|
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: 1338.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAAIGdrSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASS--KKKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 338
Cdd:cd01377 159 IAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 339 VLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd01377 239 ILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 419 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd01377 319 EQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 499 QEEYKKEGIEWEFIDFGMDLQACIDLIEKP-MGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRnvKGKQEAH 577
Cdd:cd01377 399 QEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEAH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 578 FSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDsgkgKGGKKKGSSFQTVSALHRENL 657
Cdd:cd01377 477 FILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGG----GKKKKKGGSFRTVSQLHKEQL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 658 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 737
Cdd:cd01377 553 NKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD 632
|
650 660 670
....*....|....*....|....*....|.
gi 255918225 738 iDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 1324.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 338
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 339 VLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 419 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 499 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 578
Cdd:cd14916 401 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 579 SLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENLN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 659 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 738
Cdd:cd14916 561 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 640
|
650 660 670
....*....|....*....|....*....|
gi 255918225 739 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 1292.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNAnKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKM-KGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 338
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 339 VLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14913 240 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 419 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 499 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 578
Cdd:cd14913 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 579 SLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADtGDSGKGKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14913 480 SLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATAD-ADSGKKKVAKKKGSSFQTVSALFRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 659 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 738
Cdd:cd14913 559 KLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 255918225 739 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 1251.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQ-TPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 338
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 339 VLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14917 240 VLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 419 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 499 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 578
Cdd:cd14917 400 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 579 SLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADtGDSGKGKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14917 480 SLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGAD-APIEKGKGKAKKGSSFQTVSALHRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 659 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 738
Cdd:cd14917 559 KLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 255918225 739 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 1204.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANK---GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 256
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 257 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSA 336
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 337 FDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 417 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 497 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPR-NVKGKQE 575
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRpDKKRKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 576 AHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGD--SGKGKGGKKKGSSFQTVSALH 653
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEdpKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 654 RENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 733
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 255918225 734 EGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 1164.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 338
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 339 VLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 419 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 499 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 578
Cdd:cd14923 401 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 579 SLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDS-GKGKGGKKKGSSFQTVSALHRENL 657
Cdd:cd14923 481 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSgGSKKGGKKKGSSFQTVSAVFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 658 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 737
Cdd:cd14923 561 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 255918225 738 IDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 1142.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAAIGDRsKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEK-KKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 338
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 339 VLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14918 240 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 419 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14918 320 QQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 499 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 578
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 579 SLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADtGDSGKGKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14918 480 SLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAE-ADSGAKKGAKKKGSSFQTVSALFRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 659 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 738
Cdd:cd14918 559 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 255918225 739 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14918 639 DSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| 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: 1142.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNAN-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAF 337
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 338 DVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 418 VQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 498 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAH 577
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 578 FSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENL 657
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 658 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 737
Cdd:cd14915 561 NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 255918225 738 IDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14915 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| 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: 1139.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNAN-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAF 337
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 338 DVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 418 VQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 498 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAH 577
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 578 FSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENL 657
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 658 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 737
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 255918225 738 IDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14910 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 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: 1116.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNAN-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAF 337
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 338 DVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 418 VQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 498 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAH 577
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 578 FSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFS--TYASADTGDSGKGKGGKKKGSSFQTVSALHRE 655
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSgaQTAEGASAGGGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 656 NLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEG 735
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 255918225 736 QFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 1081.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 87 IEDMAMLTFLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 167 TDRENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRSkkenpnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFG 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAG-------NVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 247 KFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTnNPYDYAFVSQ-GEVSVASID 325
Cdd:pfam00063 154 KYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQsGCYTIDGID 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 326 DSEELLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRV 405
Cdd:pfam00063 233 DSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 406 KVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 484
Cdd:pfam00063 313 KTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVNE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 485 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLYDNHlGKSNN 563
Cdd:pfam00063 393 KLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 564 FQKPRNvkgKQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLF---STYASADTGDSGKGKGGK 640
Cdd:pfam00063 471 FQKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFpdyETAESAAANESGKSTPKR 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 641 KKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 720
Cdd:pfam00063 548 TKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEF 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 255918225 721 RQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 1067.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAAIGDRSKKEnpnankGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL------GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 338
Cdd:cd14929 155 LSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 339 VLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14929 234 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 419 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14929 314 EQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 499 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 578
Cdd:cd14929 394 QEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHF 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 579 SLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGdSGKGKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14929 474 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSA-IQFGEKKRKKGASFQTVASLHKENLN 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 659 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 738
Cdd:cd14929 553 KLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFV 632
|
650 660 670
....*....|....*....|....*....|
gi 255918225 739 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 1018.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 80 NPPKFDKIEDMAMLTFLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISD 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 160 NAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASIAAigdrskkenPNANKGTLEDQIIQANPALEAFGNAKTVRN 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG---------SNTEVGSVEDQILESNPILEAFGNAKTLRN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 240 DNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNnPYDYAFVSQG-E 318
Cdd:smart00242 152 NNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGgC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 319 VSVASIDDSEELLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQA-EPDGTEDADKSAYLMGLNSADLL 397
Cdd:smart00242 231 LTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 398 KGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQL 477
Cdd:smart00242 311 KALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 478 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLYdN 556
Cdd:smart00242 391 CINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN-Q 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 557 HLGKSNNFQKPRNvkgKQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDsgkg 636
Cdd:smart00242 469 HHKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSK---- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 637 kggkkkgSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRIL 716
Cdd:smart00242 542 -------KRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLP 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255918225 717 YGDFRQRYRILNPAAIPEGQFiDSRKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRD 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: 1006.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYFASIAAIGDRSKKenpnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTGKQSSD-----GKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDV 339
Cdd:cd14934 157 AGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 340 LSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 419
Cdd:cd14934 237 LGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNME 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 420 QVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14934 317 QCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 500 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGK-QEAHF 578
Cdd:cd14934 397 EEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAHF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 579 SLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLkLMATLFSTYASADTGdsgkgKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14934 477 ELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSL-GLLALLFKEEEAPAG-----SKKQKRGSSFMTVSNFYREQLN 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 659 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFI 738
Cdd:cd14934 551 KLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FV 629
|
650 660 670
....*....|....*....|....*....|
gi 255918225 739 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 997.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAAigdRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGA---SKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 338
Cdd:cd14909 158 LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 339 VLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14909 238 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 419 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14909 318 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 499 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVK-GKQEAH 577
Cdd:cd14909 398 QEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAAH 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 578 FSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENL 657
Cdd:cd14909 478 FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 658 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQf 737
Cdd:cd14909 558 NSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE- 636
|
650 660 670
....*....|....*....|....*....|.
gi 255918225 738 iDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14909 637 -DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| 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: 840.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKR-SEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 178 GESGAGKTVNTKRVIQYFASIAAigdrSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSG----SGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDML----LVTNNPYDYAFVSQGEVSVASIDDSEELLAT 333
Cdd:cd00124 157 RLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELklelLLSYYYLNDYLNSSGCDRIDGVDDAEEFQEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 334 DSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREE--QAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEY 411
Cdd:cd00124 237 LDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGET 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 412 VTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATL--ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 489
Cdd:cd00124 317 ITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 490 FNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPR 568
Cdd:cd00124 397 FNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 569 NVKGkqeaHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSlklmatlfstyasadtgdsgkgkggkkkgssfqt 648
Cdd:cd00124 476 KAKL----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS---------------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 649 vsaLHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 728
Cdd:cd00124 518 ---QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILA 594
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 255918225 729 PAAiPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd00124 595 PGA-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| 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: 840.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 31 FDIRTECFVPDDKEEYVKAKVVSRE--GGKVTAE--TENGKTVTIKEDQVMQ--QNPPKFDKIEDMAMLTFLHEPAVLYN 104
Cdd:COG5022 6 AEVGSGCWIPDEEKGWIWAEIIKEAfnKGKVTEEgkKEDGESVSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPAVLHN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 105 LKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGK 184
Cdd:COG5022 86 LEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 185 TVNTKRVIQYFASIAAigdrskkeNPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADI 264
Cdd:COG5022 166 TENAKRIMQYLASVTS--------SSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 265 ETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNnPYDYAFVSQGEV-SVASIDDSEELLATDSAFDVLSFT 343
Cdd:COG5022 238 ETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQN-PKDYIYLSQGGCdKIDGIDDAKEFKITLDALKTIGID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 344 AEEKAGVYKLTGAIMHYGNMKFKqKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYY 423
Cdd:COG5022 317 EEEQDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 424 SIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYK 503
Cdd:COG5022 396 IRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 504 KEGIEWEFIDFgMDLQACIDLIEK--PMGIMSILEEECMFPKASDMTFKAKLYDN-HLGKSNNFQKPRNVKGKqeahFSL 580
Cdd:COG5022 476 KEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 581 VHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTgdsgkgkggkkkGSSFQTVSALHRENLNKL 660
Cdd:COG5022 551 KHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIES------------KGRFPTLGSRFKESLNSL 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 661 MTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI-- 738
Cdd:COG5022 619 MSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwk 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 739 -DSRKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQARGQLMRIEFKKIVERRDALLVIQ 817
Cdd:COG5022 699 eDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQ 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 818 WNIRAFMGVKNWPWMKLYFKIKPLLKSAETEKEM---------------------ANMKEEFGRVKDALeKSEARRKELE 876
Cdd:COG5022 779 HGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYrsylaciiklqktikrekklrETEEVEFSLKAEVL-IQKFGRSLKA 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 877 EKMVSLLQEKNdLQLQVQAEQDN-------LNDAEERCDQL-----------------------IKNKIQLE--AKVKEM 924
Cdd:COG5022 858 KKRFSLLKKET-IYLQSAQRVELaerqlqeLKIDVKSISSLklvnleleseiielkkslssdliENLEFKTEliARLKKL 936
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 925 TE--RLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLakveKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQ 1002
Cdd:COG5022 937 LNniDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLL----KKSTILVREGNKANSELKNFKKELAELSKQYGALQ 1012
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1003 EAHQQ------ALDDLQAEEDKVNTLTKSKvKLEQQVDDLEGSLEQEKK------VRMDLERAKRKLEGDLKLTQESIMD 1070
Cdd:COG5022 1013 ESTKQlkelpvEVAELQSASKIISSESTEL-SILKPLQKLKGLLLLENNqlqaryKALKLRRENSLLDDKQLYQLESTEN 1091
|
1130
....*....|....*.
gi 255918225 1071 LENDKLQLEEKLKKKE 1086
Cdd:COG5022 1092 LLKTINVKDLEVTNRN 1107
|
|
| 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: 794.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYFASIAAIGDRS------KKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF 253
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASKPKGsgavphPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 254 GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGEVSVASIDDSEELLAT 333
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 334 DSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 412
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNTV-AQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 413 TKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 491
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 492 HHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLgksnnfQKPRNVK 571
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 572 G--KQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGG---KKKGSSF 646
Cdd:cd14911 474 TdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQfgaRTRKGMF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 647 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 255918225 727 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 757.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYFASIAAigdRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVAS---SHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPEL-LDMLLVTNNpyDYAFVSQGEVSVASIDDSEELLATDSAFD 338
Cdd:cd14920 159 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 339 VLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14920 237 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENTV-AQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 418 VQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQpRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14920 316 KEQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 496 VLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLyDNHLGKSNNFQKPRNVKG 572
Cdd:cd14920 395 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 573 kqEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-----ASADTG--DSGKGKGGKKKGSS 645
Cdd:cd14920 474 --KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgLDQVTGmtETAFGSAYKTKKGM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 646 FQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 725
Cdd:cd14920 552 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 255918225 726 ILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 710.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYFASIAAiGDRSKKENPNA--NKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVAS-SFKTKKDQSSIalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPyDYAFVSQGEVSVASIDDSEELLATDSAF 337
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYS-KYRFLSNGNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 338 DVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDTA-AQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 417 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 496 VLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYdNHLGKSNNFQKPRnvKG 572
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPK--KL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 573 KQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDsGKGKGGKKKGSS 645
Cdd:cd14932 476 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdrivgldKVAGMGE-SLHGAFKTRKGM 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 646 FQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 725
Cdd:cd14932 555 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 634
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 255918225 726 ILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 695.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 178 GESGAGKTVNTKRVIQYFASIAAigdrskkenPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGG---------SSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAF 337
Cdd:cd01380 152 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 338 DVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd01380 232 TLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 418 VQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQP--RQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd01380 312 LQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 496 VLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNN-FQKPRNVKGKq 574
Cdd:cd01380 392 KLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFSNTA- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 575 eahFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMatlfstyasadtgdsgkgkggkkkgssfqTVSALHR 654
Cdd:cd01380 470 ---FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRKK-----------------------------TVGSQFR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 655 ENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAipE 734
Cdd:cd01380 518 DSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK--E 595
|
650 660 670
....*....|....*....|....*....|....
gi 255918225 735 GQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 681.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYFASIAAigdRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVAS---SHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELL-DMLLVTNNpyDYAFVSQGEVSVASIDDSEELLATDSAFD 338
Cdd:cd14921 159 VGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 339 VLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNTA-AQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 418 VQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14921 316 KEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 497 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGK 573
Cdd:cd14921 396 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 574 QEahFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDSGKGKGGKKKGSSF 646
Cdd:cd14921 475 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldQMAKMTESSLPSASKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 647 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 255918225 727 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 673.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpnanKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVAS-SHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtnNPYD-YAFVSQGEVSVASIDDSEELLATDSAFD 338
Cdd:cd14919 156 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 339 VLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14919 234 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNTA-AQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 418 VQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 497 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGK 573
Cdd:cd14919 393 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 574 qeAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDSGKGKGGKKKGSSF 646
Cdd:cd14919 472 --ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldQVAGMSETALPGAFKTRKGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 647 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14919 550 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 255918225 727 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 671.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYFASIAAiGDRSKKENPN--ANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVAS-SHKTKKDQNSlaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPyDYAFVSQGEVSVASIDDSEELLATDSAF 337
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYN-NYRFLSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 338 DVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASmPDNTA-AQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 417 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd15896 319 TQEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 496 VLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRnvKG 572
Cdd:cd15896 399 ILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPK--KL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 573 KQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYAS-----ADTGDSGKGKGGKKKGSSFQ 647
Cdd:cd15896 476 KDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRivgldKVSGMSEMPGAFKTRKGMFR 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 648 TVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 727
Cdd:cd15896 556 TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 635
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 255918225 728 NPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 657.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnPNAnKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVAS-SPKGRKE-PGV-PGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYdYAFVSQGEVSVASiDDSEELLATDSAFDV 339
Cdd:cd14930 159 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 340 LSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14930 237 LGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNTA-AQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 419 QQVYYSIGALAKSVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14930 316 EQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 497 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVkgK 573
Cdd:cd14930 395 LEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHL--R 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 574 QEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYAS-------ADTGDsgKGKGGKKKGSSF 646
Cdd:cd14930 472 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqvSSLGD--GPPGGRPRRGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 647 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14930 550 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 255918225 727 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 639.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYFASIAAigdrskkeNPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSG--------GSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDV 339
Cdd:cd01378 154 VGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 340 LSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEY---VTKGQ 416
Cdd:cd01378 234 IGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISDTSV-LDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 417 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQ-YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHhmF 495
Cdd:cd01378 313 NVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--L 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 496 VL--EQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFP-KASDMTFKAKLyDNHLGKSNNFQKPRNVK 571
Cdd:cd01378 391 TLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 572 GKQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFStyASADTGDSGKGKggkkkgssfqTVSA 651
Cdd:cd01378 469 ELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFP--EGVDLDSKKRPP----------TAGT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 652 LHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAA 731
Cdd:cd01378 537 KFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKT 616
|
650 660 670
....*....|....*....|....*....|....*..
gi 255918225 732 IPEGQFIDsRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 634.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYFASIAAigdrskkenpnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd01381 82 SGAGKTESTKLILQYLAAISG------------QHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTnNPYDYAFVSQGE-VSVASIDDSEELLATDSAFD 338
Cdd:cd01381 150 EGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-DASDYYYLTQGNcLTCEGRDDAAEFADIRSAMK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 339 VLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQRE--EQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd01381 229 VLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 417 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYF---IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 493
Cdd:cd01381 309 SAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRH 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 494 MFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNvkg 572
Cdd:cd01381 389 IFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKPKS--- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 573 KQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY--ASADTgdsgkgkggkkkGSSFQTVS 650
Cdd:cd01381 464 DLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDisMGSET------------RKKSPTLS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 651 ALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPa 730
Cdd:cd01381 532 SQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP- 610
|
650 660 670
....*....|....*....|....*....|....*...
gi 255918225 731 AIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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: 628.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRgkKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAAIGDRskkenpnankgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd01383 79 ESGAGKTETAKIAMQYLAALGGGSSG------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTnNPYDYAFVSQGE-VSVASIDDSEELLATDSAF 337
Cdd:cd01383 147 ICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLK-SASEYKYLNQSNcLTIDGVDDAKKFHELKEAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 338 DVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd01383 226 DTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 418 VQQVYYSIGALAKSVYEKMFNWMVTRINATLET-KQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd01383 306 LQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 497 LEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLyDNHLGKSNNFqkprnvKGKQE 575
Cdd:cd01383 386 LEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGERG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 576 AHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLmATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRE 655
Cdd:cd01383 458 GAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQL-PQLFASKMLDASRKALPLTKASGSDSQKQSVATKFKG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 656 NLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEG 735
Cdd:cd01383 537 QLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSAS 616
|
650 660 670
....*....|....*....|....*....|...
gi 255918225 736 QFIDSRKGAekLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01383 617 QDPLSTSVA--ILQQFNILPEMYQVGYTKLFFR 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: 612.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYfasIAAIGDRSKKenpnankgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14883 82 SGAGKTETTKLILQY---LCAVTNNHSW---------VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKK--PELLDMLLVtNNPYDYAFVSQ-GEVSVASIDDSEELLATDSA 336
Cdd:cd14883 150 KGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKL-GEPEDYHYLNQsGCIRIDNINDKKDFDHLRLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 337 FDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKG 415
Cdd:cd14883 229 MNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 416 QSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14883 309 LKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 496 VLEQEEYKKEGIEWEFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGKQ 574
Cdd:cd14883 389 KLEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPDRRRWKT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 575 EahFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFS----TYASADTGDSGKGKGGKKKGSSFQTVS 650
Cdd:cd14883 467 E--FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTypdlLALTGLSISLGGDTTSRGTSKGKPTVG 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 651 ALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 730
Cdd:cd14883 545 DTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPR 624
|
650 660 670
....*....|....*....|....*....|....*....
gi 255918225 731 AIPEGQfiDSRKGAEK-LLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14883 625 ARSADH--KETCGAVRaLMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-768 |
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: 576.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 178 GESGAGKTVNTKRVIQYfasIAAIGDRSkkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd01384 81 GESGAGKTETTKMLMQY---LAYMGGRA-----VTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGE-VSVASIDDSEELLATDSA 336
Cdd:cd01384 153 RISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKL-KDPKQFHYLNQSKcFELDGVDDAEEYRATRRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 337 FDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEP--DGTEDADK-SAYLMGLNSADLLKGLCHPRVKVGNEYVT 413
Cdd:cd01384 232 MDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPkdEKSEFHLKaAAELLMCDEKALEDALCKRVIVTPDGIIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 414 KGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 493
Cdd:cd01384 312 KPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 494 MFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLYDNhLGKSNNFQKPrnvKG 572
Cdd:cd01384 392 VFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKP---KL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 573 KQEAhFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGdsgkgkggkkKGSSFQTVSAL 652
Cdd:cd01384 467 SRTD-FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGTS----------SSSKFSSIGSR 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 653 HRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAI 732
Cdd:cd01384 536 FKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVL 615
|
650 660 670
....*....|....*....|....*....|....*.
