTKEKK 999
Cdd:CHL00204 1017 wtnSSLTEKKIKDLTDRTKTIRNQIEKITKEKK 1049
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1389-1606 |
2.57e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1389 EEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAaaaLDKKQRNFDKILAEWKQKYEESQSE 1468
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1469 LESSQKEARSLSTELFKLK-NAYEESLEHLETFKRENKNLQEEISDLTEQLGEggknvheLEKVRKQLEVEKLELQSALE 1547
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGsESFSDFLDRLSALSKIADADADLLEELKADKAE-------LEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124376530 1548 EAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHQRVVDSLQTSLDAE 1606
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1684-1925 |
2.60e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.00 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1684 QAELEELRAVVEQTERSRKLAE-QELietseRVQLLHSQNTSLINQKKK---------MESDLTQLQSEVEEAVQECrnA 1753
Cdd:PLN03188 973 QDELEHYRNFYDMGEREVLLEEiQDL-----RSQLQYYIDSSLPSARKRnsllkltysCEPSQAPPLNTIPESTDES--P 1045
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1754 EEKAKK-------AITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQK---------- 1816
Cdd:PLN03188 1046 EKKLEQerlrwteAESKWISLAEELRTELDASRALAEKQKHELDTEKRCAEELKEAMQMAMEGHARMLEQyadleekhiq 1125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1817 LEARVRELEGELEAEQKrnAESVKGMRKSERRI-----KELTYQTEEDKKNLLRLQDLVDKLQLKVkaykRQAEEAEEQA 1891
Cdd:PLN03188 1126 LLARHRRIQEGIDDVKK--AAARAGVRGAESKFinalaAEISALKVEREKERRYLRDENKSLQAQL----RDTAEAVQAA 1199
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 124376530 1892 NTNLSKFRKVQHELDEAEERADIAE-------SQVNKLRAK 1925
Cdd:PLN03188 1200 GELLVRLKEAEEALTVAQKRAMDAEqeaaeayKQIDKLKRK 1240
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1773-1925 |
3.30e-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: 42.42 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1773 KEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGK------KQLQKLEARVRELEGELEAEQKRNAESVKGMRKSE 1846
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRqldresDRNQELQKRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124376530 1847 RRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1925
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQ 161
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
866-1003 |
3.38e-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: 41.59 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 866 EKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDqliKNKIQLEAKVKEMNERLEDEEEMN-----AELTA 940
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTE---KDQTALETLEKALKDLLTDEGGAIarkeiKDLQK 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124376530 941 KKRKLEDEC-SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQE 1003
Cdd:cd22656 187 ELEKLNEEYaAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEK 250
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
837-1037 |
3.44e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 837 KIKPLLKSAETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCD-------- 908
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEeareevae 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 909 -----QLIKNKIQ--------------LEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKE 969
Cdd:PRK02224 577 lnsklAELKERIEslerirtllaaiadAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKE 656
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124376530 970 khatenkvkNLTEEMAGLDEIIAKLTKEKKALqeahQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLE 1037
Cdd:PRK02224 657 ---------RAEEYLEQVEEKLDELREERDDL----QAEIGAVENELEELEELRERREALENRVEALE 711
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
837-1085 |
3.73e-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: 41.72 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 837 KIKPLLKSAETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAeERCDQLIKNKIQ 916
Cdd:pfam15905 68 NLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLEL-TRVNELLKAKFS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 917 LEAKVKEMN----ERLEDEEEMNA---ELTAKKRKLEDECSELKKD-------IDDLELTLAKVEKEKHATENKVKNLTE 982
Cdd:pfam15905 147 EDGTQKKMSslsmELMKLRNKLEAkmkEVMAKQEGMEGKLQVTQKNlehskgkVAQLEEKLVSTEKEKIEEKSETEKLLE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 983 EMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLK 1062
Cdd:pfam15905 227 YITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLN 306
|
250 260
....*....|....*....|...