gi 255918225 733 peGQFIDSRKGAEKLLGSLDIdhNQYKFGHTKVFFK 768
Cdd:cd01384 616 --KGSDDEKAACKKILEKAGL--KGYQIGKTKVFLR 647
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-768 |
8.93e-172 |
|
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: 537.82 E-value: 8.93e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAAigdrskkenpnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAG------------STNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPElldMLLVTNNPYDYAFVSQGE-VSVASIDDSEELLATDSAF 337
Cdd:cd14872 149 ICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPA---SRGGWGSSAAYGYLSLSGcIEVEGVDDVADFEEVVLAM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 338 DVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKS---AYLMGLNSADLLKGLCHPRVKVgneyvtK 414
Cdd:cd14872 226 EQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLkevATLLGVDAATLEEALTSRLMEI------K 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 415 GQ-------SVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 486
Cdd:cd14872 300 GCdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 487 QQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSnnFQ 565
Cdd:cd14872 380 QQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS--TF 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 566 KPRNVKGKqEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYasadTGDSGKGKGgkkkgss 645
Cdd:cd14872 457 VYAEVRTS-RTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPS----EGDQKTSKV------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 646 fqTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 725
Cdd:cd14872 525 --TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYR 602
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 255918225 726 ILnPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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 |
4.87e-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: 533.59 E-value: 4.87e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 178 GESGAGKTVNTKRVIQYFASIAAigdrskkenpNANKGTLEdQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG----------GLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLlvtnnPYDYAFVSQGEVSVASID---DSEELLATD 334
Cdd:cd14903 150 TLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFL-----DSANECAYTGANKTIKIEgmsDRKHFARTK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 335 SAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE--PDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 412
Cdd:cd14903 225 EALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 413 TKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 492
Cdd:cd14903 305 TVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 493 HMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKg 572
Cdd:cd14903 385 DVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 573 kqeAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLF----STYASADTGDSGKGKGGKKKGSSFQT 648
Cdd:cd14903 463 ---TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFkekvESPAAASTSLARGARRRRGGALTTTT 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 649 VSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 728
Cdd:cd14903 540 VGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFL 619
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 255918225 729 PAAipEGQFIDSRKGAEKLLGSLDIDH-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 ... |
102-768 |
2.00e-168 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 529.13 E-value: 2.00e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 102 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 181 GAGKTVNTKRVIQYFAsiaaigdrskkENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 260
Cdd:cd01382 84 GAGKTESTKYILRYLT-----------ESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 261 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLvtnnpydyafvsqgevSVASIDDSEELLATDSAFDVL 340
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKKI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 341 SFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKS----AYLMGLNSADLLKGLCHpRVKVGNEYVTKGQ 416
Cdd:cd01382 217 GLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSEQSleyaAELLGLDQDELRVSLTT-RVMQTTRGGAKGT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 417 S------VQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQpRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 490
Cdd:cd01382 296 VikvplkVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 491 NHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLYDNHLgksNNF--QKP 567
Cdd:cd01382 375 NERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK---NHFrlSIP 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 568 RnvKGKQEAH--------FSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGdsgkgKGG 639
Cdd:cd01382 451 R--KSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKD-----SKQ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 640 KKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGD 719
Cdd:cd01382 524 KAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHD 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 255918225 720 FRQRYRILNPAAIPEgqfIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01382 604 LYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
100-768 |
1.29e-166 |
|
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: 524.72 E-value: 1.29e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYML----TDRENQSI 174
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIqsgvLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 175 LITGESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANK-------GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGK 247
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASeaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 248 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNnPYDYAFVSQGEVSVASIDDS 327
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 328 EELLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGT-EDADKSAYLMGLNSADLLKGLCHPRVK 406
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 407 VGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 486
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 487 QQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILE--EECMFPKAS--DMTFKAKLYDNHLGKS 561
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgKVNGKPGIFItlDDCWRFKGEeaNKKFVSQLHASFGRKS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 562 NNFQKPRNVKGKQ---------EAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATlfstyasadtgd 632
Cdd:cd14890 480 GSGGTRRGSSQHPhfvhpkfdaDKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIREV------------ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 633 sgkgkggkkkgssfqTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFP 712
Cdd:cd14890 548 ---------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFA 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 255918225 713 NRILYGDFRQRYRILNPAAIPEGQFIdsrkgaEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14890 613 LREEHDSFFYDFQVLLPTAENIEQLV------AVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
99-768 |
6.37e-166 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 521.45 E-value: 6.37e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAaigdrskkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVLG-----------KANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQIL----SNKKpeLLDMLLVTNNPYDYAFVSQGEVSVASIDDS--EELLA 332
Cdd:cd01379 150 VTGARISEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKPPRYLQNDGLTVQDIVNNSGnrEKFEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 333 TDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQ----AEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVG 408
Cdd:cd01379 228 IEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 409 NEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATL---ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEK 485
Cdd:cd01379 308 GETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpdRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 486 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACID-LIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHlgKSNNF 564
Cdd:cd01379 388 IQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYY 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 565 QKPRNVkgkqEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMAtlfstyasadtgdsgkgkggkkkgs 644
Cdd:cd01379 465 WRPKSN----ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 645 sfQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 724
Cdd:cd01379 516 --QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRY 593
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 255918225 725 RIL--NPAAIPEGqfidSRKGAEKLLGSLDIDHnqYKFGHTKVFFK 768
Cdd:cd01379 594 YFLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1925 |
1.57e-165 |
|
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: 535.91 E-value: 1.57e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 848 EKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMTER 927
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 928 LEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQ 1007
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1008 ALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEF 1087
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1088 DISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNK 1167
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1168 KREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANL 1247
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1248 EKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKA 1327
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1328 KNALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDAEEAVE 1407
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1408 AVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLK 1487
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1488 NAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEF 1567
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1568 NQIKAEIERKLAEKDEEMEQAKRNHLRMVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKN 1647
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1648 SQAHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLIN 1727
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1728 QKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAL 1807
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1808 KGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEA 1887
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 255918225 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 |
1.75e-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: 518.86 E-value: 1.75e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRgKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 178 GESGAGKTVNTKRVIQYFASIaaiGDRSKKenpnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF---- 253
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACA---GSEDIK-----KRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklk 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 254 -----GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILS-----------------------NKKPELLDMLL-V 304
Cdd:cd14888 152 skrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSfE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 305 TNNPYDYAFVSqGEVSVASIDDSEELLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQA---EPDGTED 381
Cdd:cd14888 232 PHLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 382 ADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGV 460
Cdd:cd14888 311 LEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 461 LDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLI-EKPMGIMSILEEEC 539
Cdd:cd14888 391 LDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEEC 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 540 MFPKASDMTFKAKLYDNHLGkSNNFQKprnVKGKQEAhFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMA 619
Cdd:cd14888 470 FVPGGKDQGLCNKLCQKHKG-HKRFDV---VKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFIS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 620 TLFSTYASADTGdsgkgkgGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNG 699
Cdd:cd14888 545 NLFSAYLRRGTD-------GNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGG 617
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 700 VLEGIRICRKGFPNRILYGDFRQRYRILNPaaipegqfidsrkgaekllGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14888 618 VLQAVQVSRAGYPVRLSHAEFYNDYRILLN-------------------GEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
100-768 |
1.74e-163 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 515.84 E-value: 1.74e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYFASIaaigdrskkeNPNANKGTLEdQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGKL 259
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAV----------NQRRNNLVTE-QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKkPELLDMLLVTNNPYDYAFVSQG-EVSVASIDDSEELLATDSAFD 338
Cdd:cd01387 150 VGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGL-PAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 339 VLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQRE---EQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKG 415
Cdd:cd01387 229 VLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 416 QSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd01387 309 LTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 496 VLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRnvKGKQ 574
Cdd:cd01387 389 KLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR--MPLP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 575 EahFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYAS--ADTGDSGKGKGGKKKGSSFQTVSAL 652
Cdd:cd01387 465 E--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAqtDKAPPRLGKGRFVTMKPRTPTVAAR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 653 HRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAI 732
Cdd:cd01387 543 FQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKL 622
|
650 660 670
....*....|....*....|....*....|....*...
gi 255918225 733 PEGQFIDSRkgaEKLLGSLD--IDHNQYKFGHTKVFFK 768
Cdd:cd01387 623 PRPAPGDMC---VSLLSRLCtvTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-766 |
1.92e-161 |
|
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: 510.10 E-value: 1.92e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY------RGKKRSEAPPHIFSISDNAYQYMLTDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 171 --NQSILITGESGAGKTVNTKRVIQYFASIAAigdRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS---ATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 249 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNP-YDYAFVSQGEVSVASIDDS 327
Cdd:cd14901 158 IRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEeYKYLNSSQCYDRRDGVDDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 328 EELLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTE-DADKSAYLMGLNSADLLKGLCHPRVK 406
Cdd:cd14901 238 VQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLaNVRAACDLLGLDMDVLEKTLCTREIR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 407 VGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQP--RQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 484
Cdd:cd14901 318 AGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFANE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 485 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLYDNhLGKSNN 563
Cdd:cd14901 398 KLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHAS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 564 FQKPRNVKGKQEahFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATlfstyasadtgdsgkgkggkkkg 643
Cdd:cd14901 476 FSVSKLQQGKRQ--FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 644 ssfqTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 723
Cdd:cd14901 531 ----TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHT 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 255918225 724 YRILNPAAIPEGQFIDSRKGAEKLLGSLDI----DHNQYKFGHTKVF 766
Cdd:cd14901 607 YSCLAPDGASDTWKVNELAERLMSQLQHSElnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
105-768 |
1.36e-157 |
|
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: 499.67 E-value: 1.36e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 105 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRG--KKRSEAPPHIFSISDNAYQYMLTDR----ENQSILIT 177
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTPQSIVVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 178 GESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANKGT-LEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 256
Cdd:cd14892 87 GESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHEsIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 257 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpELLDMLLVTNNPYDYAFVSQGE-VSVASIDDSEELLATDS 335
Cdd:cd14892 167 GRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGNcVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 336 AFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQ--KQREEQAEPDGTEDADKSAYLMGLNSADLLKGLC-----HPRVKVG 408
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVtqttsTARGSVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 409 NEYVTKGQSVQqvyySIGALAKSVYEKMFNWMVTRINAtlETKQ------------PRQYFIGVLDIAGFEIFDFNSFEQ 476
Cdd:cd14892 326 EIKLTAREAKN----ALDALCKYLYGELFDWLISRINA--CHKQqtsgvtggaaspTFSPFIGILDIFGFEIMPTNSFEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 477 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEK-PMGIMSILEEECMFP-KASDMTFKAKLY 554
Cdd:cd14892 400 LCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTIYH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 555 DNHLGKSNNFQKPRNvkgkQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSlklmatlfstyasadtgdsg 634
Cdd:cd14892 479 QTHLDKHPHYAKPRF----ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS-------------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 635 kgkggkkkgsSFqtvsalhRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNR 714
Cdd:cd14892 535 ----------KF-------RTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIR 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 715 ILYGDFRQRYRIL-----NPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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 |
7.82e-157 |
|
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: 498.82 E-value: 7.82e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 102 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESG 181
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 182 AGKTVNTKRVIQYFASIAAIGDRSKKENpnankgtledQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 261
Cdd:cd01385 84 SGKTESTNFLLHHLTALSQKGYGSGVEQ----------TILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 262 ADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTnNPYDYAFVSQGE-VSVASIDDSEELLATDSAFDVL 340
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLK-QPEDYHYLNQSDcYTLEGEDEKYEFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 341 SFTAEEKAGVYKLTGAIMHYGNMKFKQK--QREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 419 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQ----PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 494
Cdd:cd01385 313 PEAIATRDAMAKCLYSALFDWIVLRINHALLNKKdleeAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 495 FVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKlYDNHLGKSNNFQKPRnvkgK 573
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ----V 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 574 QEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLM------------------ATLFSTYASADTGDSGK 635
Cdd:cd01385 467 MEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVreligidpvavfrwavlrAFFRAMAAFREAGRRRA 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 636 GKGGKKKGSSFQ----------------TVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNG 699
Cdd:cd01385 547 QRTAGHSLTLHDrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTG 626
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 700 VLEGIRICRKGFPNRILYGDFRQRYRILnpaaIPEGQfIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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 |
2.09e-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: 490.85 E-value: 2.09e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQSLELSLKEKTSC---VEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTnNPYDYAFVSQ-GEVSVASIDDSEELLATDSAF 337
Cdd:cd14873 159 IQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLNQsGCVEDKTISDQESFREVITAM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 338 DVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDadkSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14873 238 EVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALGR---SAELLGLDPTQLTDALTQRSMFLRGEEILTPLN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 418 VQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQyFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14873 315 VQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 498 EQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHlgkSNN--FQKPRnvkgKQE 575
Cdd:cd14873 394 EQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH---ANNhfYVKPR----VAV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 576 AHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKgssfQTVSALHRE 655
Cdd:cd14873 466 NNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRR----PTVSSQFKD 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 656 NLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP-AAIPE 734
Cdd:cd14873 542 SLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRnLALPE 621
|
650 660 670
....*....|....*....|....*....|....
gi 255918225 735 gqfiDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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 |
3.04e-148 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 473.41 E-value: 3.04e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKK-RSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYFASIaaigdrSKKENPNankgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKL------SPSDDSD-----LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDV 339
Cdd:cd14897 152 LGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELEYYRQMFHD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 340 L-------SFTAEEKAGVYKLTGAIMHYGNMKFkqkqrEEQAEPDGTEDADK-----SAYLMGLNSADLLKGLCHPRVKV 407
Cdd:cd14897 231 LtnimkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 408 GNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYF-----IGVLDIAGFEIFDFNSFEQLCINFT 482
Cdd:cd14897 306 RGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 483 NEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLyDNHLGKS 561
Cdd:cd14897 386 NERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCGES 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 562 NNFQKPrnvKGKQEAhFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYasadtgdsgkgkggkk 641
Cdd:cd14897 464 PRYVAS---PGNRVA-FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY---------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 642 kgssfqtvsalHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 721
Cdd:cd14897 524 -----------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFV 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 255918225 722 QRYRILNPAAIPegqfidSRKGAE-KLLGSLDIDHNQ-YKFGHTKVFFK 768
Cdd:cd14897 593 KRYKEICDFSNK------VRSDDLgKCQKILKTAGIKgYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
101-733 |
3.23e-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: 459.00 E-value: 3.23e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAY-----------RGKKRSEAPPHIFSISDNAYQYM--- 165
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 166 -LTDRENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRSKKENPnANKGTLEDQIIQANPALEAFGNAKTVRNDNSSR 244
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMG-KSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 245 FGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILsnkkpelldmllvtnnpydyafVSQGEVSVASi 324
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMA----------------------IGASEAARKR- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 325 DDSEELLAtdsAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDA-------DKSAYLMGLNSADLL 397
Cdd:cd14900 219 DMYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 398 KGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATL-----ETKQPRQYFIGVLDIAGFEIFDFN 472
Cdd:cd14900 296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPKN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 473 SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKA 551
Cdd:cd14900 376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLAS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 552 KLYdNHLGKSNNFQKPRNVKGKqeAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKsslklmatlfstyasadtg 631
Cdd:cd14900 455 KLY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVY------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 632 dsgkgkggkkkgssfqtvSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGF 711
Cdd:cd14900 513 ------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGF 574
|
650 660
....*....|....*....|..
gi 255918225 712 PNRILYGDFRQRYRILNPAAIP 733
Cdd:cd14900 575 PIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-768 |
5.07e-143 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 459.41 E-value: 5.07e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 178 GESGAGKTVNTKRVIQYFASIAaiGDRSKKenpnankgTLeDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA--GGRKDK--------TI-AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSN-KKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSA 336
Cdd:cd14904 150 KLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 337 FDVLSFTAEEKAGVYKLTGAIMHYGNMKFkQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd14904 230 LSLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 417 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQY-FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14904 309 APVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 496 VLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNH--LGKSNNFQKPRnVKGK 573
Cdd:cd14904 389 KTVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPK-VKRT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 574 QeahFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFStyaSADTGDSGKGKGGKKKGSSFQTVSALH 653
Cdd:cd14904 467 Q---FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFG---SSEAPSETKEGKSGKGTKAPKSLGSQF 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 654 RENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 733
Cdd:cd14904 541 KTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMH 620
|
650 660 670
....*....|....*....|....*....|....*.
gi 255918225 734 EGqfiDSRKGAEKLLGSLDIDHN-QYKFGHTKVFFK 768
Cdd:cd14904 621 SK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
101-768 |
7.33e-139 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 448.71 E-value: 7.33e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGK--------KRSEAPPHIFSISDNAYQYMLTDREN 171
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 172 QSILITGESGAGKTVNTKRVIQYFASIAA--------IGDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSS 243
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevLTLTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 244 RFGKFIRIHFG-ATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNP--YDYAFVSQGE-V 319
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLsgDRYDYLKKSNcY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 320 SVASIDDSEELLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQ--REEQAEPDGTEDADKSAYLMGLNSADLL 397
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 398 KGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATL--------ETKQPRQYFIGVLDIAGFEIF 469
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 470 DFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF--IDFgMDLQACIDLIEK-PMGIMSILEEECMFPKASD 546
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 547 MTFKAKLYDNHlgksNNFQKPRNVKGKQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTya 626
Cdd:cd14907 482 EKLLNKIKKQH----KNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSG-- 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 627 sADTGDSGKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRI 706
Cdd:cd14907 556 -EDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRV 634
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255918225 707 CRKGFPNRILYGDFRQRYRILNpaaipegqfidsrkgaekllgsldidhNQYKFGHTKVFFK 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 ... |
101-768 |
9.78e-137 |
|
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: 442.42 E-value: 9.78e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYML----TDRENQSILI 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 177 TGESGAGKTVNTKRVIQYFASIAaigdrskkenpNANKgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgAT 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC-----------RGNS-QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 257 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQI---LSNKKPELLDMLLVTNNPY-DYAFVSQGEVSVASIDDSEELla 332
Cdd:cd14889 150 GHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLLDPGKYRYlNNGAGCKREVQYWKKKYDEVC-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 333 tdSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREE-QAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEY 411
Cdd:cd14889 228 --NAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 412 VTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQY---FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQ 488
Cdd:cd14889 306 IQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVelrEIGILDIFGFENFAVNRFEQACINLANEQLQY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 489 FFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDL-IEKPMGIMSILEEECMFPKASDMTFKAKLyDNHLGKSNNFQKP 567
Cdd:cd14889 386 FFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGKS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 568 RNVKGKqeahFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSF- 646
Cdd:cd14889 464 RSKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSDNFn 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 647 ----QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ 722
Cdd:cd14889 540 strkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAE 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 255918225 723 RYRIL-NPAAIPegqfiDSRKGAEKLLGSLDIdhNQYKFGHTKVFFK 768
Cdd:cd14889 620 RYKILlCEPALP-----GTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-768 |
5.74e-135 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 436.78 E-value: 5.74e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAA--WMIYTYSGLFCVTVNPYKWLPvyNAEVvAAYRGKKRSEAPPHIFSISDNAYQYMLTDRE---NQS 173
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 174 ILITGESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANKG-------TLEDQIIQANPALEAFGNAKTVRNDNSSRFG 246
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKkrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 247 KFIRIHFGATG-KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTnNPYDYAFVSQ-GEVSVASI 324
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLL-SPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 325 DDSEELLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREE----QAEPDGTEDADKSAYLMGLNSADLLKGL 400
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 401 CHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFD-FNSFEQLCI 479
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 480 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLYDNHl 558
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 559 GKSNNFQKPRNvKGKQEAhFSLVHYAGTVDYNIMGWLEKNKDPLNEtvvglyQKSSLKLMATLFStyasadtgdsgkgkg 638
Cdd:cd14891 475 KRHPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPE------DFEDLLASSAKFS--------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 639 gkkkgssfqtvsalhrENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 718
Cdd:cd14891 532 ----------------DQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYA 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 255918225 719 DFRQRYRILNPAAI------PEGQFIdsrkgaEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14891 596 ELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-729 |
1.48e-134 |
|
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: 437.03 E-value: 1.48e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYR--GKKRS---EAP----PHIFSISDNAYQYMLTD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 169 RENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 249 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQIL------SNKKPELLDMLLVTNN-PYDYAFVSQGEV-S 320
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDGITGGLQlPNEFHYTGQGGApD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 321 VASIDDSEELLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAY---LMGLNSADLL 397
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 398 KGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATL--ETKQPRQYFIGVLDIAGFEIFDFNSFE 475
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 476 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFP-KASDMTFKAKL 553
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 554 YDNHLGKSNN-------FQKPRNVKGKqeAHFSLVHYAGTVDYNI-MGWLEKNKDPLNETVVGLYQKSslklmaTLFsty 625
Cdd:cd14908 480 YETYLPEKNQthsentrFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESG------QQF--- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 626 asadtgdsgkgkggkkkgssfqtvsalhRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIR 705
Cdd:cd14908 549 ----------------------------KAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVR 600
|
650 660
....*....|....*....|....
gi 255918225 706 ICRKGFPNRILYGDFRQRYRILNP 729
Cdd:cd14908 601 VARSGYPVRLPHKDFFKRYRMLLP 624
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-729 |
3.19e-133 |
|
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: 434.32 E-value: 3.19e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYR--------GKKRSEAPPHIFSISDNAYQYML-TD 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 169 RENQSILITGESGAGKTVNTKRVIQYFASIAAigDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGR--DQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 249 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDmLLVTNNPYDYAFVSQGEVSVA-----S 323
Cdd:cd14902 159 IKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD-LLGLQKGGKYELLNSYGPSFArkravA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 324 IDDSEELLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDA---DKSAYLMGLNSADLLKGL 400
Cdd:cd14902 238 DKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 401 CHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRIN-------ATLETKQPRQYF--IGVLDIAGFEIFDF 471
Cdd:cd14902 318 SSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSdeinyfdSAVSISDEDEELatIGILDIFGFESLNR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 472 NSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLqACIDLIE-KPMGIMSILEEECMFPKASDMTFK 550
Cdd:cd14902 398 NGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNA-ACLALFDdKSNGLFSLLDQECLMPKGSNQALS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 551 AKLYDNHLGksnnfqkprnvkgkqEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADT 630
Cdd:cd14902 477 TKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSP 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 631 G-DSGKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRK 709
Cdd:cd14902 542 GaDNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARH 621
|
650 660
....*....|....*....|
gi 255918225 710 GFPNRILYGDFRQRYRILNP 729
Cdd:cd14902 622 GYSVRLAHASFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
62-821 |
6.90e-125 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 414.43 E-value: 6.90e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 62 ETENGKTVTIKEDQVMQQNPP-KFDKIEDMAMLTFLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVA 140
Cdd:PTZ00014 72 DPPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 141 AYR-GKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASiaaigdrSKKENpnaNKGTLED 219
Cdd:PTZ00014 152 RYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS-------SKSGN---MDLKIQN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 220 QIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELL 299
Cdd:PTZ00014 222 AIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 300 DMLLVTNNPyDYAFVSQGEVSVASIDDSEELLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKqrEEQAEPDGT 379
Cdd:PTZ00014 302 EKYKLKSLE-EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGK--EEGGLTDAA 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 380 EDADKS-------AYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQ 452
Cdd:PTZ00014 379 AISDESlevfneaCELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPG 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 453 PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIM 532
Cdd:PTZ00014 459 GFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVL 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 533 SILEEECMFPKASDMTFKAKLYDNHlgKSNNFQKPrnVKGKQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQK 612
Cdd:PTZ00014 539 SILEDQCLAPGGTDEKFVSSCNTNL--KNNPKYKP--AKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKA 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 613 SSLKLMATLFStyasadtGDSGKGKGGKKKgssfQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVM 692
Cdd:PTZ00014 615 SPNPLVRDLFE-------GVEVEKGKLAKG----QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVL 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 693 HQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNpAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLL 772
Cdd:PTZ00014 684 IQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAA 762
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 255918225 773 GLLEEMRDERLSR---IITRIQAQARGQLMRIEFKKIVErrdALLVIQWNIR 821
Cdd:PTZ00014 763 KELTQIQREKLAAwepLVSVLEALILKIKKKRKVRKNIK---SLVRIQAHLR 811
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-768 |
9.43e-125 |
|
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: 408.01 E-value: 9.43e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIaaigdrsKKENPNANKGTLEDQIiqanPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGK 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL-------YQDQTEDRLRQPEDVL----PILESFGHAKTILNANASRFGQVLRLHL-QHGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGEV-SVASIDDSEELLATDSAF 337
Cdd:cd14896 149 IVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 338 DVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDAD--KSAYLMGLnSADLLKGLCHPRVKVGN-EYVTK 414
Cdd:cd14896 228 QGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQV-PPERLEGAVTHRVTETPyGRVSR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 415 GQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYF--IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 492
Cdd:cd14896 307 PLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 493 HMFVLEQEEYKKEGIEWEFIDfGMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNvk 571
Cdd:cd14896 387 TLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL-- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 572 gkQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTyASADTGDSGKGKggkkkgssfqTVSA 651
Cdd:cd14896 463 --PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE-AEPQYGLGQGKP----------TLAS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 652 LHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILnpAA 731
Cdd:cd14896 530 RFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL--GS 607
|
650 660 670
....*....|....*....|....*....|....*..
gi 255918225 732 IPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14896 608 ERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
99-768 |
2.83e-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: 400.48 E-value: 2.83e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNaevVAAYRGK--KRSEAPPHIFSISDNAYQYMLT-------D 168
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 169 RENQSILITGESGAGKTVNTKRVIQYFA----SIAAIGDRSKKENPNAnkgtleDQIIQANPALEAFGNAKTVRNDNSSR 244
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISG------SELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 245 FGKFIRIHFG-----ATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDML-LVTNNPYDYAFVSQGE 318
Cdd:cd14895 152 FGKFVRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELqLELLSAQEFQYISGGQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 319 VSVAS--IDDSEELLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDA-------------- 382
Cdd:cd14895 232 CYQRNdgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltv 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 383 ----DKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQY-- 456
Cdd:cd14895 312 qqhlDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpn 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 457 ---------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE- 526
Cdd:cd14895 392 kaankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEq 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 527 KPMGIMSILEEECMFPKASDMTFKAKLYdNHLGKSNNFQKPRnvKGKQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETV 606
Cdd:cd14895 471 RPSGIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAEL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 607 VGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQT---VSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAP 683
Cdd:cd14895 548 FSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSsvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESAS 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 684 GVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPegqfidSRKGAEKLLGSLDIDHNQykFGHT 763
Cdd:cd14895 628 DQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNA------SDATASALIETLKVDHAE--LGKT 699
|
....*
gi 255918225 764 KVFFK 768
Cdd:cd14895 700 RVFLR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-768 |
4.11e-119 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 392.04 E-value: 4.11e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRG-KKRSEAPPHIFSIS----DNAYQYmltdRENQS 173
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTArralENLHGV----NKSQT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 174 ILITGESGAGKTVNTKRVIQYFASiaaigdrSKKENPNankGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF 253
Cdd:cd14876 77 IIVSGESGAGKTEATKQIMRYFAS-------AKSGNMD---LRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 254 GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLD--MLLVTNnpyDYAFVSQGEVSVASIDDSEELL 331
Cdd:cd14876 147 ASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSkyHLLGLK---EYKFLNPKCLDVPGIDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 332 ATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQReeqaepDGTEDA-----------DKSAYLMGLNSADLLKGL 400
Cdd:cd14876 224 EVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTE------QGVDDAaaisneslevfKEACSLLFLDPEALKREL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 401 CHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCIN 480
Cdd:cd14876 298 TVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFIN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 481 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHlgK 560
Cdd:cd14876 378 ITNEMLQKNFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKL--K 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 561 SNNFQKPrnVKGKQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFstyasadtgdsGKGKGGK 640
Cdd:cd14876 456 SNGKFKP--AKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALF-----------EGVVVEK 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 641 KKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 720
Cdd:cd14876 523 GKIAKGSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEF 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 255918225 721 RQRYRILNPaAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14876 603 LYQFKFLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
101-729 |
1.04e-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: 368.41 E-value: 1.04e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEA-PPHIFSISDNAYQYMLTDRE--NQSILI 176
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 177 TGESGAGKTVNTKRVIQYFASIAAiGDRSKKENPNANKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 256
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAA-SPTSWESHKIAER--IEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 257 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILsnkKPELLDMLLVTNNP--YDYAFVSQGEVSVASiDDSEellATD 334
Cdd:cd14880 160 QQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQIC---KGASADERLQWHLPegAAFSWLPNPERNLEE-DCFE---VTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 335 SAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQA---EPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEY 411
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 412 VT--KGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPR-QYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQ 488
Cdd:cd14880 313 QVfkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 489 FFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDmtfkAKLYDNHLGK--SNNFQ 565
Cdd:cd14880 393 HFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSS----AAQLQTRIESalAGNPC 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 566 KPRNvKGKQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFstyaSADTGDSGKGKGGKKKGSS 645
Cdd:cd14880 468 LGHN-KLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLF----PANPEEKTQEEPSGQSRAP 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 646 FQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 725
Cdd:cd14880 543 VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
....