gi 124376530 1063 LTQESIMDLENDKLQLEEKLKKK 1085
Cdd:pfam15905 307 AELEELKEKLTLEEQEHQKLQQK 329
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
845-1153 |
3.77e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 845 AETEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEM 924
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 925 NERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKE------K 998
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaeqalD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 999 KALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQL 1078
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124376530 1079 EEKLKKKEFDINQQNSKIEDEQVLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLE 1153
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1607-1861 |
4.18e-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: 41.34 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1607 TRSRNEVLRVKKKMEGDLNEM------EIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRN 1680
Cdd:pfam15905 52 TARKVKSLELKKKSQKNLKESkdqkelEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1681 NLLQAELEELRAVVEQTERSRKLA--EQELIETSERvqlLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAK 1758
Cdd:pfam15905 132 LELTRVNELLKAKFSEDGTQKKMSslSMELMKLRNK---LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1759 -----------------KAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlkggKKQLQKLEARV 1821
Cdd:pfam15905 209 stekekieeksetekllEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL----SKQIKDLNEKC 284
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 124376530 1822 RELEGELEAEQKRNAESVKGMRKSERRIKE-LTYQTEEDKK 1861
Cdd:pfam15905 285 KLLESEKEELLREYEEKEQTLNAELEELKEkLTLEEQEHQK 325
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1790-1932 |
4.48e-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: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1790 QTIKDLQHRLDEAEQIA--LKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQ 1867
Cdd:COG1579 7 RALLDLQELDSELDRLEhrLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124376530 1868 DL--VDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAK 1932
Cdd:COG1579 87 NNkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
900-1060 |
4.62e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 900 LNDAEERCDQLIKnkiqlEAKvKEMNERLEDEE-EMNAELTAKKRKLEDECSELKKDIDDLEltlAKVEKEKHATENKVK 978
Cdd:PRK12704 33 IKEAEEEAKRILE-----EAK-KEAEAIKKEALlEAKEEIHKLRNEFEKELRERRNELQKLE---KRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 979 NLTEEMAGLDEIIAKLTKEKKALQEAHQQaLDDLQVEEDK----VNSLSKSKVKlEQQVDDLEGSLEQEKKVRMDLERAK 1054
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEE-LEELIEEQLQelerISGLTAEEAK-EILLEKVEEEARHEAAVLIKEIEEE 181
|
....*.
gi 124376530 1055 RKLEGD 1060
Cdd:PRK12704 182 AKEEAD 187
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1682-1838 |
5.30e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1682 LLQAELEELRAVVEQTERSRK----------LAEQELIETSERVQLLHSQNTSLINQKKKMESdLTQLQSEVEEAVQECR 1751
Cdd:PRK11281 60 LVQQDLEQTLALLDKIDRQKEeteqlkqqlaQAPAKLRQAQAELEALKDDNDEETRETLSTLS-LRQLESRLAQTLDQLQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1752 NAE-----------------EKAKKAITDAAMMAEE----LKKEQDTSAHL---ERMKKNMEQTIKDLQHRLdeaEQIAL 1807
Cdd:PRK11281 139 NAQndlaeynsqlvslqtqpERAQAALYANSQRLQQirnlLKGGKVGGKALrpsQRVLLQAEQALLNAQNDL---QRKSL 215
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 124376530 1808 KG-------GKKQLQKLEARVRELEGELEAEQ-----KRNAES 1838
Cdd:PRK11281 216 EGntqlqdlLQKQRDYLTARIQRLEHQLQLLQeainsKRLTLS 258
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
833-1088 |
6.40e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 833 KLYFKIKPL-LKSAETEKEMATMKEEFGRIKETLEKSEARRKELEEKMV-------------SLLQE-----KNDLQLqV 893
Cdd:PLN02939 167 ALQGKINILeMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGAteglcvhslskelDVLKEenmllKDDIQF-L 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 894 QAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAkkrkLEDECseLKKDIDDLELTLAKvekekhaT 973
Cdd:PLN02939 246 KAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSP----LQYDC--WWEKVENLQDLLDR-------A 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 974 ENKVKNLTEEMAGLDEIIAKLTKEKKALQEAhqqalddlqveedKVNSLSKSKVKLEQQvddlegsleQEKKVRMDLERA 1053
Cdd:PLN02939 313 TNQVEKAALVLDQNQDLRDKVDKLEASLKEA-------------NVSKFSSYKVELLQQ---------KLKLLEERLQAS 370
|
250 260 270
....*....|....*....|....*....|....*
gi 124376530 1054 KRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFD 1088
Cdd:PLN02939 371 DHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
926-1155 |
6.47e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 926 ERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATEnkvKNLTEEM---------AGLDEIIAKLTK 996
Cdd:PRK11637 75 AQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQE---RLLAAQLdaafrqgehTGLQLILSGEES 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 997 EKKA--------LQEAHQQALDDLQveedkvnslsKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESI 1068
Cdd:PRK11637 152 QRGErilayfgyLNQARQETIAELK----------QTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1069 MDLENdklqleeKLKKkefdinqqnskieDEQVLAlqlqkKLKENQARIEELEEELEAERTARAKVEklrsdlSRELEEI 1148
Cdd:PRK11637 222 TGLES-------SLQK-------------DQQQLS-----ELRANESRLRDSIARAEREAKARAERE------AREAARV 270
|
....*..