gi 255918225 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 |
2.34e-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: 363.53 E-value: 2.34e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKR-SEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASIAAiGDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT-G 257
Cdd:cd14906 83 ESGSGKTEASKTILQYLINTSS-SNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 258 KLASADIETYLLEKSRVIFQL-KAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASI------------ 324
Cdd:cd14906 162 KIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsnhn 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 325 ---DDSEELLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQ---REEQAEPDGTEDADKSAYLMGLNSADLLK 398
Cdd:cd14906 242 nktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 399 GLCHPRVKVGNE--YVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINAT-LETKQPRQ----------YFIGVLDIAG 465
Cdd:cd14906 322 ALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKfNQNTQSNDlaggsnkknnLFIGVLDIFG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 466 FEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKA 544
Cdd:cd14906 402 FENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 545 SDMTFKAKlYDNHLGKSNNFQKPRNVKGKqeahFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFST 624
Cdd:cd14906 481 SEQSLLEK-YNKQYHNTNQYYQRTLAKGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQ 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 625 YASADTGDSGKGKGGKkkgssfqTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGI 704
Cdd:cd14906 556 QITSTTNTTKKQTQSN-------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTI 628
|
650 660
....*....|....*....|....
gi 255918225 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 |
1.38e-106 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 358.64 E-value: 1.38e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYR-------GKKRSEA---PPHIFSISDNAYQYMLTD 168
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 169 RENQSILITGESGAGKTVNTKRVIQYFA------SIAAIGDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNS 242
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAvhcgtgNNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 243 SRFGKFIRIHF-GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNK----KPELLDMLLVTNNPYDYAFVSQG 317
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 318 EVSVA--SIDDSEELLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQ--KQREEQAEPDGTEDA----------D 383
Cdd:cd14899 242 LCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 384 KSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQY------- 456
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 457 --------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlQACIDLIE-K 527
Cdd:cd14899 402 ddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 528 PMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVV 607
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 608 GLYQKSSLKLMATLFSTYASAD-TGDSGKGKGGKKKGSSFQT------VSALHRENLNKLMTNLKTTHPHFVRCIIPNER 680
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDaNGDSELDGFGGRTRRRAKSaiaavsVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 255918225 681 KAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 725
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
105-768 |
4.71e-106 |
|
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: 354.58 E-value: 4.71e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 105 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRS-----EAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASiaaigdrskkeNPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAY-----------GHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYdYAFVSQGEVSVA-SIDDSEELLATDSAF 337
Cdd:cd14886 156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASKCYDApGIDDQKEFAPVRSQL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 338 DVLsFTAEEKAGVYKLTGAIMHYGNMKFKQKQR---EEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 414
Cdd:cd14886 235 EKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIIS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 415 GQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 494
Cdd:cd14886 314 PVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 495 FVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKP-MGIMSILEEECMFPKASDMTFKAKLyDNHLgKSNNFQKPrnvKGK 573
Cdd:cd14886 394 FKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSFIPG---KGS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 574 QeAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTyASADTGDSGKgkggkkkgssfQTVSALH 653
Cdd:cd14886 468 Q-CNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSD-IPNEDGNMKG-----------KFLGSTF 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 654 RENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL---NPA 730
Cdd:cd14886 535 QLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSS 614
|
650 660 670
....*....|....*....|....*....|....*...
gi 255918225 731 AIPEGQfiDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 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 ... |
101-768 |
5.08e-105 |
|
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: 352.19 E-value: 5.08e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 101 VLYNLKERYAAWMI-YTYSGLFCVTVNPYKWLPvYNAEVvaaYRGKKRSEA-----PPHIFSISDNAY-QYMLTDRENQS 173
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMP-FNSEE---ERKKYLALPdprllPPHIWQVAHKAFnAIFVQGLGNQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 174 ILITGESGAGKTVNTKRVIQYfasiaaIGDRSKKENPNANKGTLEDQIIQ----ANPALEAFGNAKTVRNDNSSRFGKFI 249
Cdd:cd14875 79 VVISGESGSGKTENAKMLIAY------LGQLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 250 RIHF-GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDY-------AFVSQGeVSV 321
Cdd:cd14875 153 KLYFdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYkclnggnTFVRRG-VDG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 322 ASIDDSEELLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDAdKSAYLMGLNSADLLKGLC 401
Cdd:cd14875 232 KTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 402 hprVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLetkQPRQ-----YFIGVLDIAGFEIFDFNSFEQ 476
Cdd:cd14875 311 ---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASI---TPQGdcsgcKYIGLLDIFGFENFTRNSFEQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 477 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLYD 555
Cdd:cd14875 385 LCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 556 NHLGKSNNFQKPRNVKGKQeahFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADtgdsgk 635
Cdd:cd14875 464 QWANKSPYFVLPKSTIPNQ---FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLA------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 636 gkggkkkgSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRI 715
Cdd:cd14875 535 --------RRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRR 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 255918225 716 LYGDF-RQRYRILNPAAIPEGQFIDSRKGAEKLLGSLDIDHN----QYKFGHTKVFFK 768
Cdd:cd14875 607 PIEQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYYQRLYGwakpNYAVGKTKVFLR 664
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
101-768 |
7.49e-104 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 349.69 E-value: 7.49e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 181 GAGKTVNTKRVIQYFASIA-AIGDRSKKENPNAnkgtledqiiqANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAgSVGGVLSVEKLNA-----------ALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFvsqGEVSVASIDD----SEELLATDS 335
Cdd:cd01386 152 ASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF---GIVPLQKPEDkqkaAAAFSKLQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 336 AFDVLSFTAEEKAGVYKLTGAIMHYGN---MKFKQKQREEQAEPdgtEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 412
Cdd:cd01386 229 AMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 413 T---------------KGQSVQQvyySIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN----- 472
Cdd:cd01386 306 TtssgqesparsssggPKLTGVE---ALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrg 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 473 -SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEK---------------PMGIMSILE 536
Cdd:cd01386 383 aTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 537 EECMFPKASDMTFKAKLYdNHLGKSNNFQKPRNV-KGKQEAHFSLVHYAGT--VDYNIMGWLEKNK-DPLNETVVGLYQK 612
Cdd:cd01386 463 EEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLrRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQE 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 613 SSlKLMATLFSTYASADtgdsgkgkggkkkgSSFQtvsalhrenLNKLMTNLKTTHPHFVRCIIPN------ERKAPGV- 685
Cdd:cd01386 542 SQ-KETAAVKRKSPCLQ--------------IKFQ---------VDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPa 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 686 -----MDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA----AIPEGQFIDSRKGAEKLLGSLDIDHN 756
Cdd:cd01386 598 agdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkkLGLNSEVADERKAVEELLEELDLEKS 677
|
730
....*....|..
gi 255918225 757 QYKFGHTKVFFK 768
Cdd:cd01386 678 SYRIGLSQVFFR 689
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-743 |
2.09e-94 |
|
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: 318.38 E-value: 2.09e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKwlPVYNAEVVAAYRgKKRSEAPPHIFSISDNAYQYMLTdRENQSILITGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYFASiaaigdrskkenPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgaTGKL 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE------------RTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpelldmLLVTNNPYDYAFVSQGEVSVasIDDSEELLATDSAFDV 339
Cdd:cd14898 144 TGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSAMKS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 340 LSFTAEEKagVYKLTGAIMHYGNMKFKQkqrEEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 419
Cdd:cd14898 216 LGIANFKS--IEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 420 QVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQyfIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14898 291 QARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 500 EEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFP--KASDMTFKAKLYDNHlgksnnfqkprNVKGKQEAH 577
Cdd:cd14898 369 GMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAwgNVKNLLVKIKKYLNG-----------FINTKARDK 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 578 FSLVHYAGTVDYNIMGWLEKNKdplnetvvglyQKSSLKlmatLFSTYASADTGDSgkgkggkkkgssfQTVSALHRENL 657
Cdd:cd14898 437 IKVSHYAGDVEYDLRDFLDKNR-----------EKGQLL----IFKNLLINDEGSK-------------EDLVKYFKDSM 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 658 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIpegQF 737
Cdd:cd14898 489 NKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLF---EV 565
|
....*.
gi 255918225 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 ... |
100-727 |
1.92e-93 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 318.30 E-value: 1.92e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYR---GKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 176
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 177 TGESGAGKTVNTKRVIQYFASIAAigdrskkenpnANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 256
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTCRAS-----------SSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 257 GK-LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGE----VSVASIDDSEELL 331
Cdd:cd14878 151 KKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHL-NNLCAHRYLNQTMredvSTAERSLNREKLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 332 ATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEY 411
Cdd:cd14878 230 VLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 412 VTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQ 487
Cdd:cd14878 310 IIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 488 QFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACID-LIEKPMGIMSILEEECMFPKASDMTFKAKLyDNHLGKSNNFQK 566
Cdd:cd14878 390 HYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPSGFLSLLDEESQMIWSVEPNLPKKL-QSLLESSNTNAV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 567 PRNVKG--------KQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTyasadtgdsgkgkg 638
Cdd:cd14878 469 YSPMKDgngnvalkDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS-------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 639 gkkkgsSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 718
Cdd:cd14878 535 ------KLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFS 608
|
....*....
gi 255918225 719 DFRQRYRIL 727
Cdd:cd14878 609 DFLSRYKPL 617
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-768 |
1.24e-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: 309.27 E-value: 1.24e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAA--------WMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 171 NQSILITGESGAGKTVNTKRVIQYfasIAAIGDRSKkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIR 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTY---LAAVSDRRH----GADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 251 IHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKK-PELLDMLLVTNNPYDYafvsqgevsvasiddseE 329
Cdd:cd14887 154 LHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVaAATQKSSAGEGDPEST-----------------D 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 330 LLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEP-----------DGTEDADKSAYLMGLNS----- 393
Cdd:cd14887 217 LRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKrkltsvsvgceETAADRSHSSEVKCLSSglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 394 -------ADLLKGLCHPRVKVGNEYV------------TKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPR 454
Cdd:cd14887 297 easrkhlKTVARLLGLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 455 QY--------------FIGVLDIAGFEIF---DFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFI--DFG 515
Cdd:cd14887 377 SEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 516 MDLQACIDLIEKP------------------------MGIMSILEEE-CMFPKASDMTFKAKLYDNHLGK----SNNFQK 566
Cdd:cd14887 457 FSFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKN 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 567 PRNVKGKQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNEtvvglyqksSLKLMATLFSTYASADTGDSGKGKGGKKKGSsf 646
Cdd:cd14887 537 ITPALSRENLEFTVSHFACDVTYDARDFCRANREATSD---------ELERLFLACSTYTRLVGSKKNSGVRAISSRR-- 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 647 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14887 606 STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYET 685
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 255918225 727 LNPAAIPEgqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14887 686 KLPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
101-768 |
1.98e-86 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 297.31 E-value: 1.98e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEvvaaYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 181 GAGKTVNTKRVIQYFASiaaigdRSKKENPNANkgTLEDqiiqANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 260
Cdd:cd14937 79 GSGKTEASKLVIKYYLS------GVKEDNEISN--TLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 261 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPyDYAFVSQGEVSVASIDDSEELLATDSAFDVL 340
Cdd:cd14937 147 SSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDKM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 341 SFTAEEKAGVYKLTGAIMhYGNMKFKQ-----KQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKG 415
Cdd:cd14937 226 NMHDMKDDLFLTLSGLLL-LGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 416 QSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14937 305 LSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 496 VLEQEEYKKEGIEWEFIDFGMDlQACIDLIEKPMGIMSILEEECMFPKASDMTFkAKLYDNHLGKSNNFQkprNVKGKQE 575
Cdd:cd14937 385 EKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYA---STKKDIN 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 576 AHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLfstYASADTGDSGKGKggkkkgssfQTVSALHRE 655
Cdd:cd14937 460 KNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSL---YEDVEVSESLGRK---------NLITFKYLK 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 656 NLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRIcRKGFPNRILYGDFRQRYRILNPAAIPEG 735
Cdd:cd14937 528 NLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDS 606
|
650 660 670
....*....|....*....|....*....|...
gi 255918225 736 QFIDSRKGAEKLLGSLDIDhnQYKFGHTKVFFK 768
Cdd:cd14937 607 SLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
105-767 |
1.37e-85 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 295.23 E-value: 1.37e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 105 LKERYAAWMIYTY---SGLfcVTVNPYKWLPVYNAEVVAAYR-------GKKRSEAPPHIFSISDNAYQYMLTDRENQSI 174
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 175 LITGESGAGKTVNTKRVIQYFASIAAigdRSKKENPnankgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 254
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSS---HSKKGTK------LSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 255 ATGKLASADIETYLLEKSRVIfQLKA-ERNYHIFYQILSNKKPELLDmLLVTNNPYDYAFV----SQGEVSVASIDDSE- 328
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQ-HLGLDDPSDYALLasygCHPLPLGPGSDDAEg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 329 -ELLATdsAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQkqreeqaEPDGTEDA---------DKSAYLMGLNSADLLK 398
Cdd:cd14879 237 fQELKT--ALKTLGFKRKHVAQICQLLAAILHLGNLEFTY-------DHEGGEESavvkntdvlDIVAAFLGVSPEDLET 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 399 GLCHPRVKVGNEYVT-----KGQSVQQvyysiGALAKSVYEKMFNWMVTRINATL-ETKQPRQYFIGVLDIAGFEIFD-- 470
Cdd:cd14879 308 SLTYKTKLVRKELCTvfldpEGAAAQR-----DELARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSst 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 471 -FNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEEC-MFPKASDM 547
Cdd:cd14879 383 gGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 548 TFKAKLyDNHLGKSNNFQKPRNVKGKQEAH-FSLVHYAGTVDYNIMGWLEKNKDPLNETVVglyqksslklmaTLFSTya 626
Cdd:cd14879 462 QMLEAL-RKRFGNHSSFIAVGNFATRSGSAsFTVNHYAGEVTYSVEGFLERNGDVLSPDFV------------NLLRG-- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 627 sadtgdsgkgkggkkkgssfqtvSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRI 706
Cdd:cd14879 527 -----------------------ATQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAAR 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255918225 707 CRKGFPNRILYGDFRQRYrilnpaaIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFF 767
Cdd:cd14879 584 LRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-716 |
1.74e-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: 1.74e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEA-------PPHIFSISDNAYQYMLTDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 171 NQSILITGESGAGKTVNTKRVIQYFASIAaiGDRSKKEnpnankgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIR 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQ--TDSQMTE--------RIDKLIYINNILESMSNATTIKNNNSSRCGRINL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 251 IHF---------GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFV------- 314
Cdd:cd14884 151 LIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLnpdeshq 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 315 ---SQGEVSVAS--IDDSEELLATDSA-----FDVLSFTAEEKAGV---YKLTGAIMHYGNMKFKQkqreeqaepdgted 381
Cdd:cd14884 231 krsVKGTLRLGSdsLDPSEEEKAKDEKnfvalLHGLHYIKYDERQInefFDIIAGILHLGNRAYKA-------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 382 adkSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINAT----------LETK 451
Cdd:cd14884 297 ---AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNvlkckekdesDNED 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 452 QPR--QYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEW--EFIDFGMDLQACIDLIEK 527
Cdd:cd14884 374 IYSinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICcsDVAPSYSDTLIFIAKIFR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 528 PMGIMSILEEECMfpKASDMTFKAKLYDNH----------LGK-SNNFQKPRNVKGK-QEAHFSLVHYAGTVDYNIMGWL 595
Cdd:cd14884 454 RLDDITKLKNQGQ--KKTDDHFFRYLLNNErqqqlegkvsYGFvLNHDADGTAKKQNiKKNIFFIRHYAGLVTYRINNWI 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 596 EKNKDPLNETVVGLYQKSSlklMATLFSTYASADTGDsgkgkggkkkgssFQTVSALHRENLNKLMTNLKTTHPHFVRCI 675
Cdd:cd14884 532 DKNSDKIETSIETLISCSS---NRFLREANNGGNKGN-------------FLSVSKKYIKELDNLFTQLQSTDMYYIRCF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 255918225 676 IPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRIL 716
Cdd:cd14884 596 LPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
100-736 |
7.44e-70 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 248.25 E-value: 7.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYrgkkrseappHIFSISDNAYQYMLTDREN-QSILITG 178
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 179 ESGAGKTVNTKRVIQYFASiaaigdrskkeNPNANKGTLEDQIIQAnpALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14874 72 ESGSGKSYNAFQVFKYLTS-----------QPKSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLYKRNVL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNpYDYAFVSQGEVSVASIDDSEELLATDSAFD 338
Cdd:cd14874 139 TGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL-QKFFYINQGNSTENIQSDVNHFKHLEDALH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 339 VLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQR---EEQAEPDGTEDADK-SAYLMGLNSADLLKGLChPRVKVGNEYvtk 414
Cdd:cd14874 218 VLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKwVAFLLEVDFDQLVNFLL-PKSEDGTTI--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 415 gqSVQQVYYSIGALAKSVYEKMFNWMVTRINatLETKQPRQY-FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 493
Cdd:cd14874 294 --DLNAALDNRDSFAMLIYEELFKWVLNRIG--LHLKCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKH 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 494 MFVLEQEEYKKEGIEwefIDFGMdlQACID-------LIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNnFQK 566
Cdd:cd14874 370 SFHDQLVDYAKDGIS---VDYKV--PNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 567 PRNvkgKQEAHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYaSADTGDSgkgkggkkkgssF 646
Cdd:cd14874 444 ARN---KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY-SSNTSDM------------I 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 647 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14874 508 VSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRC 587
|
650
....*....|
gi 255918225 727 LNPAAIPEGQ 736
Cdd:cd14874 588 LLPGDIAMCQ 597
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-748 |
8.18e-70 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 248.49 E-value: 8.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPvyNAEVVAAYRGKKRSeapPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 180 SGAGKTVNTKRVIQYFASIAAIGDRSkkenpNANKgtledQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGKL 259
Cdd:cd14881 77 SGSGKTYASMLLLRQLFDVAGGGPET-----DAFK-----HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDGAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDML-LVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 338
Cdd:cd14881 146 YRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLhLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKACLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 339 VLS--FTaeekaGVYKLTGAIMHYGNMKFKQKQrEEQAEPDGTEDADKSAYLMGLNSADLLKGL---CHprvkvgneyVT 413
Cdd:cd14881 226 ILGipFL-----DVVRVLAAVLLLGNVQFIDGG-GLEVDVKGETELKSVAALLGVSGAALFRGLttrTH---------NA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 414 KGQ---SVQQVYYSIG---ALAKSVYEKMFNWMVTRIN------ATLETKQpRQYFIGVLDIAGFEIFDFNSFEQLCINF 481
Cdd:cd14881 291 RGQlvkSVCDANMSNMtrdALAKALYCRTVATIVRRANslkrlgSTLGTHA-TDGFIGILDMFGFEDPKPSQLEHLCINL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 482 TNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-IDFgMDLQACIDLIEK-PMGIMSILEEECMfPKASDMTFKAKLYDNHlg 559
Cdd:cd14881 370 CAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQH-- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 560 KSNN-FQKPRNVKGKQeahFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMatlFSTYasadTGDsgkgkg 638
Cdd:cd14881 446 RQNPrLFEAKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNFG---FATH----TQD------ 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 639 gkkkgssFQTvsalhreNLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 718
Cdd:cd14881 510 -------FHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFK 575
|
650 660 670
....*....|....*....|....*....|
gi 255918225 719 DFRQRYRILNPAAiPEGQFIDSRKGAEKLL 748
Cdd:cd14881 576 AFNARYRLLAPFR-LLRRVEEKALEDCALI 604
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
105-720 |
9.51e-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: 9.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 105 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYrgKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAG 183
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 184 KTVNTKRVIQYFASIAAigDRSKkenpnankgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASAD 263
Cdd:cd14905 85 KSENTKIIIQYLLTTDL--SRSK---------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 264 IETYLLEKSRVIFQLKAERNYHIFYQILSN-KKPELLDMLLVTNNPYDYaFVSQGEVSVASIDDSEELLATDSAFDVLSF 342
Cdd:cd14905 154 LYSYFLDENRVTYQNKGERNFHIFYQFLKGiTDEEKAAYQLGDINSYHY-LNQGGSISVESIDDNRVFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 343 TAEEKAGVYKLTGAIMHYGNMKFKQKQREeqaepdgTEDADKSaylmglnsadLLKGLCH----PRVKVGNEYVT-KGQS 417
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRT----------LIESLSHnitfDSTKLENILISdRSMP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 418 VQQVYYSIGALAKSVYEKMFNWMVTRINATLetkQPRQY--FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14905 296 VNEAVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 496 VLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKpmgIMSILEEECMFPKASDMTFKAKLydnhlgksNNFQKPRNVKGKQE 575
Cdd:cd14905 373 KQEQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKKP 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 576 AHFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMAT---LFSTYASADTGDSGKGKGGKKKGSSFQTVSAL 652
Cdd:cd14905 442 NKFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSrdgVFNINATVAELNQMFDAKNTAKKSPLSIVKVL 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 653 ------HRENLNKLMTN-------------------LKTTHP-------------HFVRCIIPNERKAPGVMDNPLVMHQ 694
Cdd:cd14905 522 lscgsnNPNNVNNPNNNsgggggggnsgggsgsggsTYTTYSstnkainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQ 601
|
650 660 670
....*....|....*....|....*....|
gi 255918225 695 LRCNGVLEGIRICRKGFP----NRILYGDF 720
Cdd:cd14905 602 IKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-767 |
7.32e-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: 230.24 E-value: 7.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 102 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKR----------SEAPPHIFSISDNAYQYMLTDREN 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 172 QSILITGESGAGKTVNTKRVIQYFASIA-AIGDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIR 250
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGdETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 251 IHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKK--PELLDMLLVTNNPYDYAFVSQG--EVSVASID- 325
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFALDa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 326 -DSEELLatdSAFDVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLN-------SADLL 397
Cdd:cd14893 244 rDYRDLM---SSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQSCALKdpaqillAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 398 KglCHPRV------------KVGNEYVT--KGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPR--------- 454
Cdd:cd14893 321 E--VEPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksnivin 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 455 QYFIGVLDIAGFEIFD--FNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWE-------FIDFGMDLQACIDLI 525
Cdd:cd14893 399 SQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVEnrltvnsNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 526 E-KPMGIMSILEEECMFPKASDMTFKAKLYDNH-----LGKSNNFQKPRNVKGKQEAHFSLV----HYAGTVDYNIMGWL 595
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNeavggLSRPNMGADTTNEYLAPSKDWRLLfivqHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 596 EKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDS--GKGKGGKKKGSSFQTVSALHRENLN--------------K 659
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKaaKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 660 LMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRilnpaaipegQFID 739
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK----------NVCG 708
|
730 740 750
....*....|....*....|....*....|..
gi 255918225 740 SRKGAEKLLGSLD----IDHNQYKFGHTKVFF 767
Cdd:cd14893 709 HRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-251 |
5.82e-61 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 206.43 E-value: 5.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 121 FCVTVNPYKWLPVYNAEVV-AAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASIA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 255918225 200 AIGDRSKKEN----PNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 251
Cdd:cd01363 81 FNGINKGETEgwvyLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
101-727 |
5.52e-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: 5.52e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 181 GAGKTVNTKRVIQYfasIAAIGDrskkenpnANKGTLEdQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 260
Cdd:cd14882 83 YSGKTTNARLLIKH---LCYLGD--------GNRGATG-RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 261 SADIETYLLEKSRVIFQLKAERNYHIFYQILS--NKKPELLDMLLVTNNPYDYAFVSQG-------------EVSVASID 325
Cdd:cd14882 151 GAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERYK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 326 DSEELLAtdsafdVLSFTAEEKAGVYKLTGAIMHYGNMKFKQKQREeqAEPDGTEDADKSAYLMGLNSADLLKGLCHPRV 405
Cdd:cd14882 231 EFEEILK------DLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 406 KVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETkqPR-----QYFIGVLDIAGFEIFDFNSFEQLCIN 480
Cdd:cd14882 303 IKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 481 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEecmfpkAS-DMTFKAKLYDNHLG 559
Cdd:cd14882 381 TLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD------ASrSCQDQNYIMDRIKE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 560 KSNNFQKPRNvkgkqeAH-FSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTyasadtgdsgkgkg 638
Cdd:cd14882 455 KHSQFVKKHS------AHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 639 gkKKGSSFQTVSALHR----ENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNR 714
Cdd:cd14882 515 --SQVRNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYR 592
|
650
....*....|...
gi 255918225 715 ILYGDFRQRYRIL 727
Cdd:cd14882 593 IPFQEFLRRYQFL 605
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-766 |
2.88e-50 |
|
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: 191.97 E-value: 2.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSE-APPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 178 GESGAGKTVNTKRVIQYFA------------SIAAIGDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRF 245
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAyqvkgsrrlptnLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 246 GKFIRIHFgATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYdYAFVSQGEVSVASID 325
Cdd:cd14938 161 SKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIEN-YSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 326 DSEELLATDSAFDVLSFTAEEKAGVYKLTGAIMHYGN-------------MKFKQKQRE----------EQAEPDGTEDA 382
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 383 DKSAYL----MGLNSADLLKGLCHPRVkVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYF- 457
Cdd:cd14938 319 VKNLLLacklLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININt 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 458 --IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM--GIMS 533
Cdd:cd14938 398 nyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 534 ILEEECMfPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAhFSLVHYAGTVDYNIMGWLEKNKDPLNETVVGLYQKS 613
Cdd:cd14938 478 LLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 614 SLKLMATLFSTYASADTGDSGKGKGGKKKGSSF-----------QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKA 682
Cdd:cd14938 556 ENEYMRQFCMFYNYDNSGNIVEEKRRYSIQSALklfkrrydtknQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKR 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 683 P-GVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPaaipegqfiDSRKGAEKLLGSLDIDHNQYKFG 761
Cdd:cd14938 636 ElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMIG 706
|
....*
gi 255918225 762 HTKVF 766
Cdd:cd14938 707 NNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
846-1745 |
2.16e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 131.72 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 846 ETEKEMANMKEEFGRVKDALeksearrKELEEKMVSllqekndlqLQVQAEQdnlndAEercdQLIKNKIQLEAKVKEM- 924
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDIL-------NELERQLKS---------LERQAEK-----AE----RYKELKAELRELELALl 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 925 TERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEA 1004
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1005 HQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKK 1084
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1085 KEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEeeleaertaRAKVEKLRSDLSRELEEISERLEEAGGATSVQIE 1164
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELL---------KKLEEAELKELQAELEELEEELEELQEELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1165 MNKKREAEFQKMRRDLEEATLQHEATAAALrkkhaDSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTsnmeQIIKAK 1244
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARL-----DSLERLQENLEGFSEGVKALLKNQSGLSGILGVLS----ELISVD 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1245 ANLEK-VSRTLEDQANEYRVKLEEAQRSLNDFTTQ----RAKLQTENGELARQLEEKEALISQLTRGKLSYtqqmedLKR 1319
Cdd:TIGR02168 533 EGYEAaIEAALGGRLQAVVVENLNAAKKAIAFLKQnelgRVTFLPLDSIKGTEIQGNDREILKNIEGFLGV------AKD 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1320 QLEEEGKAKNALAHALQSSRHDCDL-----LREQYEEEMEAkAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKK 1394
Cdd:TIGR02168 607 LVKFDPKLRKALSYLLGGVLVVDDLdnaleLAKKLRPGYRI-VTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEK 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1395 LAQRLQDAEEAVEAVNAkcssLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQK 1474
Cdd:TIGR02168 686 IEELEEKIAELEKALAE----LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1475 EARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGeggknvhELEKIRKQLEVEKLELQSALEEAEASLE 1554
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD-------ELRAELTLLNEEAANLRERLESLERRIA 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1555 HEEGKILRAQLEFNQIKAEIErKLAEKDEEMEQAKRNHLRMVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQA 1634
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIE-SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1635 NRIASEAQKHLKNSQAHLKDTQLQLDD-AVHANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRK-------LAEQ 1706
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlAAIE 993
|
890 900 910
....*....|....*....|....*....|....*....
gi 255918225 1707 ELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEE 1745
Cdd:TIGR02168 994 EYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1175-1929 |
1.40e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 125.94 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1175 KMRRdlEEATLQHEATAAALrKKHADSVAELGEQIDNLQRVKQKLEKEKsefklELddvtsnmeqiikaKANLEKVSRTL 1254
Cdd:TIGR02168 171 KERR--KETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERYK-----EL-------------KAELRELELAL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1255 edqaneYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHA 1334
Cdd:TIGR02168 230 ------LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1335 LQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKK------LAQRLQDAEEAVEA 1408
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaeleeLESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1409 VNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEwkqkyeesqselessqKEARSLSTELFKLKN 1488
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE----------------AELKELQAELEELEE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1489 AYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFN 1568
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1569 QIKAEIERKLAekdeeMEQAKRNHLRM--VDSLQTSLDA-ETRSRNEALRVKKKMEGDLNEMEIQLSQANRIAS------ 1639
Cdd:TIGR02168 528 LISVDEGYEAA-----IEAALGGRLQAvvVENLNAAKKAiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNiegflg 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1640 ------EAQKHLKNSQAHLKDTQLQLDDAVHANDDLKE---NIAIV------------------ERRNNLL--QAELEEL 1690
Cdd:TIGR02168 603 vakdlvKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrpGYRIVtldgdlvrpggvitggsaKTNSSILerRREIEEL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1691 RAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEE 1770
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1771 LKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIK 1850
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKE--------ELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1851 ELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1929
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
978-1873 |
5.49e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 123.63 E-value: 5.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 978 KNLTEEMAGldeiIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVddlegslEQEKKVRmDLERAKRKL 1057
Cdd:TIGR02168 158 RAIFEEAAG----ISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQA-------EKAERYK-ELKAELREL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1058 EGDLkltqesimdLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKL 1137
Cdd:TIGR02168 226 ELAL---------LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1138 RSDLSRELEEISERLEEAGG---ATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQR 1214
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERqleELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1215 VKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEyrVKLEEAQRSLNDFTTQRAKLQTENGELARQLE 1294
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE--IEELLKKLEEAELKELQAELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1295 EKEALISQLTRGKLSYTQQMEDLkRQLEEEGKAKNALAHALQSsrhdcdlLREQYEEEMEAKAELQRVLSKANSEVAQWR 1374
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLER-------LQENLEGFSEGVKALLKNQSGLSGILGVLS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1375 TKYETDaiqrtEELEEAKKK-LAQRLQ-----DAEEAVEAVNA-------KCSSLEKTKHR---LQNEIEDLMVDVERSN 1438
Cdd:TIGR02168 527 ELISVD-----EGYEAAIEAaLGGRLQavvveNLNAAKKAIAFlkqnelgRVTFLPLDSIKgteIQGNDREILKNIEGFL 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1439 AAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNL-----QEEISD 1513
Cdd:TIGR02168 602 GVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSsilerRREIEE 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1514 LTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERkLAEKDEEMEQAKRNHL 1593
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ-LEERIAQLSKELTELE 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1594 RMVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDavhanddLKENI 1673
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES-------LERRI 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1674 AIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIEtservqlLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNA 1753
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-------LESELEALLNERASLEEALALLRSELEELSEELREL 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1754 EEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNMEQTIKDL--QHRLDEAEQIALK-GGKKQLQKLEARVRELENELEA 1830
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLE---LRLEGLEVRIDNLQERLseEYSLTLEEAEALEnKIEDDEEEARRRLKRLENKIKE 983
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 255918225 1831 EQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKL 1873
Cdd:TIGR02168 984 LGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
835-1454 |
1.56e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 118.89 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 835 YFKIKPLLKSAETE---KEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLI 911
Cdd:COG1196 215 YRELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 912 KNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEII 991
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 992 AKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDL 1071
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1072 ENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAK---------VEKLRSDLS 1142
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLaglrglagaVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1143 RELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKE 1222
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1223 KSEFKLELDDVTSnmeqiikAKANLEKVSRTLEDQANEYRVKLEEAQRSLndftTQRAKLQTENGELARQLEEKEALISQ 1302
Cdd:COG1196 615 YYVLGDTLLGRTL-------VAARLEAALRRAVTLAGRLREVTLEGEGGS----AGGSLTGGSRRELLAALLEAEAELEE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1303 LTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAqwrtKYETDAI 1382
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPEP 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1383 QRTEELEEAKKKLAQRLQD-------AEEAVEAVNAKCSSLEKTKHRLQNEIEDLM-----VDVERSNAAAAALDKKQRN 1450
Cdd:COG1196 760 PDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEeaieeIDRETRERFLETFDAVNEN 839
|
....
gi 255918225 1451 FDKI 1454
Cdd:COG1196 840 FQEL 843
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
842-1610 |
1.03e-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: 116.31 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 842 LKSAETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKV 921
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 922 KEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKAL 1001
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1002 QEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLEraKRKLEGDLKLTQESIMDLENDKLQLEEK 1081
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1082 LKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERT---ARAKVEKLRSDLSRELEEISER------- 1151
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfseGVKALLKNQSGLSGILGVLSELisvdegy 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1152 ---LEEAGGATSVQIEMNKKREAefqkmrRDLEEATLQHEATAAAL----RKKHADSVAELGEQIDNLQRVKQ---KLEK 1221
Cdd:TIGR02168 536 eaaIEAALGGRLQAVVVENLNAA------KKAIAFLKQNELGRVTFlpldSIKGTEIQGNDREILKNIEGFLGvakDLVK 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1222 EKSEFKLEL----------DDVTSNMEQIIKAKANLEKVSRTLE------------DQAN----EYRVKLEEAQRSLNDF 1275
Cdd:TIGR02168 610 FDPKLRKALsyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDlvrpggvitggsAKTNssilERRREIEELEEKIEEL 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1276 TTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEA 1355
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1356 KAELQRVLSKANSEVAQWRTKYETDAIQRT------EELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIED 1429
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKalrealDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1430 LMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTEL-------FKLKNAYEESLEHLETFKR 1502
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELreleskrSELRRELEELREKLAQLEL 929
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1503 ENKNLQEEISDLTEQLGEGGKNVHELekirkqLEVEKLELQSALEEAEASLEHEEGKI-------LRAQLEFNQIKaeiE 1575
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYSLTLEE------AEALENKIEDDEEEARRRLKRLENKIkelgpvnLAAIEEYEELK---E 1000
|
810 820 830
....*....|....*....|....*....|....*..
gi 255918225 1576 RK--LAEKDEEMEQAKRNHLRMVDslqtSLDAETRSR 1610
Cdd:TIGR02168 1001 RYdfLTAQKEDLTEAKETLEEAIE----EIDREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1249-1925 |
1.33e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 112.84 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1249 KVSRTLEDQANEYRVKLEEAQRSLndfttqraKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEeegKAK 1328
Cdd:TIGR02168 145 KISEIIEAKPEERRAIFEEAAGIS--------KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAE---KAE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1329 NALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYETdAIQRTEELEEAKKKLAQRLQDAEEAVEA 1408
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1409 VNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKN 1488
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1489 AYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLE-- 1566
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEel 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1567 ------FNQIKAEIERKLAEKDEEMEQAKRNH------LRMVDSLQTSLDAETRSRNEALRVKKKMEGDL---------- 1624
Cdd:TIGR02168 453 qeelerLEEALEELREELEEAEQALDAAERELaqlqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvd 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1625 NEMEIQLSQA------------NRIASEAQKHLKNSQAH---------LKDTQLQLDDA--------------------- 1662
Cdd:TIGR02168 533 EGYEAAIEAAlggrlqavvvenLNAAKKAIAFLKQNELGrvtflpldsIKGTEIQGNDReilkniegflgvakdlvkfdp 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1663 ------------VHANDDLKENIAI----------------------------VERRNNLL--QAELEELRAVVEQTERS 1700
Cdd:TIGR02168 613 klrkalsyllggVLVVDDLDNALELakklrpgyrivtldgdlvrpggvitggsAKTNSSILerRREIEELEEKIEELEEK 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1701 RKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAEEK---AKKAITDA----AMMAEELKK 1773
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqLSKELTELeaeiEELEERLEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1774 EQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELT 1853
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALRE-ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255918225 1854 YQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1925
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1075-1731 |
1.33e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.17 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1075 KLQLEEKLKKKE---FDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISER 1151
Cdd:COG1196 217 ELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1152 LEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALrkkhadsvAELGEQIDNLQRVKQKLEKEKSEFKLELD 1231
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL--------EELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1232 DVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTrgklsyt 1311
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE------- 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1312 QQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEA 1391
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1392 KKKLAQRLQDAEEAVEAVnakcsslektkhrLQNEIEDLMVDVERSNAAAAAldkKQRNFDKILAEWKQKYEESQSELES 1471
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAA-------------LEAALAAALQNIVVEDDEVAA---AAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1472 SQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKnvhelekIRKQLEVEKLELQSALEEAEA 1551
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR-------RAVTLAGRLREVTLEGEGGSA 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1552 SLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRMVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQL 1631
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1632 SQANRIASEaqkhlknsqahlkdtqlqLDDAVHANDDLKENIAIVERRNNLLQAELEELRAVVEqtersrkLAEQELIET 1711
Cdd:COG1196 739 EELLEEEEL------------------LEEEALEELPEPPDLEELERELERLEREIEALGPVNL-------LAIEEYEEL 793
|
650 660
....*....|....*....|
gi 255918225 1712 SERVQLLHSQNTSLINQKKK 1731
Cdd:COG1196 794 EERYDFLSEQREDLEEARET 813
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
842-1591 |
3.70e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 104.76 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 842 LKSAETEKEMAnmkEEFGRVKDalEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKV 921
Cdd:TIGR02169 200 LERLRREREKA---ERYQALLK--EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 922 KEMTERLED--EEEMNA------ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAK 993
Cdd:TIGR02169 275 EELNKKIKDlgEEEQLRvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 994 LTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLEN 1073
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1074 DKLQLEEKLKKKEFDISQQNSKIE---------DEQALAL-----QLQKKLKENQARIEELEEELEAERTA----RAKVE 1135
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEqlaadlskyEQELYDLkeeydRVEKELSKLQRELAEAEAQARASEERvrggRAVEE 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1136 KLRSDLS------RELEEISER----LEEAGG-----------ATSVQ-IEMNKKREA------EFQKMRRDLEEATLQH 1187
Cdd:TIGR02169 515 VLKASIQgvhgtvAQLGSVGERyataIEVAAGnrlnnvvveddAVAKEaIELLKRRKAgratflPLNKMRDERRDLSILS 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1188 EATAAALrkkhADSVAELGEQIDNLQR-------VKQKLEKEKS---EFKL-----ELDDVTSNMEQIIKAKANLEKVSR 1252
Cdd:TIGR02169 595 EDGVIGF----AVDLVEFDPKYEPAFKyvfgdtlVVEDIEAARRlmgKYRMvtlegELFEKSGAMTGGSRAPRGGILFSR 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1253 TLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGEL-------ARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEG 1325
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELsqelsdaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1326 KAKNALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKanSEVAQWRTKYetdaiqrtEELEEAKKKLAQRLQDAEEA 1405
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAEL--------SKLEEEVSRIEARLREIEQK 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1406 VEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFK 1485
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1486 LKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIR------KQLEVEKLELQSALEEAE-----ASLE 1554
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEpvnmlAIQE 980
|
810 820 830
....*....|....*....|....*....|....*...
gi 255918225 1555 HEEGKILRAQLEFNQIKAEIERK-LAEKDEEMEQAKRN 1591
Cdd:TIGR02169 981 YEEVLKRLDELKEKRAKLEEERKaILERIEEYEKKKRE 1018
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
989-1851 |
1.67e-21 |
|
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: 102.50 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 989 EIIAKLTKE--KKALQEAHQQaLDDLQAEEDKVNTL-TKSKVKLEQQVDDLEGSLEQ---EKKVRMDLERAKRKLEGDLK 1062
Cdd:pfam15921 66 KIIAYPGKEhiERVLEEYSHQ-VKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1063 ltqesiMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAE------------RTA 1130
Cdd:pfam15921 145 ------NQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1131 RAKVEKLRSDLSRELEEISERLEEAGGA-TSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQI 1209
Cdd:pfam15921 219 GSAISKILRELDTEISYLKGRIFPVEDQlEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1210 DNLQRVKQKLEKEKSEFKLELDDVTSNMEQIikaKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGEL 1289
Cdd:pfam15921 299 SQLEIIQEQARNQNSMYMRQLSDLESTVSQL---RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1290 ARQLE---------EKEALISQLTRGKL-----SYTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCdllREQYEEEMEA 1355
Cdd:pfam15921 376 DDQLQklladlhkrEKELSLEKEQNKRLwdrdtGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEC---QGQMERQMAA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1356 KAELQRVLSKANSEVAQWRTKYE---------TDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNE 1426
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEmlrkvveelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1427 IEDLMVD---VERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFK-- 1501
Cdd:pfam15921 533 LQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKil 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1502 RENKNLQeeisdlteqlgeggknVHELEKIRKQLEVEKLELQSALEE---AEASLEHEEGKILR----AQLEFNQIKAEI 1574
Cdd:pfam15921 613 KDKKDAK----------------IRELEARVSDLELEKVKLVNAGSErlrAVKDIKQERDQLLNevktSRNELNSLSEDY 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1575 E---RKLAEKDEEMEQAKrNHLRM-VDSLQTSLDaetRSRNEAlrvkKKMEG-DLNEMEIQLSQANRIASEAQK--HLKN 1647
Cdd:pfam15921 677 EvlkRNFRNKSEEMETTT-NKLKMqLKSAQSELE---QTRNTL----KSMEGsDGHAMKVAMGMQKQITAKRGQidALQS 748
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1648 SQAHLKDTQLQLDDAVH----ANDDLKENIAIVERRNNLLQAELEELRAvvEQTERSRKLAEQELIETSERVQLLHSQNt 1723
Cdd:pfam15921 749 KIQFLEEAMTNANKEKHflkeEKNKLSQELSTVATEKNKMAGELEVLRS--QERRLKEKVANMEVALDKASLQFAECQD- 825
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1724 slINQKKKMESDLTQLQ--TEVEEAVQECRNAEEKAKKAITDAAMMAE---ELKKEQDTSAHL-----------ERMKKN 1787
Cdd:pfam15921 826 --IIQRQEQESVRLKLQhtLDVKELQGPGYTSNSSMKPRLLQPASFTRthsNVPSSQSTASFLshhsrktnalkEDPTRD 903
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255918225 1788 MEQTIKDLQHRLDEAEQIAL-----KGGKKQLQKLEARVRELENELE-----AEQKRNAESVKGMRKSERRIKE 1851
Cdd:pfam15921 904 LKQLLQELRSVINEEPTVQLskaedKGRAPSLGALDDRVRDCIIESSlrsdiCHSSSNSLQTEGSKSSETCSRE 977
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
845-1580 |
2.75e-21 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 102.07 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 845 AETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLqLQVQAEQDNLNDAEERcdQLIKNKIQLEAKVKEM 924
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKEKREYEGY--ELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 925 TERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLEL---------------TLAKVEKEKHATENKVKNLTEEMAGLDE 989
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlgeeeqlrvkeKIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 990 IIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQE-----------KKVRMDLERAKRK-- 1056
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefaetrdelKDYREKLEKLKREin 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1057 -LEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVE 1135
Cdd:TIGR02169 403 eLKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1136 KLRSDLSRELEEISERL----EEAGGATSVQIEMNKKREAEFQKMrRDLEEATLQHEA---TAAALRKKHA----DSVAE 1204
Cdd:TIGR02169 483 KELSKLQRELAEAEAQAraseERVRGGRAVEEVLKASIQGVHGTV-AQLGSVGERYATaieVAAGNRLNNVvvedDAVAK 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1205 lgEQIDNLQRVK------------QKLEKEKS--------EFKLELDDVTSNMEQIIKAKANLEKVSRTLE---DQANEY 1261
Cdd:TIGR02169 562 --EAIELLKRRKagratflplnkmRDERRDLSilsedgviGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEaarRLMGKY 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1262 R-VKLE--------------EAQRSLNDFTT-QRAKLQTENGELARQLEEKEALISQLTRGK---LSYTQQMEDLKRQLE 1322
Cdd:TIGR02169 640 RmVTLEgelfeksgamtggsRAPRGGILFSRsEPAELQRLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIG 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1323 EEGKAKNALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQwrtkYETDAIQRTEELEEAKKKLAQrlqda 1402
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE----LEEDLHKLEEALNDLEARLSH----- 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1403 eEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTE 1482
Cdd:TIGR02169 791 -SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1483 LFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEgKILR 1562
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-EIPE 948
|
810
....*....|....*...