gi 124376530 1149 SERLEEA 1155
Cdd:PRK11637 271 RDKQKQA 277
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
955-1085 |
6.48e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 955 DIDDLELTLAKVEKEKHATENkvknltEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQVEEDKVNSLSKSKVKLEQQVD 1034
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1035 DLEGSLEQEKKVRMDLERAKRKLEGDL------------------KLTQEsimdlENDKL-QLEEKLKKK 1085
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLLREEVteediaevvsrwtgipvgKLLEG-----EREKLlNLEEELHER 550
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
881-1043 |
7.00e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.12 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 881 SLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDE-EEMNAELTAKKRKLED---------ECS 950
Cdd:cd00176 37 ALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRwEELRELAEERRQRLEEaldlqqffrDAD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 951 ELKKDIDDLELTLAKVEKEKHATE-----NKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQalDDLQVEEDKVNSLSKS 1025
Cdd:cd00176 117 DLEQWLEEKEAALASEDLGKDLESveellKKHKELEEELEAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNER 194
|
170
....*....|....*...
gi 124376530 1026 KVKLEQQVDDLEGSLEQE 1043
Cdd:cd00176 195 WEELLELAEERQKKLEEA 212
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
915-1222 |
7.36e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 41.38 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 915 IQLEAKVKEMNERLEDEEEMNAELTakKRKLEDECSELKKDIDdLELTLAKvekEKHATENKVKNLTEEMA--------- 985
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPS--ELALNEMIEKLKKEID-LEYTEAV---IAMGLQERLENLREEFSkansqdqlm 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 986 --GLDEIIAKLTKE-KKALQEAhqQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVR--MDLERAKRKLEGD 1060
Cdd:PLN03229 506 hpVLMEKIEKLKDEfNKRLSRA--PNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKevMDRPEIKEKMEAL 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1061 LKLTQESIMDLENDklqLEEKLKKKefdINQQNSKIEDE-----QVLALQLQKKLKENQARIEELEEELEaertaRAKVE 1135
Cdd:PLN03229 584 KAEVASSGASSGDE---LDDDLKEK---VEKMKKEIELElagvlKSMGLEVIGVTKKNKDTAEQTPPPNL-----QEKIE 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1136 KLRSDLSRELEEISE-----------RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATlqheaTAAALRKKHADSVAE 1204
Cdd:PLN03229 653 SLNEEINKKIERVIRssdlkskiellKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEAL-----NSSELKEKFEELEAE 727
|
330
....*....|....*...
gi 124376530 1205 LGEQIDNLQRVKQKLEKE 1222
Cdd:PLN03229 728 LAAARETAAESNGSLKND 745
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
847-1100 |
7.72e-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: 41.28 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 847 TEKEMATMKEEFGRIKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDN--LNDAEERCDQLIKNKIQLEAKVKEm 924
Cdd:pfam09731 159 VKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPplLDAAPETPPKLPEHLDNVEEKVEK- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 925 NERLEDEEEMNAELTAKKRklEDECSELKKDIDDLELTLAKVEKEKHATENKVknLTEEMAGLDEIIAKLTKEKKALQEA 1004
Cdd:pfam09731 238 AQSLAKLVDQYKELVASER--IVFQQELVSIFPDIIPVLKEDNLLSNDDLNSL--IAHAHREIDQLSKKLAELKKREEKH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1005 HQQALDDLQVEEDKVNSLSKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESImdleNDKLQLEEKLKK 1084
Cdd:pfam09731 314 IERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAH----EEHLKDVLVEQE 389
|
250
....*....|....*....
gi 124376530 1085 KEFDINQQ---NSKIEDEQ 1100
Cdd:pfam09731 390 IELQREFLqdiKEKVEEER 408
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1683-1777 |
9.32e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1683 LQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQEcrnaEEKAKKAIT 1762
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQE----RKQKRKEIT 222
|
90
....*....|....*
gi 124376530 1763 DAAMMAEELkKEQDT 1777
Cdd:PRK11448 223 DQAAKRLEL-SEEET 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1550-1939 |
9.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1550 EASLEHEEGKILRAQlefNQIKAEIERKLAEKDEEMEQAKRNHQRVVDsLQTSLDAETRSRNEVLRVKKKMEGDLNEMEI 1629
Cdd:COG4717 48 LERLEKEADELFKPQ---GRKPELNLKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1630 QLShanrmAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELI 1709
Cdd:COG4717 124 LLQ-----LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1710 ET----SERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSA------ 1779
Cdd:COG4717 199 EEleelQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIltiagv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1780 -------------HLERMKKNMEQTIKDLQ--HRLDEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRK 1844
Cdd:COG4717 279 lflvlgllallflLLAREKASLGKEAEELQalPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124376530 1845 SERRIKELTYQTEedKKNLLRLQDLVDKLQLkvkaykRQAEEAEEQANTNLSKFRKVQHELDEA--EERADIAESQVNKL 1922
Cdd:COG4717 359 LEEELQLEELEQE--IAALLAEAGVEDEEEL------RAALEQAEEYQELKEELEELEEQLEELlgELEELLEALDEEEL 430
|
410
....*....|....*..
gi 124376530 1923 RAKSRDIGAKQKMHDEE 1939
Cdd:COG4717 431 EEELEELEEELEELEEE 447
|
|
| |