gi 255918225 1563 AQLEFNQIKAEIERKLAE 1580
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1108-1911 |
3.64e-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: 101.30 E-value: 3.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1108 KKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEaggatsVQIEMNKKReaEFQKMRRDLEEAtlqh 1187
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLER------LRREREKAE--RYQALLKEKREY---- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1188 EATAAALRKKHADsvaelgEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANL-EKVSRTLEDQANEYRVKLE 1266
Cdd:TIGR02169 224 EGYELLKEKEALE------RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1267 EaqrslndFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLR 1346
Cdd:TIGR02169 298 E-------LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1347 EQYEEEMEAKAELQRvlskansEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNE 1426
Cdd:TIGR02169 371 AELEEVDKEFAETRD-------ELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1427 IEDLMVDVErsnaaaaALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTElfklknayeesLEHLETFKRENKN 1506
Cdd:TIGR02169 443 KEDKALEIK-------KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE-----------LAEAEAQARASEE 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1507 LQEEISDLTEQLGEGGKNVHELekIRKQLEVEKlELQSALEEA-----------------EASLEHEEGKILRAQ-LEFN 1568
Cdd:TIGR02169 505 RVRGGRAVEEVLKASIQGVHGT--VAQLGSVGE-RYATAIEVAagnrlnnvvveddavakEAIELLKRRKAGRATfLPLN 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1569 QIKAE--------------IERKLAEKDEEMEQAKRNHLR---MVDSLQT-----------SLDAE-----------TRS 1609
Cdd:TIGR02169 582 KMRDErrdlsilsedgvigFAVDLVEFDPKYEPAFKYVFGdtlVVEDIEAarrlmgkyrmvTLEGElfeksgamtggSRA 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1610 RNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEE 1689
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1690 LRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLtqLQTEVEEAVQECRNAEEKAKKAITDAAMMAE 1769
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1770 ELKKEQDTSAHLERMKKNMEQTIKDLQHRLDE-AEQIALKGGKK-----QLQKLEARVRELENELEAEQKRNAESVKGMR 1843
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiEKEIENLNGKKeeleeELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255918225 1844 KSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSkFRKVQHELDEAEER 1911
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1312-1931 |
3.74e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.17 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1312 QQMEDLKRQ---------LEEEGKAKNALAHALQSsrhdcDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYEtdai 1382
Cdd:COG1196 200 RQLEPLERQaekaeryreLKEELKELEAELLLLKL-----RELEAELEELEAELEELEAELEELEAELAELEAELE---- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1383 qrteELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKY 1462
Cdd:COG1196 271 ----ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1463 EESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLEL 1542
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1543 QSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRnhlrmvdslqtsLDAETRSRNEALRVKKKMEG 1622
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL------------LEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1623 DLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHAnddlkenIAIVERRNNLLQaeleelRAVVEQTERSRK 1702
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE-------AALEAALAAALQ------NIVVEDDEVAAA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1703 LAEQELIETSERVQLLHSqntSLINQKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLE 1782
Cdd:COG1196 562 AIEYLKAAKAGRATFLPL---DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1783 RMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVkgmRKSERRIKELTYQTEEDKKN 1862
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL---EEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1863 LMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSkfrKVQHELDEAEERADIAESQVNKLRAKSRDIGA 1931
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLE---EEALEELPEPPDLEELERELERLEREIEALGP 781
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
951-1862 |
5.11e-21 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 100.91 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 951 ELKKDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQAL--DDLQAEEDKV--------- 1019
Cdd:TIGR02169 154 ERRKIIDEIA-GVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYegyellkek 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1020 NTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDL-ENDKLQLEEKLKKKEFDISQQNSKIED 1098
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1099 EQALALQLQKKlkenqarieeleeeleaertaRAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRR 1178
Cdd:TIGR02169 313 KERELEDAEER---------------------LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1179 DLEEAtlqhEATAAALRKKHADSVAEL---GEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVS---- 1251
Cdd:TIGR02169 372 ELEEV----DKEFAETRDELKDYREKLeklKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKedka 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1252 ---RTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLE------ 1322
Cdd:TIGR02169 448 leiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtv 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1323 -EEGKAKNALAHALqssrhdcdllreqyeeEMEAKAELQRVLSKaNSEVAQWRTKYETD------------AIQRTEELE 1389
Cdd:TIGR02169 528 aQLGSVGERYATAI----------------EVAAGNRLNNVVVE-DDAVAKEAIELLKRrkagratflplnKMRDERRDL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1390 EAKKK-----LAQRLQDAEEAVEAVNAKC-------SSLEKTKhRLQNEIEDLMVD---VERSNAAAAALDKKQRnfdki 1454
Cdd:TIGR02169 591 SILSEdgvigFAVDLVEFDPKYEPAFKYVfgdtlvvEDIEAAR-RLMGKYRMVTLEgelFEKSGAMTGGSRAPRG----- 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1455 laewkqkyeeSQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEK---- 1530
Cdd:TIGR02169 665 ----------GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeek 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1531 ---IRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRMVDslqtsldaET 1607
Cdd:TIGR02169 735 lkeRLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE--------EE 806
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1608 RSRNEAlrVKKKMEGDLNEmeiqLSQANRIASEAQKHLKNSQahlkdtqlqlddavhanDDLKENIAIVERRNNLLQAEL 1687
Cdd:TIGR02169 807 VSRIEA--RLREIEQKLNR----LTLEKEYLEKEIQELQEQR-----------------IDLKEQIKSIEKEIENLNGKK 863
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1688 EELRAVVEQTERSRKLAEQELIEtservqlLHSQNTSLINQKKKMESDLTQLQTEVEEAvqECRNAEEKAKKAItdaamM 1767
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGD-------LKKERDELEAQLRELERKIEELEAQIEKK--RKRLSELKAKLEA-----L 929
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1768 AEELKkeqdtsaHLERMKKNMEQtikdlqhrlDEAEQIALKGGKKQLQKLEARVRELE-------NELEAEQKRNAESVK 1840
Cdd:TIGR02169 930 EEELS-------EIEDPKGEDEE---------IPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKE 993
|
970 980
....*....|....*....|....*
gi 255918225 1841 GMRK--SERR-IKELTYQTEEDKKN 1862
Cdd:TIGR02169 994 KRAKleEERKaILERIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1202-1830 |
8.75e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.01 E-value: 8.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1202 VAELGEQIDNLQRVKQKLEKEKsEFKLELDdvtsnmeqIIKAKANLEKVsRTLEDQANEYRVKLEEAQRSLNDFTTQRAK 1281
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYR-ELKEELK--------ELEAELLLLKL-RELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1282 LQTENGELARQLEEKEalisqltrgklsytqqmEDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEAKAELQR 1361
Cdd:COG1196 265 LEAELEELRLELEELE-----------------LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1362 VLSKansevaqwrtkyETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAA 1441
Cdd:COG1196 328 LEEE------------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1442 AALDKKQRNFDKILAEWKQKyeesqseLESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEG 1521
Cdd:COG1196 396 AELAAQLEELEEAEEALLER-------LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1522 GKNVHELEKIRKQLEVEKLELQS---ALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRMVDS 1598
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAArllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1599 LQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQA-HLKDTQLQLDDAVHANDdlkENIAIVE 1677
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAvDLVASDLREADARYYVL---GDTLLGR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1678 RRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAEEKA 1757
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1758 KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEA 1830
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
208-708 |
2.96e-20 |
|
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: 98.28 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 208 ENPNANKGTleDQIIQANPALEAFGNAKTVRNDNSSRFGKF--IRIHFGATG---KLASADIETYLLEKSRVIFQL---- 278
Cdd:cd14894 238 KNPHAAKKL--SIVLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgres 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 279 --KAERNYHIFYQILSNKKPELLDMLLVTNNPYD------YAFVSQGEVSVASIDDSEELLATD--------SAFDVLSF 342
Cdd:cd14894 316 gdQNELNFHILYAMVAGVNAFPFMRLLAKELHLDgidcsaLTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNV 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 343 TAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGT---EDADKSAYLMGLNSADLLKGLCHPR---VKVGNEYVTKGQ 416
Cdd:cd14894 396 SPDEQKTIFKVLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 417 SVQQVYYSIGALAKSVYEKMFNWMV------TRINATLETKQPRQY-----------FIGVLDIAGFEIFDFNSFEQLCI 479
Cdd:cd14894 476 EKGQVNHVRDTLARLLYQLAFNYVVfvmneaTKMSALSTDGNKHQMdsnasapeavsLLKIVDVFGFEDLTHNSLDQLCI 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 480 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEfidfgmdlQACIDLIEKPMGIMSILEEECMFPKASDMT----------F 549
Cdd:cd14894 556 NYLSEKLYAREEQVIAVAYSSRPHLTARDSE--------KDVLFIYEHPLGVFASLEELTILHQSENMNaqqeekrnklF 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 550 KAKLYDNHlgkSNNFQKPRNVKGKQEAH---------FSLVHYAGTVDYNIMGWLEKNKDPLNETV-VGLYQKSSLKL-- 617
Cdd:cd14894 628 VRNIYDRN---SSRLPEPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLlVGLKTSNSSHFcr 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 618 MATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRC 697
Cdd:cd14894 705 MLNESSQLGWSPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRS 784
|
570
....*....|.
gi 255918225 698 NGVLEGIRICR 708
Cdd:cd14894 785 QRLIRQMEICR 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
919-1795 |
1.26e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 96.29 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 919 AKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKdIDDLELTLAKVE-----KEKHATENKVKNLTEEMAGLDEIIAK 993
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 994 LTKEKKALQEAHQQALDDLQAEEDKVNTLTKSK-VKLEQQVDDLEGSLEQekkvrmdlerakrkLEGDLKLTQESIMDLE 1072
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAEIAS--------------LERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1073 NDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERL 1152
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1153 EEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHAdsvaelgeqidnlqrvkqKLEKEKSEFKLELDD 1232
Cdd:TIGR02169 402 NEL-----------KRELDRLQEELQRLSEELADLNAAIAGIEAKIN------------------ELEEEKEDKALEIKK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1233 VTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEA-------LISQLTR 1305
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1306 GKLSYTQQMEDLKRQ------LEEEGKAKNA--LAHALQSSRHDCDLLReqyeeEMEAKAELQRVLSKANSevaqwrTKY 1377
Cdd:TIGR02169 533 VGERYATAIEVAAGNrlnnvvVEDDAVAKEAieLLKRRKAGRATFLPLN-----KMRDERRDLSILSEDGV------IGF 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1378 ETDAIQRTEELEEAkkkLAQRLQDaeeaveavNAKCSSLEKTKhRLQNEIEDLMVD---VERSNAAAAALDKKQRnfdki 1454
Cdd:TIGR02169 602 AVDLVEFDPKYEPA---FKYVFGD--------TLVVEDIEAAR-RLMGKYRMVTLEgelFEKSGAMTGGSRAPRG----- 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1455 laewkqkyeeSQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEK---- 1530
Cdd:TIGR02169 665 ----------GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeek 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1531 ---IRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRMVDSLQTSLDAET 1607
Cdd:TIGR02169 735 lkeRLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARL 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1608 RSRNEALRvKKKMEGDLNEMEIQLSQANRIASEAQK-----HLKNSQAHLKDTQLQLDDAVHANDDLKENIAIVERRNNL 1682
Cdd:TIGR02169 815 REIEQKLN-RLTLEKEYLEKEIQELQEQRIDLKEQIksiekEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1683 LQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMES------DLTQLQTEVEEAVQECRNAEEK 1756
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelSLEDVQAELQRVEEEIRALEPV 973
|
890 900 910
....*....|....*....|....*....|....*....
gi 255918225 1757 AKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDL 1795
Cdd:TIGR02169 974 NMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
843-1591 |
1.80e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 96.36 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 843 KSAETEKEMANMKEEFGRVKDALEKSEARRKElEEKMVSLLQEKND---LQLQVQAEQDNLNDAEERCDQLIK------- 912
Cdd:PTZ00121 1118 EEAKKKAEDARKAEEARKAEDARKAEEARKAE-DAKRVEIARKAEDarkAEEARKAEDAKKAEAARKAEEVRKaeelrka 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 913 ---NKIQlEAKVKEMTERLED----EEEMNAELTAK---KRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTE 982
Cdd:PTZ00121 1197 edaRKAE-AARKAEEERKAEEarkaEDAKKAEAVKKaeeAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 983 EMAGLDEII----------AKLTKEKKALQEAHQQALDDLQAEEDKVNT------LTKSKVKLEQQVDDLEGSLEQEKKV 1046
Cdd:PTZ00121 1276 EARKADELKkaeekkkadeAKKAEEKKKADEAKKKAEEAKKADEAKKKAeeakkkADAAKKKAEEAKKAAEAAKAEAEAA 1355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1047 RMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFdisqqNSKIEDEQALALQLQKKLKENQariEELEEELEA 1126
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA-----KKKAEEDKKKADELKKAAAAKK---KADEAKKKA 1427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1127 ERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEfqKMRRDLEEATLQHEATAAALR-KKHADSVAEL 1205
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD--EAKKKAEEAKKADEAKKKAEEaKKKADEAKKA 1505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1206 GEQIDNLQRVKQKLEKEKSEfKLELDDVTSNMEQIIKA--KANLEKVSRTLEDQANEYRVKLEEAQRSlndftTQRAKLQ 1283
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKA-----EEDKNMA 1579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1284 TENGELARQLEEKEaLISQLTRGKLSYTQQMEDLKRqlEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEAKAELQRVL 1363
Cdd:PTZ00121 1580 LRKAEEAKKAEEAR-IEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1364 SKANSEVAQWRTKYETDAiQRTEEL----EEAKKKLAQRLQDAEEA--VEAVNAKCSSLEKTKHRLQNEIEDLMVDVERS 1437
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDK-KKAEEAkkaeEDEKKAAEALKKEAEEAkkAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1438 naaaaaldKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAY--EESLEHLETFKRENKNLQEEISDLT 1515
Cdd:PTZ00121 1736 --------KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1516 EQLGEGGKNVHELEKIRKQLEVEKLE-----LQSALEEAEASLEH------EEGKILRAQLEFNQIKAEIErklaEKDEE 1584
Cdd:PTZ00121 1808 ANIIEGGKEGNLVINDSKEMEDSAIKevadsKNMQLEEADAFEKHkfnknnENGEDGNKEADFNKEKDLKE----DDEEE 1883
|
....*..
gi 255918225 1585 MEQAKRN 1591
Cdd:PTZ00121 1884 IEEADEI 1890
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
843-1728 |
7.41e-19 |
|
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: 93.70 E-value: 7.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 843 KSAETEKEMANMKEEFGRVKDALEKS----EARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLE 918
Cdd:pfam01576 353 KHTQALEELTEQLEQAKRNKANLEKAkqalESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 919 AKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEiiakltkek 998
Cdd:pfam01576 433 EKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQE--------- 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 999 kalqeahqqaldDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEgdlkltqesiMDLENDKLQL 1078
Cdd:pfam01576 504 ------------QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQ----------RELEALTQQL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1079 EEKLKKKEfdisqqnskiedeqalalqlqkklkenqarieeleeeleaertaraKVEKLRSDLSRELEEISERLEEagga 1158
Cdd:pfam01576 562 EEKAAAYD----------------------------------------------KLEKTKNRLQQELDDLLVDLDH---- 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1159 tSVQIEMN-KKREAEFQKMRRDLEEATLQH----EATAAALRKKHADSVAeLGEQIDNLQRVKQKLEKEKSEFKLELDDV 1233
Cdd:pfam01576 592 -QRQLVSNlEKKQKKFDQMLAEEKAISARYaeerDRAEAEAREKETRALS-LARALEEALEAKEELERTNKQLRAEMEDL 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1234 TSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNdfTTQRAKLQTEngelarqleekealisqltrgklsytQQ 1313
Cdd:pfam01576 670 VSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQ--ATEDAKLRLE--------------------------VN 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1314 MEDLKRQLEEEGKAKNalahalqssrhdcdllreqyeeemEAKAELQRVLSKansEVAQWRTKYETDAIQRTEELeEAKK 1393
Cdd:pfam01576 722 MQALKAQFERDLQARD------------------------EQGEEKRRQLVK---QVRELEAELEDERKQRAQAV-AAKK 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1394 KLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAaaldkkqrnfDKILAEWKQkyeesqselesSQ 1473
Cdd:pfam01576 774 KLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASR----------DEILAQSKE-----------SE 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1474 KEARSLSTELFKLKnayeeslEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASL 1553
Cdd:pfam01576 833 KKLKNLEAELLQLQ-------EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNT 905
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1554 EHEEGKILRAQLEFNQIKAEI--ERKLAEKDEEMEQAKRNHLRMVDSLQTSLDAETRSRNEALrvKKKMEGDLNEMEIQL 1631
Cdd:pfam01576 906 ELLNDRLRKSTLQVEQLTTELaaERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSS--IAALEAKIAQLEEQL 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1632 SQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIET 1711
Cdd:pfam01576 984 EQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDA 1063
|
890
....*....|....*..
gi 255918225 1712 SERVQLLHSQNTSLINQ 1728
Cdd:pfam01576 1064 TESNESMNREVSTLKSK 1080
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1214-1936 |
4.37e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 91.74 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1214 RVKQKLEKEKSEFKLELDDVTSNMEQIIK---AKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTE--NGE 1288
Cdd:PTZ00121 1088 RADEATEEAFGKAEEAKKTETGKAEEARKaeeAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDarKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1289 LARQLEEK---EALISQLTRGKLSYTQQMEDLK-----RQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEAK-AEL 1359
Cdd:PTZ00121 1168 EARKAEDAkkaEAARKAEEVRKAEELRKAEDARkaeaaRKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkAEE 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1360 QRvlskANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDlmvdversNA 1439
Cdd:PTZ00121 1248 ER----NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE--------AK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1440 AAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELfklkNAYEESLEHLETFKRENKNLQEEISDLTEQlg 1519
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA----EAAEEKAEAAEKKKEEAKKKADAAKKKAEE-- 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1520 eggknVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEfnqiKAEIERKLAEKDEEMEQAKRNHLRMVDSL 1599
Cdd:PTZ00121 1390 -----KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK----KADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1600 QTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKhlkNSQAHLKDTQLQLDDAVHANDDLK---ENIAIV 1676
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK---AAEAKKKADEAKKAEEAKKADEAKkaeEAKKAD 1537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1677 ERRNNLLQAELEELRAV--VEQTERSRKlAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAE 1754
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAeeLKKAEEKKK-AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1755 EKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGG--KKQLQKLEARVRELENElEAEQ 1832
Cdd:PTZ00121 1617 EAKIKA--------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeAKKAEEDKKKAEEAKKA-EEDE 1687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1833 KRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAE---EQANTNLSKFRKVQHELDEAE 1909
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEE 1767
|
730 740 750
....*....|....*....|....*....|....*
gi 255918225 1910 ERAD--------IAESQVNKLRAKSRDIGAKKMHD 1936
Cdd:PTZ00121 1768 KKAEeirkekeaVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
832-1513 |
7.12e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.97 E-value: 7.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 832 MKLYFKIKPLLKSAETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDlQLQVQAEQdnlndAEERCDQLi 911
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEE-----AKKKADAA- 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 912 KNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKL-EDECSELKKDIDDLEltlAKVEKEKHATENKVKnlTEEMAGLDEI 990
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEAKKKADAAK---KKAEEKKKADEAKKK--AEEDKKKADE 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 991 IAKLTKEKKALQEAHQQALDDLQAEEdkvntlTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGD-LKLTQESIM 1069
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADE------AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAEEAK 1483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1070 DLENDKLQLEEKLKKKEfdisqQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEIS 1149
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKAD-----EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1150 ERLEEAggatsvQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEfkle 1229
Cdd:PTZ00121 1559 KAEEKK------KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA---- 1628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1230 lDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRslndfttqRAKLQTENGELARQLEEKEALISQLTRGKLS 1309
Cdd:PTZ00121 1629 -EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK--------KAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1310 YTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEmEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEEL- 1388
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED-KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKe 1778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1389 ----EEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKilAEWKQKYEE 1464
Cdd:PTZ00121 1779 avieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEAD--AFEKHKFNK 1856
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 255918225 1465 SQSELESSQKEARSlSTELFKLKNAYEESLEHLETFKRENKNLQEEISD 1513
Cdd:PTZ00121 1857 NNENGEDGNKEADF-NKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
856-1855 |
2.55e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 89.02 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 856 EEFGRVKDALEKSEARRKELEEKMVSLLQEK-NDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMTERLEDEEE- 933
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLRNQLQNTvHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEa 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 934 ------------------MNAELTAKKRKLEDECSELKKDIDDLEltlAKVEKEKHATENKVKNLTEEMAG-LDEIIAKL 994
Cdd:pfam15921 200 sgkkiyehdsmstmhfrsLGSAISKILRELDTEISYLKGRIFPVE---DQLEALKSESQNKIELLLQQHQDrIEQLISEH 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 995 TKEKKALQE----AHQQAlDDLQAEEDKVNTLTKSKVKL-EQQVDDLEGSLEQekkVRMDLERAKRKLEGDLKLTQESIM 1069
Cdd:pfam15921 277 EVEITGLTEkassARSQA-NSIQSQLEIIQEQARNQNSMyMRQLSDLESTVSQ---LRSELREAKRMYEDKIEELEKQLV 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1070 dLENDKLQlEEKLKKKEFdiSQQNSKIEDeqalalQLQKKLkenqarieeleeeleaertarAKVEKLRSDLSRELEEiS 1149
Cdd:pfam15921 353 -LANSELT-EARTERDQF--SQESGNLDD------QLQKLL---------------------ADLHKREKELSLEKEQ-N 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1150 ERLEEAGGATSVQIEmnkkreaefqKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKeksefkle 1229
Cdd:pfam15921 401 KRLWDRDTGNSITID----------HLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEK-------- 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1230 lddVTSNMEQIIKAKANLEKVSRTLEDQaneyRVKLEEAQRSLNDFTtqrAKLQtengELARQLEEKEALISQLTRGKLS 1309
Cdd:pfam15921 463 ---VSSLTAQLESTKEMLRKVVEELTAK----KMTLESSERTVSDLT---ASLQ----EKERAIEATNAEITKLRSRVDL 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1310 YTQQMEDLKRQLEEEGKAKNAL-AHALQSSRHD--CDLLREQYEEEMEAKAELQRVLSKANSEVAQwrtkYETDAIQRTE 1386
Cdd:pfam15921 529 KLQELQHLKNEGDHLRNVQTECeALKLQMAEKDkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ----LEKEINDRRL 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1387 ELEEAK----------KKLAQRLQDAE-EAVEAVNAKCSSLEKTKHrLQNEIEDLMVDVERSNaaaAALDKKQRNFDKIL 1455
Cdd:pfam15921 605 ELQEFKilkdkkdakiRELEARVSDLElEKVKLVNAGSERLRAVKD-IKQERDQLLNEVKTSR---NELNSLSEDYEVLK 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1456 AEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEE-------------SLEHLETFKRENKN-LQEEISDLTEQLGEG 1521
Cdd:pfam15921 681 RNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdghamkvamGMQKQITAKRGQIDaLQSKIQFLEEAMTNA 760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1522 GKNVHELEKIRKQLEVEKLELQSALEEAEASLEheegkILRAQlefnqikaeiERKLAEKDEEMEQAKRNHlrmvdSLQT 1601
Cdd:pfam15921 761 NKEKHFLKEEKNKLSQELSTVATEKNKMAGELE-----VLRSQ----------ERRLKEKVANMEVALDKA-----SLQF 820
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1602 SLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNS---QAHLKDTQLQLDDAVHANDDLKENiAIVER 1678
Cdd:pfam15921 821 AECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKPRLLQPAsftRTHSNVPSSQSTASFLSHHSRKTN-ALKED 899
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1679 RNNLLQAELEELRAVVEQTE-----------------RSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQlqt 1741
Cdd:pfam15921 900 PTRDLKQLLQELRSVINEEPtvqlskaedkgrapslgALDDRVRDCIIESSLRSDICHSSSNSLQTEGSKSSETCSR--- 976
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1742 eveEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDL---------QHR----------LDEA 1802
Cdd:pfam15921 977 ---EPVLLHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSPKKSPVHSLLTSSaegsigsssQYRsaktihspdsVKDS 1053
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1803 EQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQ 1855
Cdd:pfam15921 1054 QSLPIETTGKTCRKLQNRLESLQTLVEDLQLKNQAMSSMIRNQEKRIQKVKDQ 1106
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
861-1427 |
3.91e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 88.17 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 861 VKDALEKSEARRKELEEKMVSllQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTa 940
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEE--KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 941 kkrkledecsELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEkKALQEAHQQALDDLQAEedkvn 1020
Cdd:PRK02224 255 ----------TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLDDADAEAVEARREE----- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1021 tltkskvkLEQQVDDLEGSLEQekkVRMDLERAKRKLEGdlklTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQ 1100
Cdd:PRK02224 319 --------LEDRDEELRDRLEE---CRVAAQAHNEEAES----LREDADDLEERAEELREEAAELESELEEAREAVEDRR 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1101 ALALQLQKKLKENQARIE-------ELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGG--------------AT 1159
Cdd:PRK02224 384 EEIEELEEEIEELRERFGdapvdlgNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEG 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1160 SVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKkhADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQ 1239
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER--AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1240 IIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELAR------QLEEKEALISQLtRGKLSYTQQ 1313
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaAIADAEDEIERL-REKREALAE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1314 MEDLKR-QLEEEGKAKNALAHALQSSRhdcdllreqYEEEMEAKAELQRVLSKANSEVAQWRTkyETDAIQRT------- 1385
Cdd:PRK02224 621 LNDERReRLAEKRERKRELEAEFDEAR---------IEEAREDKERAEEYLEQVEEKLDELRE--ERDDLQAEigavene 689
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 255918225 1386 -EELEEAKKKLAQrLQDAEEAVEAVNAKCSSLEKTKHRLQNEI 1427
Cdd:PRK02224 690 lEELEELRERREA-LENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1204-1933 |
1.04e-16 |
|
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: 86.77 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1204 ELGEQIDNLQRVKQKLEKEKSEFKleldDVTSNMEQIIKAKANLEKVSRT---LEDQANEYRVKLEEAQRSLNDFTtqra 1280
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELK----ELEKKHQQLCEEKNALQEQLQAeteLCAEAEEMRARLAARKQELEEIL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1281 klqtenGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKnalaHALQSSRHDCDLLREQYEEEMEAKAELQ 1360
Cdd:pfam01576 78 ------HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAAR----QKLQLEKVTTEAKIKKLEEDILLLEDQN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1361 RVLSKAnsevaqwrtkyetdaiqrteeleeaKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAA 1440
Cdd:pfam01576 148 SKLSKE-------------------------RKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1441 AAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGE 1520
Cdd:pfam01576 203 RQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLES 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1521 GGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRMVDSLQ 1600
Cdd:pfam01576 283 ERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1601 TSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKEniaiverRN 1680
Cdd:pfam01576 363 EQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAE-------KL 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1681 NLLQAELEELRAVVEQTE-RSRKLA------EQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNA 1753
Cdd:pfam01576 436 SKLQSELESVSSLLNEAEgKNIKLSkdvsslESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNV 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1754 EEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKggkkqLQKLEARVRELENELEAEQK 1833
Cdd:pfam01576 516 ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDK-----LEKTKNRLQQELDDLLVDLD 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1834 RNAESVKGMRKSERRIKELTyqtEEDKKNLMRLQDLVDKlqlkvkaykrqaeeAEEQANTNLSKFRKVQHELDEAEERAD 1913
Cdd:pfam01576 591 HQRQLVSNLEKKQKKFDQML---AEEKAISARYAEERDR--------------AEAEAREKETRALSLARALEEALEAKE 653
|
730 740
....*....|....*....|
gi 255918225 1914 IAESQVNKLRAKSRDIGAKK 1933
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSK 673
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
862-1575 |
2.31e-16 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 85.46 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 862 KDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLiKNKIQ-LEAKVKEMTERLEDEEEMNAELTA 940
Cdd:TIGR04523 25 KNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNS-NNKIKiLEQQIKDLNDKLKKNKDKINKLNS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 941 KKRKLEDECSELKKDIDDLELTLAKVEKEKHATE-------NKVKNLTEEMAGLDEIIAKLTKEKKALqeahqqalddlq 1013
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEEL------------ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1014 aeEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLErakrKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQN 1093
Cdd:TIGR04523 172 --ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1094 SKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEaggatsvqiEMNKKREAEF 1173
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ---------DWNKELKSEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1174 QKMRRDLEEATLQheataaalRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRT 1253
Cdd:TIGR04523 317 KNQEKKLEEIQNQ--------ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1254 LEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLtrgklsyTQQMEDLKRQLEEEGKAKNALAH 1333
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN-------NSEIKDLTNQDSVKELIIKNLDN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1334 ALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQDAEEAVEAVNAKC 1413
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL---------------KKLNEEKKELEEKVKDLTKKISSLKEKI 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1414 SSLEKTKHRLQNEIEDLMVDVER--SNAAAAALDKKQRNFDKILAEWKQKYEesqselessqkearslstelfKLKNAYE 1491
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQK---------------------SLKKKQE 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1492 ESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIK 1571
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEII 665
|
....
gi 255918225 1572 AEIE 1575
Cdd:TIGR04523 666 KKIK 669
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1011-1805 |
6.16e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.81 E-value: 6.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1011 DLQAEEDKVNTLTKS--KVKLEQQVDDLEGSLEQEKKVRMDLERAK--RKLEGDLKLTQ----ESIMDLENDKL-----Q 1077
Cdd:PTZ00121 1080 DFDAKEDNRADEATEeaFGKAEEAKKTETGKAEEARKAEEAKKKAEdaRKAEEARKAEDarkaEEARKAEDAKRveiarK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1078 LEEKLKKKEFDISQQNSKIED-----EQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERL 1152
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAarkaeEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1153 EEAggatsvqiemNKKREAEFQKMRRDLEEATLQHEATAAALRKKHAdsvAELGEQIDNLQRVKQKLEKEKSEFKLELDD 1232
Cdd:PTZ00121 1240 EEA----------KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE---ARKADELKKAEEKKKADEAKKAEEKKKADE 1306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1233 VTSNMEQIIKAKaNLEKVSRTLEDQANEYRVKLEEAQRSLN------DFTTQRAKLQTENGELARQLEEKEALISQLTRG 1306
Cdd:PTZ00121 1307 AKKKAEEAKKAD-EAKKKAEEAKKKADAAKKKAEEAKKAAEaakaeaEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1307 KLSYTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYE----EEMEAKAELQRVLSKANSEVAQWR----TKYE 1378
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkkkaDEAKKKAEEAKKADEAKKKAEEAKkaeeAKKK 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1379 TDAIQRTEEL----------EEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQ 1448
Cdd:PTZ00121 1466 AEEAKKADEAkkkaeeakkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1449 RNFDKILAEWKQKYEESQSELESSQKEARSLSTELFK---LKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNV 1525
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1526 HELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEfnQIKAEIERKLAE---KDEEMEQAKRNHLRMVDSLQTS 1602
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE--AKKAEEDKKKAEeakKAEEDEKKAAEALKKEAEEAKK 1703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1603 LDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASE----AQKHLKNSQAHLKDTQLQLDDAVHANDDLKENIAIVER 1678
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEdkkkAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1679 RnnlLQAELEELRAVVEQTERSRKlaeqeliETSERVQLLHSQNTSLINQKKKMESdltqlqTEVEEAVQECRNAEEKAK 1758
Cdd:PTZ00121 1784 E---LDEEDEKRRMEVDKKIKDIF-------DNFANIIEGGKEGNLVINDSKEMED------SAIKEVADSKNMQLEEAD 1847
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 255918225 1759 KAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRlDEAEQI 1805
Cdd:PTZ00121 1848 AFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA-DEIEKI 1893
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
967-1823 |
2.03e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 82.71 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 967 EKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQAlddlQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKV 1046
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE----KLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1047 RMDLERAKRKLEGDLKLTQESIMDLEN----------DKLQLEEKLKKKEFDISQQNSKIEDEQALALQ-----LQKKLK 1111
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEkekklqeeelKLLAKEEEELKSELLKLERRKVDDEEKLKESEkekkkAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1112 ENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEatlqhEATA 1191
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE-----EEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1192 AALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKAN-LEKVSRTLEDQANEYRVKLEEAQR 1270
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLkDELELKKSEDLLKETQLVKLQEQL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1271 SLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAhalqssrhdCDLLREQYE 1350
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTA---------VIVEVSATA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1351 EEMEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRlqnEIEDL 1430
Cdd:pfam02463 558 DEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGIL---KDTEL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1431 MVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSlstELFKLKNAYEESLEHLETFKRENKNLQEE 1510
Cdd:pfam02463 635 TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQ---EKAESELAKEEILRRQLEIKKKEQREKEE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1511 ISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSA---LEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQ 1587
Cdd:pfam02463 712 LKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDeeeEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1588 AKRNHLRMVDSLqtsldaetrsRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLqldDAVHAND 1667
Cdd:pfam02463 792 KEEKLKAQEEEL----------RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL---AEEELER 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1668 DLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNtSLINQKKKMESDLTQLQTEVEEAV 1747
Cdd:pfam02463 859 LEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE-EKENEIEERIKEEAEILLKYEEEP 937
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1748 QECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM---EQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRE 1823
Cdd:pfam02463 938 EELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMaieEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
899-1536 |
2.19e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.42 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 899 NLNDAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELT---LAKVEKEKHATEN 975
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 976 KVKNLTEEMAGLDEIIAKLTKEKKALqeahqqalddlqaeEDKVNTLTKSKVKLEQQVdDLEGSLEQEKKVRMDLERAKR 1055
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEEL--------------EEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1056 KLEGDLKLTQESIMDLENDKLQLEEkLKKKEFDISQQNSKIEdEQALALQLQKKLKENQARIEELEEELEAERTARA--K 1133
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEE-LKKKLKELEKRLEELE-ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEleE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1134 VEKLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKH-ADSVAELGEQIDNL 1212
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGEL-----------KKEIKELKKAIEELKKAKGKCPVCGRELTEEHrKELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1213 QRVKQKLEKEKSEFK---LELDDVTSNMEQIIKAKANLEKVsRTLEDQANEYRV-KLEEAQRSLNDFTTQRAKLQTENGE 1288
Cdd:PRK03918 465 EKELKEIEEKERKLRkelRELEKVLKKESELIKLKELAEQL-KELEEKLKKYNLeELEKKAEEYEKLKEKLIKLKGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1289 LARQLEEKEALISQLTrgklsytqQMEDLKRQLEEEGKaknalahalqssrhdcDLLREQYEEEMEAKAELQRvlskans 1368
Cdd:PRK03918 544 LKKELEKLEELKKKLA--------ELEKKLDELEEELA----------------ELLKELEELGFESVEELEE------- 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1369 evaqwrtkyetdaiqRTEELEEAKKKLaqrlqdaeeaVEAVNAkcsslEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQ 1448
Cdd:PRK03918 593 ---------------RLKELEPFYNEY----------LELKDA-----EKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1449 RNFDKILAEWKQKYeesqselesSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHEL 1528
Cdd:PRK03918 643 EELRKELEELEKKY---------SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
....*...
gi 255918225 1529 EKIRKQLE 1536
Cdd:PRK03918 714 EKLEKALE 721
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1610-1925 |
2.63e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1610 RNEALRVKKKMEGDLN-------EMEIQLSQANRIASEAQKHLKNsQAHLKDTQLQLddAVHANDDLKENIAIVERRNNL 1682
Cdd:COG1196 174 KEEAERKLEATEENLErledilgELERQLEPLERQAEKAERYREL-KEELKELEAEL--LLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1683 LQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAIT 1762
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1763 DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKgM 1842
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA-E 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1843 RKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKL 1922
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
...
gi 255918225 1923 RAK 1925
Cdd:COG1196 490 AAR 492
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
842-1403 |
8.17e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 80.55 E-value: 8.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 842 LKSAETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNlndAEERCDQLIKNKIQLEAKV 921
Cdd:pfam15921 250 LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 922 kemterledeEEMNAELTAKKRKLEDECSELKKD--IDDLELTLAKVEKEKHATENkvKNLTEEmagLDEIIAKLTKEKK 999
Cdd:pfam15921 327 ----------SQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQ---LQKLLADLHKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1000 ALQEAHQQ--------------------ALDDLQAEEDKVNTLTKS-----KVKLEQQVDDLEG---SLEQEKKVRMDLE 1051
Cdd:pfam15921 392 ELSLEKEQnkrlwdrdtgnsitidhlrrELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneSLEKVSSLTAQLE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1052 RAKRKLEGDLKLTQESIMDLENDKL---QLEEKLKKKEFDISQQNSKIEDEQA---LALQLQKKLKENQARIEELEEELE 1125
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLESSERtvsDLTASLQEKERAIEATNAEITKLRSrvdLKLQELQHLKNEGDHLRNVQTECE 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1126 AERTARAKVEKLRSDLSRELEEISERLEEAG---GATSV-----QIEMNKKR-EAEFQKMRRDLEEATLQH-EATAAALR 1195
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGrtaGAMQVekaqlEKEINDRRlELQEFKILKDKKDAKIRElEARVSDLE 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1196 KKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDF 1275
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1276 TTQRAKLQTENGE-------LARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSSRH-------D 1341
Cdd:pfam15921 712 RNTLKSMEGSDGHamkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATeknkmagE 791
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255918225 1342 CDLLREQYEEEMEAKAELQRVLSKANSEVAQWRtkyetDAIQRTEElEEAKKKLAQRLQDAE 1403
Cdd:pfam15921 792 LEVLRSQERRLKEKVANMEVALDKASLQFAECQ-----DIIQRQEQ-ESVRLKLQHTLDVKE 847
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
845-1583 |
1.30e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 80.02 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 845 AETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEM 924
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 925 TERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEA 1004
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1005 HQQALDDLQA--EEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLE----NDKLQL 1078
Cdd:pfam02463 435 EEESIELKQGklTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKarsgLKVLLA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1079 EEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGA 1158
Cdd:pfam02463 515 LIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSI 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1159 TSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSefKLELDDVTSNME 1238
Cdd:pfam02463 595 AVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAE--KSEVKASLSELT 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1239 QIIKAKANLEKVSRTLEDQANEY-RVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDL 1317
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILrRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1318 KRQLEEEGKAKNALAHALQSSRHDcDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQ 1397
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKEL-AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIK 831
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1398 RLQDAEEAVEavnakcsSLEKTKHRLQNEIEDLMVDVErsnaAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEAR 1477
Cdd:pfam02463 832 EEELEELALE-------LKEEQKLEKLAEEELERLEEE----ITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKK 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1478 SLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEE 1557
Cdd:pfam02463 901 ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAI 980
|
730 740
....*....|....*....|....*.
gi 255918225 1558 GKILRAQLEFNQIKAEIERKLAEKDE 1583
Cdd:pfam02463 981 EEFEEKEERYNKDELEKERLEEEKKK 1006
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
32-76 |
2.79e-14 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 68.61 E-value: 2.79e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 255918225 32 DIRTECFVPDDKEEYVKAKVVSREGGKVTAETENGKTVTIKEDQV 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1238-1929 |
2.93e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.96 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1238 EQIIKAKANLEKVSRTLE------DQANEYRVKLEEAQRSLNDFTTQRAKLQ-TENGELARQLEEKEALISQLTRGKLSY 1310
Cdd:TIGR02169 170 RKKEKALEELEEVEENIErldliiDEKRQQLERLRREREKAERYQALLKEKReYEGYELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1311 TQQMEDLKRQLEEEGKAKNALAHalqssrhdcdlLREQYEEEMEAKAElqrvlskanSEVAQWRTKYETDAIQRtEELEE 1390
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQ-----------LLEELNKKIKDLGE---------EEQLRVKEKIGELEAEI-ASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1391 AKKKLAQRLQDAEEAVEavnakcsSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKkqrnfdkILAEWKQKYEESQSELE 1470
Cdd:TIGR02169 309 SIAEKERELEDAEERLA-------KLEAEIDKLLAEIEELEREIEEERKRRDKLTE-------EYAELKEELEDLRAELE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1471 SSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEggknvheLEKIRKQLEVEKLELQSALEEAE 1550
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD-------LNAAIAGIEAKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1551 ASLEHEEGKILRAQLEFNQIKAEIERKLAEKD---EEMEQAKRNHLRMVDSLQTSLDAETRSRNEALRVKKKMEG----- 1622
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDrveKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGvhgtv 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1623 -DLNEME------IQLSQANR----------IASEAQKHLKNSQA---------HLKDTQLQLDDAVHAN---------- 1666
Cdd:TIGR02169 528 aQLGSVGeryataIEVAAGNRlnnvvveddaVAKEAIELLKRRKAgratflplnKMRDERRDLSILSEDGvigfavdlve 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1667 -DDLKENIAIVERRNNLLQAELEELRAVVEQ----------------------TERSRKL----AEQELIETSERVQLLH 1719
Cdd:TIGR02169 608 fDPKYEPAFKYVFGDTLVVEDIEAARRLMGKyrmvtlegelfeksgamtggsrAPRGGILfsrsEPAELQRLRERLEGLK 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1720 SQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRL 1799
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1800 DEAEQiALKGGKKQLQKLEAR-----VRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQ 1874
Cdd:TIGR02169 768 EELEE-DLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 255918225 1875 LKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1929
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
839-1387 |
3.35e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 839 KPLLKSAETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQlqvqAEQDNLNDAEERCDQLIKNKIQLE 918
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 919 AKVKEMTERLEdeeemnaELTAKKRKLED-------------ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMA 985
Cdd:PRK03918 259 EKIRELEERIE-------ELKKEIEELEEkvkelkelkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 986 GLDEIIAKLTKEKKALQEahqqALDDLQAEEDKVNTLTKSKVKLEQ--QVDDLEGSLEQEKKVRM--DLERAKRKLEGDL 1061
Cdd:PRK03918 332 ELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEAKAKKEEleRLKKRLTGLTPEKLEKEleELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1062 KLTQESIMDLENDKLQLE---EKLKKKEF-------------------DISQQNSKIEDEQALALQLQKKLKENQARIEE 1119
Cdd:PRK03918 408 SKITARIGELKKEIKELKkaiEELKKAKGkcpvcgrelteehrkelleEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1120 LEEELEAERTARAKVEKLRS-----------DLSRELEEISERLEEAGGATSVQIEMNK--KREAEFQKMRRDLEEATLQ 1186
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKEleeklkkynleELEKKAEEYEKLKEKLIKLKGEIKSLKKelEKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1187 HEATAAALRKKHAD----SVAELGEQIDNLQRVKQK---LEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEdqan 1259
Cdd:PRK03918 568 LEEELAELLKELEElgfeSVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE---- 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1260 EYRVKLEEAQRSLNDftTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALaHALQSSR 1339
Cdd:PRK03918 644 ELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL-EKLEKAL 720
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1340 HDCDLLREQY-----EEEMEAKAELQRVLSKANSEVAQwrTKYETDAIQRTEE 1387
Cdd:PRK03918 721 ERVEELREKVkkykaLLKERALSKVGEIASEIFEELTE--GKYSGVRVKAEEN 771
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1055-1589 |
4.12e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 78.14 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1055 RKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIeeleeeleaertarakv 1134
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKI----------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1135 EKLRSDLSRELEEISERLEEaggatsvqieMNKKrEAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQR 1214
Cdd:TIGR04523 99 NKLNSDLSKINSEIKNDKEQ----------KNKL-EVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1215 VKQKLEKEKSEFKLELDDVTSNMEQI-------------IKAK-----------ANLEKVSRTLEDQANEYRVKLEEAQR 1270
Cdd:TIGR04523 167 QKEELENELNLLEKEKLNIQKNIDKIknkllklelllsnLKKKiqknkslesqiSELKKQNNQLKDNIEKKQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1271 SLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNA-----LAHALQSSRHDCDLL 1345
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1346 REQYEEEMEAKAELQRVLSKANSEvaqwRTKYETDAIQRTEELEEAKKK------------------------LAQRLQD 1401
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKE----LTNSESENSEKQRELEEKQNEieklkkenqsykqeiknlesqindLESKIQN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1402 AEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLST 1481
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1482 ELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHE--EGK 1559
Cdd:TIGR04523 483 NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKE 562
|
570 580 590
....*....|....*....|....*....|
gi 255918225 1560 ILRAQLEFNQIKAEIERKLAEKDEEMEQAK 1589
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1572-1931 |
5.30e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.19 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1572 AEIERKLAEKDEEMEQAKRNHLR---MVDSLQTSLDAETRSRNEALRV------KKKMEG-----DLNEMEIQLSQANRI 1637
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERYqallkeKREYEGyellkEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1638 ASEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKENI-AIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQ 1716
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1717 LLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSahlermkKNMEQTIKDLQ 1796
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL-------KDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1797 HRLDEAEQIALKGGKkQLQKLEARVRELENELEAEQKRNAESvkgmrksERRIKELTYQTEEDKKNLMRLQDLVDKLQLK 1876
Cdd:TIGR02169 399 REINELKRELDRLQE-ELQRLSEELADLNAAIAGIEAKINEL-------EEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 255918225 1877 VKAYKRQAEEAEEqantnlsKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGA 1931
Cdd:TIGR02169 471 LYDLKEEYDRVEK-------ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1293-1921 |
1.41e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1293 LEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAkNALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQ 1372
Cdd:PTZ00121 1026 IEKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKA-EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAK 1104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1373 wrtKYETDAIQRTEELEEAKKKL--------AQRLQDAEEAVEAVNAKCSSLEKTKHRLQN----EIEDLMVDVERSNAA 1440
Cdd:PTZ00121 1105 ---KTETGKAEEARKAEEAKKKAedarkaeeARKAEDARKAEEARKAEDAKRVEIARKAEDarkaEEARKAEDAKKAEAA 1181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1441 AAALDKKQ-----RNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLT 1515
Cdd:PTZ00121 1182 RKAEEVRKaeelrKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1516 EQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRM 1595
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA 1341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1596 VDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQlddavHANDDLKENIAI 1675
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK-----KKADELKKAAAA 1416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1676 VERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQllHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAEE 1755
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK--KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1756 KAKKAitDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEaRVRELENELEAEQKRN 1835
Cdd:PTZ00121 1495 AKKKA--DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKK 1571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1836 AESVKGM--RKSE-------RRIKELTYQTEEDKKnlMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKF----RKVQ 1902
Cdd:PTZ00121 1572 AEEDKNMalRKAEeakkaeeARIEEVMKLYEEEKK--MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKeaeeKKKA 1649
|
650
....*....|....*....
gi 255918225 1903 HELDEAEERADIAESQVNK 1921
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAK 1668
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1032-1640 |
1.44e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.26 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1032 QVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKkefdISQQNSKIEdeqalalQLQKKLK 1111
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLRE----INEISSELP-------ELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1112 ENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEeaggatsvQIEMNKKREAEFQKMRRDLEEAtlqheata 1191
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE--------RIEELKKEIEELEEKVKELKEL-------- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1192 aalrKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRvKLEEAQRS 1271
Cdd:PRK03918 289 ----KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE-ELEERHEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1272 LNDFTTQRAKLQTENGELA-RQLEEKEALISQLTRGKLSYTQQMEDL---KRQLEEEGKAKNALAHALQSSRHDCDL--- 1344
Cdd:PRK03918 364 YEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAKGKCPVcgr 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1345 ---------LREQYEEEM-----------EAKAELQRVLSKANSEVAQWRT--KYETDAIQRTEELEEAKKKLAQRLQDA 1402
Cdd:PRK03918 444 elteehrkeLLEEYTAELkriekelkeieEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELEKK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1403 EEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTE 1482
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNE 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1483 LFKLKNA---YEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKI-----RKQLEVEKLELQSALEEAEASLE 1554
Cdd:PRK03918 604 YLELKDAekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1555 HEEGKIlraqlefNQIKAEIErKLAEKDEEMEQAKRNhlrmVDSLQTSLDAETRSRNEALRVKKKMEgdlnemEIQLSQA 1634
Cdd:PRK03918 684 ELEKRR-------EEIKKTLE-KLKEELEEREKAKKE----LEKLEKALERVEELREKVKKYKALLK------ERALSKV 745
|
....*.
gi 255918225 1635 NRIASE 1640
Cdd:PRK03918 746 GEIASE 751
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1260-1842 |
2.77e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.46 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1260 EYRVKLEEAQRSLNDFttqRAKLQTENGELARQLEEKEA--LISQLTRGKLSYTQQMEDLKRQLEEEGKAKnalahalqS 1337
Cdd:PRK02224 166 EYRERASDARLGVERV---LSDQRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQAR--------E 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1338 SRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYET------DAIQRTEELEEAKKKLAQRLQDAEEAVEAVNA 1411
Cdd:PRK02224 235 TRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREElaeevrDLRERLEELEEERDDLLAEAGLDDADAEAVEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1412 KCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQkyeesqselessqkEARSLSTELfklknayE 1491
Cdd:PRK02224 315 RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE--------------EAAELESEL-------E 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1492 ESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIK 1571
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1572 -----------------AEIERKLAEKDEEMEQAKRNHLRMVDSLQTSLDA-ETRSRNEALRVKKKMEGDL-----NEME 1628
Cdd:PRK02224 454 cpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDLvEAEDRIERLEERREDLEELiaerrETIE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1629 IQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAvhanDDLKENIAIVERRNNLLQAELEELRAVVEQTERsRKLAEQEL 1708
Cdd:PRK02224 534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEA----EEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEI 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1709 IETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEA-VQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKN 1787
Cdd:PRK02224 609 ERLREKREALAELNDERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1788 MEQTIKDLQHRLDeaeqiALKGGKKQLQKLEARVRELEN---ELEAE-QKRNAESVKGM 1842
Cdd:PRK02224 689 ELEELEELRERRE-----ALENRVEALEALYDEAEELESmygDLRAElRQRNVETLERM 742
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1383-1910 |
3.34e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.10 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1383 QRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKhrlqNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEwKQKY 1462
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEE-LKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1463 EESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEveklEL 1542
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK----EL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1543 QSALEEAEASLE-HEEGKILRAQLEfnQIKAEIE----RKLAEKDEEMEQAK---RNHLRMVDSLQTSLDAETRSRNEAL 1614
Cdd:PRK03918 351 EKRLEELEERHElYEEAKAKKEELE--RLKKRLTgltpEKLEKELEELEKAKeeiEEEISKITARIGELKKEIKELKKAI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1615 RVKKKMEGD--LNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDavhanddlkeniaiverrnnlLQAELEELRA 1692
Cdd:PRK03918 429 EELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERK---------------------LRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1693 VVEQTERSRKLAEqelietservqllhsqntsLINQKKKMESDLTQLQTE-VEEAVQECRNAEEKAKKAITDAAMMAEEL 1771
Cdd:PRK03918 488 VLKKESELIKLKE-------------------LAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1772 KKEQD---TSAHLERMKKNMEQTIKDLQHRLDEA--------------------EQIALKGGKKQLQKLEARVRELENEL 1828
Cdd:PRK03918 549 EKLEElkkKLAELEKKLDELEEELAELLKELEELgfesveeleerlkelepfynEYLELKDAEKELEREEKELKKLEEEL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1829 EAEQKRNAESVKGMRKSERRIKELtyQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEA 1908
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEEL--EKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
..
gi 255918225 1909 EE 1910
Cdd:PRK03918 707 EK 708
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1486-1928 |
3.93e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 75.15 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1486 LKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNvHE--LEKIRKQLeveklelqSALEEAEASLEHEEGKIlrA 1563
Cdd:pfam15921 143 LRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLS-HEgvLQEIRSIL--------VDFEEASGKKIYEHDSM--S 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1564 QLEFNQIKAEIERKLAEKDEEMEQAKRNHLRMVDSLQTsLDAETRSRNEAL--RVKKKMEGDLNEMEIQLSQANRIASEA 1641
Cdd:pfam15921 212 TMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEA-LKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1642 QKHLKNSQAHLKDTQLQlddavhanddlkeniaiVERRNNLLQAELEELRAVVEQTE---RSRKLAEQELIETSERVQLL 1718
Cdd:pfam15921 291 RSQANSIQSQLEIIQEQ-----------------ARNQNSMYMRQLSDLESTVSQLRselREAKRMYEDKIEELEKQLVL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1719 HSqntslinqkkkmeSDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHR 1798
Cdd:pfam15921 354 AN-------------SELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1799 LDEAEQialkggkkQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVK 1878
Cdd:pfam15921 421 LDDRNM--------EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1879 AYKR----------QAEEAEEQANTNLSKFR--------KVQHELDEAEERADI-AESQVNKLRAKSRD 1928
Cdd:pfam15921 493 SSERtvsdltaslqEKERAIEATNAEITKLRsrvdlklqELQHLKNEGDHLRNVqTECEALKLQMAEKD 561
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1039-1929 |
9.28e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 73.93 E-value: 9.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1039 SLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKiEDEQALALQLQKKLKENQARIE 1118
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY-ENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1119 ELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGatsvQIEMNKKREA-EFQKMRRDLEEATLQHEATAAALRKK 1197
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLN----DLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1198 HADSVAELGE-----QIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSL 1272
Cdd:TIGR00606 342 KTELLVEQGRlqlqaDRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1273 NDFTTQRAKLQTENGELARQLEEKEALISQLT---RGKLSYTQQ----MEDLKRQLEEEGKAKNALAHALQSSRHDCDLL 1345
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLGRTIELKKEILEKKQeelKFVIKELQQlegsSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1346 REQYEEemEAKAELQRVLSKANSEVAQWRTKYETdaiqRTEELEEAKKKLaqrlqDAEEAVEAVNAKCSS---------- 1415
Cdd:TIGR00606 502 EVKSLQ--NEKADLDRKLRKLDQEMEQLNHHTTT----RTQMEMLTKDKM-----DKDEQIRKIKSRHSDeltsllgyfp 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1416 ----LEKTKHRLQNEI---EDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEES-------------QSELESSQKE 1475
Cdd:TIGR00606 571 nkkqLEDWLHSKSKEInqtRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgsqdeesdLERLKEEIEK 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1476 ARSLSTELFKLKNAYEESLEHLET------------FKREnKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQ 1543
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQLTDenqsccpvcqrvFQTE-AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEML 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1544 SALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLA--EKDEEMEQAKRNHLRMVDSLQTSLDAETRSRNEALRVKKKME 1621
Cdd:TIGR00606 730 GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNdiEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIA 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1622 GDLNEMeiQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRavvEQTERSR 1701
Cdd:TIGR00606 810 QQAAKL--QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIG---TNLQRRQ 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1702 KLAEQeLIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQecrNAEEKAKKAITDAAMMAEELKK-------- 1773
Cdd:TIGR00606 885 QFEEQ-LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS---SKETSNKKAQDKVNDIKEKVKNihgymkdi 960
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1774 EQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENELEAE--QKRNAESVKGMRKSERRIKE 1851
Cdd:TIGR00606 961 ENKIQDGKDDYLKQKETELNTVNAQLEECEK--------HQEKINEDMRLMRQDIDTQkiQERWLQDNLTLRKRENELKE 1032
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1852 L-----TYQTEEDKKNLMRLQDLVDKLQLKVKAYKR-------QAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQV 1919
Cdd:TIGR00606 1033 VeeelkQHLKEMGQMQVLQMKQEHQKLEENIDLIKRnhvlalgRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRT 1112
|
970
....*....|
gi 255918225 1920 NKLRAKSRDI 1929
Cdd:TIGR00606 1113 TELVNKDLDI 1122
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
942-1576 |
1.91e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 942 KRKLEDECSELKKDIDDLELTLAKVEKEKHATE--NKVKNLTEEMAGLDEIIAKLTKEKKALQ-EAHQQALDDLQAEEDK 1018
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1019 vntLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDlkltqeSIMDLENDKLQLEEKLKKKEFDISQQNSKIED 1098
Cdd:COG4913 300 ---LRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1099 EQALALQLQKKLKENQARIEELEEELEAER----TARAKVEKLRSDLSRELEEISERLEEaggatsvqIEMNKKR-EAEF 1173
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELealeEALAEAEAALRDLRRELRELEAEIAS--------LERRKSNiPARL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1174 QKMRRDLEEATLQHEA-------------------TAA--ALR---------KKHADSVAELGEQID-----NLQRVKQK 1218
Cdd:COG4913 443 LALRDALAEALGLDEAelpfvgelievrpeeerwrGAIerVLGgfaltllvpPEHYAAALRWVNRLHlrgrlVYERVRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1219 LEKEKSEF--------KLELDD--VTSNMEQIIKAKANLEKVsRTLEDQANEYR-------VKLEEAQRSLNDFTTQRAK 1281
Cdd:COG4913 523 LPDPERPRldpdslagKLDFKPhpFRAWLEAELGRRFDYVCV-DSPEELRRHPRaitragqVKGNGTRHEKDDRRRIRSR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1282 LQT--ENgelARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLlrEQYEEEMEAKAEL 1359
Cdd:COG4913 602 YVLgfDN---RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV--ASAEREIAELEAE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1360 QRVLSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVErsna 1439
Cdd:COG4913 677 LERLDASSDDL---------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE---- 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1440 AAAALDKKQRNFDkiLAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKnlqeeisDLTEQLG 1519
Cdd:COG4913 738 AAEDLARLELRAL--LEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWP-------AETADLD 808
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1520 EGGKNVHELEKIRKQLEVEKL-ELQSALEEAEASLEHEEGKILRAQL--EFNQIKAEIER 1576
Cdd:COG4913 809 ADLESLPEYLALLDRLEEDGLpEYEERFKELLNENSIEFVADLLSKLrrAIREIKERIDP 868
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1571-1935 |
2.30e-12 |
|
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: 72.78 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1571 KAEIERKLAEKDEEMEQAKRNhLRMVDSLQTSLDAETRSRNEALRVKKKME--------GDLNEMEIQLSQANRIASEAQ 1642
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDI-LNELERQLKSLERQAEKAERYKELKAELRelelallvLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1643 KHLKNSQAHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQN 1722
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1723 TSLINQKKKMESDLTQLQTEVEEavqecrnaeekakkaitdaamMAEELKKeqdtsahLERMKKNMEQTIKDLQHRLDEA 1802
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELES---------------------LEAELEE-------LEAELEELESRLEELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1803 EQiALKGGKKQLQKLEARVRELENELEAEQKRNAESVKgmRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKR 1882
Cdd:TIGR02168 385 RS-KVAQLELQIASLNNEIERLEARLERLEDRRERLQQ--EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEE 461
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1883 QAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKKMH 1935
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1310-1907 |
3.48e-12 |
|
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: 72.07 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1310 YTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVaqwrtkyeTDAIQRT-EEL 1388
Cdd:pfam15921 83 YSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL--------RNQLQNTvHEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1389 EEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHrlqnEIEDLMVDVERSNAaaaaldkkqrnfDKILAEWKQKYEESQSE 1468
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ----EIRSILVDFEEASG------------KKIYEHDSMSTMHFRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1469 LESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQE-------------------EISDLTEQLGEGGKNVH--- 1526
Cdd:pfam15921 219 GSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIElllqqhqdrieqlisehevEITGLTEKASSARSQANsiq 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1527 -ELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAK--RNHL-----RMVDS 1598
Cdd:pfam15921 299 sQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARteRDQFsqesgNLDDQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1599 LQTSLdAETRSRNEALRVKKKMEGDLNEME----IQLSQANRIASEAQKHLKNSQAHLK----DTQLQLDDAVHANDDLK 1670
Cdd:pfam15921 379 LQKLL-ADLHKREKELSLEKEQNKRLWDRDtgnsITIDHLRRELDDRNMEVQRLEALLKamksECQGQMERQMAAIQGKN 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1671 ENIAIVERRNNLLQAELEELRAVVEQTErsrklAEQELIETSERVqlLHSQNTSLINQKKKME---SDLTQLQTEVEEAV 1747
Cdd:pfam15921 458 ESLEKVSSLTAQLESTKEMLRKVVEELT-----AKKMTLESSERT--VSDLTASLQEKERAIEatnAEITKLRSRVDLKL 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1748 QEC---RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTI------------------KDLQHRLDEAEQIA 1806
Cdd:pfam15921 531 QELqhlKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVgqhgrtagamqvekaqleKEINDRRLELQEFK 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1807 LKGGKKqlqklEARVRELE---NELEAEQKRNAESVKGMRKSERRIKELTYQ-TEEDKKNLMRLQDLVDKLQLKVKAYKR 1882
Cdd:pfam15921 611 ILKDKK-----DAKIRELEarvSDLELEKVKLVNAGSERLRAVKDIKQERDQlLNEVKTSRNELNSLSEDYEVLKRNFRN 685
|
650 660
....*....|....*....|....*
gi 255918225 1883 QAEEAEEQANTNLSKFRKVQHELDE 1907
Cdd:pfam15921 686 KSEEMETTTNKLKMQLKSAQSELEQ 710
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
865-1541 |
3.83e-12 |
|
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: 71.92 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 865 LEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDnlnDAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAK--- 941
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTL---CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKrea 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 942 ---KRKLEDECSELKKDIDDLELTLAKVEKEKHATE--NKVKNLTEEMAGLDEIIAKLT------KEKKALQEAHQQALD 1010
Cdd:TIGR00618 252 qeeQLKKQQLLKQLRARIEELRAQEAVLEETQERINraRKAAPLAAHIKAVTQIEQQAQrihtelQSKMRSRAKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1011 DLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQ--ESIMDLENDKLQLEEKLKKKEFD 1088
Cdd:TIGR00618 332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQqkTTLTQKLQSLCKELDILQREQAT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1089 ISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKK 1168
Cdd:TIGR00618 412 IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1169 REA---EFQKMRRDLEEATLQHEATAAAL----------------RKKHADS--------------VAELGEQIDNLQRV 1215
Cdd:TIGR00618 492 VLArllELQEEPCPLCGSCIHPNPARQDIdnpgpltrrmqrgeqtYAQLETSeedvyhqltserkqRASLKEQMQEIQQS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1216 KQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEE 1295
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1296 KEALISQLTRGKLSYTQQMEDLKRQLEEegkaknALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQWRT 1375
Cdd:TIGR00618 652 QLTLTQERVREHALSIRVLPKELLASRQ------LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEN 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1376 KYETdaiqRTEELEEAKKKLAQRLQDAEEavEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNaAAAALDKKQRNFDKIL 1455
Cdd:TIGR00618 726 ASSS----LGSDLAAREDALNQSLKELMH--QARTVLKARTEAHFNNNEEVTAALQTGAELSH-LAAEIQFFNRLREEDT 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1456 AEWKQKyEESQSELESSQKEARSLSTELFklknayEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQL 1535
Cdd:TIGR00618 799 HLLKTL-EAEIGQEIPSDEDILNLQCETL------VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKI 871
|
....*...
gi 255918225 1536 --EVEKLE 1541
Cdd:TIGR00618 872 iqLSDKLN 879
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
848-1602 |
4.31e-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: 71.62 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 848 EKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQ--VQAEQDNLNDAEERCDQL----------IKNKI 915
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQadRHQEHIRARDSLIQSLATrleldgfergPFSER 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 916 QLEAKVKEMTERLEDEEEMNAELTA--------KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL 987
Cdd:TIGR00606 391 QIKNFHTLVIERQEDEAKTAAQLCAdlqskerlKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSS 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 988 DEIIAK---LTKEKKALQEAHQQALDDLQAEEDKV-----NTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEG 1059
Cdd:TIGR00606 471 DRILELdqeLRKAERELSKAEKNSLTETLKKEVKSlqnekADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQ 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1060 DLKLTQESIMDLEN------DKLQLEEKLKKKEFDISQQNSKIED---EQALALQLQKKLKENQARIEELEEELEAERTA 1130
Cdd:TIGR00606 551 IRKIKSRHSDELTSllgyfpNKKQLEDWLHSKSKEINQTRDRLAKlnkELASLEQNKNHINNELESKEEQLSSYEDKLFD 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1131 RAKVEKLRSDLSR---ELEEISERLEEAGGATSVQ-----------------IEMNKKREAEFQKMRRDLEEATL----Q 1186
Cdd:TIGR00606 631 VCGSQDEESDLERlkeEIEKSSKQRAMLAGATAVYsqfitqltdenqsccpvCQRVFQTEAELQEFISDLQSKLRlapdK 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1187 HEATAAALRKKHADSVAELGeQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIikaKANLEKVSRTLEdqanEYRVKLE 1266
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLG-LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL---KNDIEEQETLLG----TIMPEEE 782
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1267 EAQRSLNDFTTQRaklqtengELARQLEEKEALISQLTRgklsyTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLR 1346
Cdd:TIGR00606 783 SAKVCLTDVTIME--------RFQMELKDVERKIAQQAA-----KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNR 849
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1347 EQYEEEMEAKAELQRVLSKANSEVAQWRTkyetdAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNE 1426
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKTNELKSEKLQIGT-----NLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1427 IEDLMVDVERSNAAAA-ALDKKQRNFDKILAEWK--QKYEESQSELESSQKEarslsTELFKLKNAYEESLEHLETFKRE 1503
Cdd:TIGR00606 925 KEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKdiENKIQDGKDDYLKQKE-----TELNTVNAQLEECEKHQEKINED 999
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1504 NKNLQEEI-------SDLTEQLGEGGKN--VHELEKIRKQLEVEKLELQ--------SALEEAEASLEHEEGKILRAQLE 1566
Cdd:TIGR00606 1000 MRLMRQDIdtqkiqeRWLQDNLTLRKREneLKEVEEELKQHLKEMGQMQvlqmkqehQKLEENIDLIKRNHVLALGRQKG 1079
|
810 820 830
....*....|....*....|....*....|....*.
gi 255918225 1567 FNQIKAEIERKLAEKdeEMEQAKRNHLRMVDSLQTS 1602
Cdd:TIGR00606 1080 YEKEIKHFKKELREP--QFRDAEEKYREMMIVMRTT 1113
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1210-1929 |
8.76e-12 |
|
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: 70.77 E-value: 8.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1210 DNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRsLNDFTTQRAKLQTENGEL 1289
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQ-KREAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1290 ARQLEEKEALISqltrgKLSYTQQMEDLKRQLEEEGKAKNALAHALQSSRhdcdllrEQYEEEMEAKAELQRVLSKANSE 1369
Cdd:TIGR00618 266 RARIEELRAQEA-----VLEETQERINRARKAAPLAAHIKAVTQIEQQAQ-------RIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1370 VAQwrtKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEdlmVDVERSNAAAAALDKKQR 1449
Cdd:TIGR00618 334 VKQ---QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKT---TLTQKLQSLCKELDILQR 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1450 NFDKILAEwKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGgKNVHELE 1529
Cdd:TIGR00618 408 EQATIDTR-TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK-EQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1530 KIRKQLEVEKLELQSALE-EAEASLEHEEGK-------------ILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRM 1595
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPcPLCGSCIHPNPArqdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1596 vDSLQTSLDAETRSRNealRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHANDDlkENIAI 1675
Cdd:TIGR00618 566 -QEIQQSFSILTQCDN---RSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHL--QQCSQ 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1676 VERRNNLLQAELEELRAVVEQTERSRKLAEQELiETSERVQLLHSQNTSLINQKKKMESDLTQLQTeveeavqecrnaee 1755
Cdd:TIGR00618 640 ELALKLTALHALQLTLTQERVREHALSIRVLPK-ELLASRQLALQKMQSEKEQLTYWKEMLAQCQT-------------- 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1756 kakkaitdaaMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELEN---ELEAEQ 1832
Cdd:TIGR00618 705 ----------LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNnneEVTAAL 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1833 KRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERA 1912
Cdd:TIGR00618 775 QTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKY 854
|
730
....*....|....*..
gi 255918225 1913 DIAESQVNKLRAKSRDI 1929
Cdd:TIGR00618 855 EECSKQLAQLTQEQAKI 871
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
836-1248 |
9.85e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 9.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 836 FKIKPLLKSAETEKEMANMKEEFGRVK---DALEKSEARRKELEEKMVSLLQEKNDLQLQVQ------AEQDNLNDAEER 906
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEeriKELEEKEERLEELKKKLKELEKRLEELEERHElyeeakAKKEELERLKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 907 CDQLIKNKIqlEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLE-----LTLAKVEKEKHATEN------ 975
Cdd:PRK03918 381 LTGLTPEKL--EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkCPVCGRELTEEHRKElleeyt 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 976 -KVKNLTEEMAGLDEIIAKLTKEKKALQEA---------HQQALDDLQAEEDKVNTLTKSkvKLEQQVDDLEGSLEQEKK 1045
Cdd:PRK03918 459 aELKRIEKELKEIEEKERKLRKELRELEKVlkkeselikLKELAEQLKELEEKLKKYNLE--ELEKKAEEYEKLKEKLIK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1046 VRMDLERAKRKLegdlkltqESIMDLENDKLQLEEKLKKKEFDISQQNSKI-----EDEQALALQLQK---------KLK 1111
Cdd:PRK03918 537 LKGEIKSLKKEL--------EKLEELKKKLAELEKKLDELEEELAELLKELeelgfESVEELEERLKElepfyneylELK 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1112 ENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVqiEMNKKREAEFQKMRRDLEEATLQHEaTA 1191
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELE-EL 685
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 255918225 1192 AALRKKHADSVAELGEQIDNLQRVKQKLEKekseFKLELDDVTSNMEQIIKAKANLE 1248
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELREKVKKYKALLK 738
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
839-1520 |
1.35e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 69.75 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 839 KPLLKSAETEKEMANM-KEEFGRVKDALEKSEARRKELEEKMVSLlqeKNDLQLQVQAEQDNLNDAEercdqliKNKIQL 917
Cdd:pfam05483 144 KDLIKENNATRHLCNLlKETCARSAEKTKKYEYEREETRQVYMDL---NNNIEKMILAFEELRVQAE-------NARLEM 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 918 EAKVKEMTERLED-EEEMNAELTAKKRK---LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAK 993
Cdd:pfam05483 214 HFKLKEDHEKIQHlEEEYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDH 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 994 LTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKL----EQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIM 1069
Cdd:pfam05483 294 LTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1070 DLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEIS 1149
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIH 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1150 ErLEEAGGATSVQIEMNKKreaEFQKMRRDLEEATLQHeataaalrkkhadsvAELGEQIDNLQRVKQKLEKEKSEFKLE 1229
Cdd:pfam05483 454 D-LEIQLTAIKTSEEHYLK---EVEDLKTELEKEKLKN---------------IELTAHCDKLLLENKELTQEASDMTLE 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1230 LDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRslnDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLS 1309
Cdd:pfam05483 515 LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKI 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1310 YTQQMEDLKRQLEEEGKaknalahALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELE 1389
Cdd:pfam05483 592 LENKCNNLKKQIENKNK-------NIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIE 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1390 EAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMvdversnaaaAALDKKQRNFDKILAEWKQKYEESQSEL 1469
Cdd:pfam05483 665 DKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMV----------ALMEKHKHQYDKIIEERDSELGLYKNKE 734
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 255918225 1470 ESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGE 1520
Cdd:pfam05483 735 QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
849-1772 |
1.57e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 70.08 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 849 KEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKnDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMTERL 928
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 929 EDEEEMNAELTAKKRKLEDECSELKKDIDdleltlakvekekHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAH--- 1005
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKtel 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1006 --QQALDDLQAEEDKVNTLTKSKVKLEQQ----VDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLE 1079
Cdd:TIGR00606 346 lvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1080 EKLKKKEFDISQQNSKIEDEqalalqlQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggat 1159
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELK-------KEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNS---- 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1160 svQIEMNKKREAEFQKMRRDLEEaTLQHEATAAALRKKHADSVaelgEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQ 1239
Cdd:TIGR00606 495 --LTETLKKEVKSLQNEKADLDR-KLRKLDQEMEQLNHHTTTR----TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLG 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1240 IIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLndfttqrAKLQTENGELARQLEEKEALISQLTR------GKLSYTQQ 1313
Cdd:TIGR00606 568 YFPNKKQLEDWLHSKSKEINQTRDRLAKLNKEL-------ASLEQNKNHINNELESKEEQLSSYEDklfdvcGSQDEESD 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1314 MEDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQY-------EEEMEAKAELQRVLSKANSEVAQWRTKYEtdaiQRTE 1386
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLK----STES 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1387 ELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQN---EIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYE 1463
Cdd:TIGR00606 717 ELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKvnrDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMER 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1464 ESQSELESSQKEARSLS-TELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLEL 1542
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAkLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1543 QSALEEAEASLEHEEGKILRAQLEFNQIK---------AEIERKLAEKDEEMEQAKRNHLRMVDSLQTSLDAETRSRNEA 1613
Cdd:TIGR00606 877 GTNLQRRQQFEEQLVELSTEVQSLIREIKdakeqdsplETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGY 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1614 LR-----VKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELE 1688
Cdd:TIGR00606 957 MKdienkIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEE 1036
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1689 ELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEavQECRNAEEKAKKAITDAAMMA 1768
Cdd:TIGR00606 1037 LKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE--PQFRDAEEKYREMMIVMRTTE 1114
|
....
gi 255918225 1769 EELK 1772
Cdd:TIGR00606 1115 LVNK 1118
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1489-1926 |
2.42e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.30 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1489 AYEESLEHLETfkrenknLQEEISDLTEQLGEGGKNVHEL-EKIRKQLEvEKLELQSALEEAEASLEHEEGKILRAQLEF 1567
Cdd:PRK02224 245 EHEERREELET-------LEAEIEDLRETIAETEREREELaEEVRDLRE-RLEELEEERDDLLAEAGLDDADAEAVEARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1568 NQIKAEIErKLAEKDEEMEQAKRNHLRMVDSLQTSLDaETRSRNEALRVK-KKMEGDLNEMEIQLSQANRIASEAQKHLK 1646
Cdd:PRK02224 317 EELEDRDE-ELRDRLEECRVAAQAHNEEAESLREDAD-DLEERAEELREEaAELESELEEAREAVEDRREEIEELEEEIE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1647 NSQAHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSR---KLAE--QElIETSERVQLLHSQ 1721
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagKCPEcgQP-VEGSPHVETIEED 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1722 NtsliNQKKKMESDLTQLQTEVEEAvqecrnaEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDE 1801
Cdd:PRK02224 474 R----ERVEELEAELEDLEEEVEEV-------EERLERA--------EDLVEAEDRIERLEERREDLEELIAERRETIEE 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1802 AEQialkggkkQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKL-------- 1873
Cdd:PRK02224 535 KRE--------RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaiadaed 606
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 255918225 1874 QLKVKAYKRQA-EEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKS 1926
Cdd:PRK02224 607 EIERLREKREAlAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1653-1938 |
2.76e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1653 KDTQLQLDDAvhanddlKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQ-----------ELIETSERVQLLHSQ 1721
Cdd:COG1196 175 EEAERKLEAT-------EENLERLEDILGELERQLEPLERQAEKAERYRELKEElkeleaellllKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1722 NTSLINQKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDE 1801
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1802 AEQiALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYK 1881
Cdd:COG1196 328 LEE-ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 255918225 1882 RQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKKMHDEE 1938
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
869-1211 |
4.63e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 869 EARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLiknkiqleAKVKEMTERLEDEEEMNAELTAKKRKLEde 948
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL--------QRLAEYSWDEIDVASAEREIAELEAELE-- 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 949 csELKKDIDDLEltlaKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKvk 1028
Cdd:COG4913 679 --RLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-- 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1029 LEQQVDDLEGSlEQEKKVRMDLERAKRKLEGDLKLTQESIMDLendklqLEEKLKKKEFDISQQNSKIEDEQALALQLQK 1108
Cdd:COG4913 751 LEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERA------MRAFNREWPAETADLDADLESLPEYLALLDR 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1109 ----KLKENQARIEELEEeleaeRTARAKVEKLRSDLSRELEEISERLEEA---------GGATSVQIEMNKKREAEFQK 1175
Cdd:COG4913 824 leedGLPEYEERFKELLN-----ENSIEFVADLLSKLRRAIREIKERIDPLndslkripfGPGRYLRLEARPRPDPEVRE 898
|
330 340 350
....*....|....*....|....*....|....*.
gi 255918225 1176 MRRDLEEATLQHEATAAALRKKHADSVAELGEQIDN 1211
Cdd:COG4913 899 FRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1176-1804 |
7.57e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1176 MRRDLEEATLQHEATAAAlrKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDvtsnmEQIIKAKANLEKvsrtLE 1255
Cdd:COG4913 240 AHEALEDAREQIELLEPI--RELAERYAAARERLAELEYLRAALRLWFAQRRLELLE-----AELEELRAELAR----LE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1256 DQANEYRVKLEEAQRSLNDFTTQRAKLQTEN-GELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHA 1334
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1335 LQSSRHDCDLLREQYEEemeAKAELQRVLSKANSEVAQWRTkyETDAIQRT-----EELEEAKKKLAQRLQDAEEAVEAV 1409
Cdd:COG4913 389 AAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEA--EIASLERRksnipARLLALRDALAEALGLDEAELPFV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1410 nakCSSLE-KTKHRL-QNEIE--------DLMVDVERSNAAAAALDK---KQR-NFDKIlaewkqkyEESQSELESSQKE 1475
Cdd:COG4913 464 ---GELIEvRPEEERwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPRLD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1476 ARSLSTELFKLKNAYEESLEHLetfkrenknlqeeisdlteqlgeggknvhelekIRKQLEVEKLElqsaleeAEASLEH 1555
Cdd:COG4913 533 PDSLAGKLDFKPHPFRAWLEAE---------------------------------LGRRFDYVCVD-------SPEELRR 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1556 EEGKILRAqlefNQIKAEieRKLAEKDEEMEQAKRNHL-----RMVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQ 1630
Cdd:COG4913 573 HPRAITRA----GQVKGN--GTRHEKDDRRRIRSRYVLgfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQER 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1631 LSQANRIA--SEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKEniaiverrnnlLQAELEELRAVVEQtersrklAEQEL 1708
Cdd:COG4913 647 REALQRLAeySWDEIDVASAEREIAELEAELERLDASSDDLAA-----------LEEQLEELEAELEE-------LEEEL 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1709 IETSERVQLLHSQNTSLinqkkkmESDLTQLQTEVEEAVQECRNAEEKAkkaitdaammAEELKKEQDTSAHLERMKKNM 1788
Cdd:COG4913 709 DELKGEIGRLEKELEQA-------EEELDELQDRLEAAEDLARLELRAL----------LEERFAAALGDAVERELRENL 771
|
650
....*....|....*.
gi 255918225 1789 EQTIKDLQHRLDEAEQ 1804
Cdd:COG4913 772 EERIDALRARLNRAEE 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
846-1430 |
1.11e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 846 ETEKEMANMKEEFG---RVKDALEKSEARRKELE------EKMVSLLQEKNDLQ-----LQVQAEQDNLNDAEERCDQLI 911
Cdd:COG4913 222 DTFEAADALVEHFDdleRAHEALEDAREQIELLEpirelaERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 912 KNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLE-DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEI 990
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 991 IAKLTKEKKALQEAHQQALDDLQAEEDKvntLTKSKVKLEQQVDDLEG---SLEQeKKVRMD--LERAKRKLEGDLKLTQ 1065
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAE---AEAALRDLRRELRELEAeiaSLER-RKSNIParLLALRDALAEALGLDE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1066 ESI------MDLEN----------------------------------DKLQLEEKL---KKKEFDISQQNSKIeDEQAL 1102
Cdd:COG4913 458 AELpfvgelIEVRPeeerwrgaiervlggfaltllvppehyaaalrwvNRLHLRGRLvyeRVRTGLPDPERPRL-DPDSL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1103 ALQLQkkLKENQARieELEEELEAERTARAKVEKLRsdlsrELEEISERLEEAGgatsvQIEMNKKReaeFQKMRRDLEE 1182
Cdd:COG4913 537 AGKLD--FKPHPFR--AWLEAELGRRFDYVCVDSPE-----ELRRHPRAITRAG-----QVKGNGTR---HEKDDRRRIR 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1183 AT--LQHEATA--AALRKKHA---DSVAELGEQIDNLQRVKQKLEKEKS------EFKLELDDVTSNMEQIIKAKANLEK 1249
Cdd:COG4913 600 SRyvLGFDNRAklAALEAELAeleEELAEAEERLEALEAELDALQERREalqrlaEYSWDEIDVASAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1250 VS------RTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEE 1323
Cdd:COG4913 680 LDassddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1324 EGKAKNALAHALQSSRHDCDLLREQYEEEMEAKaeLQRVLSKANSEVAQWRTKYET----DAI---QRTEELEEAKKKLA 1396
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERA--MRAFNREWPAETADLDADLESlpeyLALldrLEEDGLPEYEERFK 837
|
650 660 670
....*....|....*....|....*....|....
gi 255918225 1397 QRLQDAEEavEAVNAKCSSLEKTKHRLQNEIEDL 1430
Cdd:COG4913 838 ELLNENSI--EFVADLLSKLRRAIREIKERIDPL 869
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
846-1302 |
1.17e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.99 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 846 ETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQA-------EQDNLNDAEERCDQLIKNKIQLE 918
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAhneeaesLREDADDLEERAEELREEAAELE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 919 AKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAkltkEK 998
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE----EA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 999 KALQEA--------------HQQALDDlqaEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRmDLERAKRKLEGDLKLT 1064
Cdd:PRK02224 446 EALLEAgkcpecgqpvegspHVETIEE---DRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDL 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1065 QESIMD----LENDKLQLEEKLKKKEfdisQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSD 1140
Cdd:PRK02224 522 EELIAErretIEEKRERAEELRERAA----ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTL 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1141 LSrELEEISERLEEAGGATSVQIEMNKKRE---AEFQKMRRDLEEATlqHEATAAALRKKHADSVAELGEQIDNLQRvkq 1217
Cdd:PRK02224 598 LA-AIADAEDEIERLREKREALAELNDERRerlAEKRERKRELEAEF--DEARIEEAREDKERAEEYLEQVEEKLDE--- 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1218 kLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYrvklEEAQRSLNDFTTQRAKLQTEN-GELARQLEEK 1296
Cdd:PRK02224 672 -LREERDDLQAEIGAVENELEELEELRERREALENRVEALEALY----DEAEELESMYGDLRAELRQRNvETLERMLNET 746
|
....*.
gi 255918225 1297 EALISQ 1302
Cdd:PRK02224 747 FDLVYQ 752
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1200-1873 |
1.53e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1200 DSVAELGEQIDNLQRVKQKLEKEKSEFKLeLDDVTSNMEQIIKAKANLEKVsRTLEDQANEYRV--KLEEAQRSLNDFTT 1277
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLAEL-EYLRAALRLWFAqrRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1278 QRAKLQTENGELARQLEEKEALISQLTRGKL-SYTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEAK 1356
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRgNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1357 AELQRVLSKANSEVAQWRTKYE---TDAIQRTEELEEAKKKLAQRLQDAE--------EAVEAVNAKCSSLEKTKHRL-- 1423
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEealAEAEAALRDLRRELRELEAEIASLErrksnipaRLLALRDALAEALGLDEAELpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1424 --------------QNEIE--------DLMVDVERSNAAAAALDK---KQR-NFDKIlaewkqkyEESQSELESSQKEAR 1477
Cdd:COG4913 463 vgelievrpeeerwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1478 SLSTELFKLKNAYEESLEHL-------------ETFKRENKNLQEE--ISD------------LTEQLGEGGKN---VHE 1527
Cdd:COG4913 535 SLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRAITRAgqVKGngtrhekddrrrIRSRYVLGFDNrakLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1528 LEKIRKQLEVEKLELQSALEEAEASLEHEEGKILR----AQLEFNQIK-AEIERKLAEKDEEMEQAKRNHLRmVDSLQTS 1602
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEIDvASAEREIAELEAELERLDASSDD-LAALEEQ 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1603 LDAetrsrnealrvkkkMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAvhanddlkeniaiVERRNNL 1682
Cdd:COG4913 694 LEE--------------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA-------------EDLARLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1683 LQAELEELRAVVEQTERSRKLAEQelietservqllhsqntsLINQKKKMESDLTQLQTEVEEAVQE-CRNAEEKAKKAI 1761
Cdd:COG4913 747 LRALLEERFAAALGDAVERELREN------------------LEERIDALRARLNRAEEELERAMRAfNREWPAETADLD 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1762 TDAAMMAEELK-----KEQDTSAHLERMK----KNMEQTIKDLQHRLDEAEQIAlkggKKQLQKLEARVRELE-NE---- 1827
Cdd:COG4913 809 ADLESLPEYLAlldrlEEDGLPEYEERFKellnENSIEFVADLLSKLRRAIREI----KERIDPLNDSLKRIPfGPgryl 884
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 255918225 1828 -LEAEQKRNAEsVKGMRKSERRIKELTYQTEED--KKNLMRLQDLVDKL 1873
Cdd:COG4913 885 rLEARPRPDPE-VREFRQELRAVTSGASLFDEElsEARFAALKRLIERL 932
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
837-1286 |
1.64e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 837 KIKPLLKSAETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQ 916
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 917 LEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHatENKVKnlTEEMAGLDEIIAKLTK 996
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIK--AAEEAKKAEEDKKKAE 1678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 997 EKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQEsimdlendkL 1076
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE---------A 1749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1077 QLEEKLKKKefdiSQQNSKIEDEQALALQlqkklKENQARIEELEEELEAERtaRAKVEKLRSDLSRELEEISERLEEAG 1156
Cdd:PTZ00121 1750 KKDEEEKKK----IAHLKKEEEKKAEEIR-----KEKEAVIEEELDEEDEKR--RMEVDKKIKDIFDNFANIIEGGKEGN 1818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1157 GATSVQIEM---NKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDV 1233
Cdd:PTZ00121 1819 LVINDSKEMedsAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDI 1898
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255918225 1234 TS---------NMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTEN 1286
Cdd:PTZ00121 1899 EReipnnnmagKNNDIIDDKLDKDEYIKRDAEETREEIIKISKKDMCINDFSSKFCDYMKDN 1960
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
849-1428 |
2.35e-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: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 849 KEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMTERL 928
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 929 EDEEEMNAELTAKKRKLEDECSELKKDIDD---LELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAH 1005
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKnksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1006 QQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMdlERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKK 1085
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1086 EFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEiserleeaggatsvQIEM 1165
Cdd:TIGR04523 341 NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN--------------QEKL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1166 NKKREAEFQKMRRDLEEATLQHEaTAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSnmeQIIKAKA 1245
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIE-RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR---SINKIKQ 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1246 NLEKVSRTLEDQANEyrvkleeaqrsLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEE-- 1323
Cdd:TIGR04523 483 NLEQKQKELKSKEKE-----------LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKdd 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1324 EGKAKNALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVaqwrtkyeTDAIQRTEELEEAKKKLAQRLQDAE 1403
Cdd:TIGR04523 552 FELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEK--------KDLIKEIEEKEKKISSLEKELEKAK 623
|
570 580
....*....|....*....|....*
gi 255918225 1404 EAVEAVNAKCSSLEKTKHRLQNEIE 1428
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1273-1938 |
2.44e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1273 NDFTTQRAKLQTENGELARQLEEKEaliSQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEE 1352
Cdd:PTZ00121 1079 FDFDAKEDNRADEATEEAFGKAEEA---KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1353 MEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKcsslEKTKHRLQNEIEDLM- 1431
Cdd:PTZ00121 1156 IARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAE----EARKAEDAKKAEAVKk 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1432 VDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLknayEESLEHLETFKRENKNLQEEI 1511
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA----EEKKKADEAKKAEEKKKADEA 1307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1512 SDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQlefnqiKAEIERKLAEKDEEMEQAKRN 1591
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE------AAEEKAEAAEKKKEEAKKKAD 1381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1592 HLRMvdslqtslDAETRSRNEALRvKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHAnDDLKE 1671
Cdd:PTZ00121 1382 AAKK--------KAEEKKKADEAK-KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA-DEAKK 1451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1672 NIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESdltQLQTEVEEAVQECR 1751
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE---AKKAEEAKKADEAK 1528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1752 NAEEKAKkaiTDAAMMAEELKKEQDTSaHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVREL------E 1825
Cdd:PTZ00121 1529 KAEEAKK---ADEAKKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeeE 1604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1826 NELEAEQKRNAESVKG----MRKSE---RRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQAntnlSKF 1898
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIkaeeLKKAEeekKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA----EEA 1680
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 255918225 1899 RKVQHELDEAEERADIAESQVNKLRAKSRDIGAKKMHDEE 1938
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
856-1335 |
2.59e-10 |
|
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: 65.97 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 856 EEFGRVKDALEKSEAR-RKELEEKMVSL---------LQEKNDLQLQVQAEQDNLND--AEERcDQLIKNKIQLEAKVKE 923
Cdd:pfam01576 562 EEKAAAYDKLEKTKNRlQQELDDLLVDLdhqrqlvsnLEKKQKKFDQMLAEEKAISAryAEER-DRAEAEAREKETRALS 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 924 MTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL-DEIIAklTKEKKALQ 1002
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELeDELQA--TEDAKLRL 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1003 EAHQQALD-----DLQAEEDKVNTLTKSKVKleqQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQ 1077
Cdd:pfam01576 719 EVNMQALKaqferDLQARDEQGEEKRRQLVK---QVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREE 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1078 LEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGG 1157
Cdd:pfam01576 796 AVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGAS 875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1158 ATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRK--KHADSV-AELGEQIDNLQRV---KQKLEKEKSEFKLELD 1231
Cdd:pfam01576 876 GKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKstLQVEQLtTELAAERSTSQKSesaRQQLERQNKELKAKLQ 955
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1232 DVTS----------------------NMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGEL 1289
Cdd:pfam01576 956 EMEGtvkskfkssiaaleakiaqleeQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQL 1035
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 255918225 1290 ARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHAL 1335
Cdd:pfam01576 1036 KRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
846-1112 |
3.17e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.43 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 846 ETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMT 925
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 926 ERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEah 1005
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE-- 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1006 qqalddlqaeedKVNTLTKSKVKLEQQVDDLEGSLEQEK--KVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLK 1083
Cdd:TIGR04523 525 ------------KIEKLESEKKEKESKISDLEDELNKDDfeLKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
250 260
....*....|....*....|....*....
gi 255918225 1084 KKEFDISQQNSKIEDEQALALQLQKKLKE 1112
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1479-1925 |
5.42e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.66 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1479 LSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEA---EASLEH 1555
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIknkLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1556 ---------EEGKILRAQL-----EFNQIKAEIERKLAEKDEEMEQAKRNHLRMVDSLQ------TSLDAETRSRNEALR 1615
Cdd:TIGR04523 202 llsnlkkkiQKNKSLESQIselkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDeqnkikKQLSEKQKELEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1616 VKKKMEGDLNEMEIQLSQANR-----IASEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEEL 1690
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNqkeqdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1691 RAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEE 1770
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1771 LKKEQDTSAHLERMKKNMEQTIKDLQHRLD-------------EAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAE 1837
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqnlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1838 SVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQL-KVKAYKRQAEEAEEQANTNLSKfrkvqhELDEAEERADIAE 1916
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLeKEIDEKNKEIEELKQTQKSLKK------KQEEKQELIDQKE 595
|
....*....
gi 255918225 1917 SQVNKLRAK 1925
Cdd:TIGR04523 596 KEKKDLIKE 604
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
849-1257 |
7.62e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 849 KEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQD--NLNDAEERCDQLIKNKIQLEAKVKEMTE 926
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 927 RLEDEEEMNAELTAKKRKLEDEC-----------SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 995
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 996 KEKKALQE-----------AHQQALDDLQAEEDKV---------------NTLTKSKVKLEQQVDDLEGSLEQEKKVRMD 1049
Cdd:COG4717 241 LEERLKEArlllliaaallALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1050 LERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEfdisqqnskiedEQALALQLQKKLKENQARIEELEEELEAERT 1129
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAE------------ELEEELQLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1130 ARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKR--EAEFQKMRRDLEEATLQHEataaALRKKHADSVAELG- 1206
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELE----ELREELAELEAELEq 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 255918225 1207 -EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMeqiiKAKANLEKVSRTLEDQ 1257
Cdd:COG4717 465 lEEDGELAELLQELEELKAELRELAEEWAALK----LALELLEEAREEYREE 512
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
916-1359 |
8.95e-10 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 63.38 E-value: 8.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 916 QLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 995
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 996 KEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDK 1075
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1076 LQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSreleeiserleEA 1155
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS-----------SM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1156 GGATSvqiemnkKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEF-KLElddvt 1234
Cdd:pfam07888 264 AAQRD-------RTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELqRLE----- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1235 snmEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLndfTTQRAKLQTENGELARQLEEKEALisqltrgkLSYTQQM 1314
Cdd:pfam07888 332 ---ERLQEERMEREKLEVELGREKDCNRVQLSESRREL---QELKASLRVAQKEKEQLQAEKQEL--------LEYIRQL 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 255918225 1315 EdlkRQLEEEGKAKNALAHALQSSRHDCDLL--REQYEEEMEAKAEL 1359
Cdd:pfam07888 398 E---QRLETVADAKWSEAALTSTERPDSPLSdsEDENPEALQPPRPL 441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1346-1937 |
1.54e-09 |
|
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: 63.55 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1346 REQYEEEMEAKAELQRVLSKANSEVAQWRTKYET----DAIQRteELEEAK-KKLAQRLQDAEEAVEAVNAKCSSLEKTK 1420
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKaeryQALLK--EKREYEgYELLKEKEALERQKEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1421 HRLQNEIEDLmvdVERSNAAAAALDKKQRNFDKILAEwkqkyeesqsELESSQKEARSLSTELFKLKNAYEESLEHLETF 1500
Cdd:TIGR02169 254 EKLTEEISEL---EKRLEEIEQLLEELNKKIKDLGEE----------EQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1501 KRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIErklaE 1580
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE----K 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1581 KDEEMEQAKRNHLRMVDSLQtSLDAETRSRNEALrvkKKMEGDLNEMEIQLSqanriasEAQKHLKNSQAHLKDTQLQLD 1660
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQ-RLSEELADLNAAI---AGIEAKINELEEEKE-------DKALEIKKQEWKLEQLAADLS 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1661 DAVHANDDLKENIAIVERRNNLLQAELEELRA---VVEQTERSRKLAEQELietSERVQLLHSQNTSLINQKKkmesdlt 1737
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAqarASEERVRGGRAVEEVL---KASIQGVHGTVAQLGSVGE------- 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1738 QLQTEVEEAVQECRNA-----EEKAKKAITDAA------MMAEELKKEQDTSAHLERMKKN------------------- 1787
Cdd:TIGR02169 536 RYATAIEVAAGNRLNNvvvedDAVAKEAIELLKrrkagrATFLPLNKMRDERRDLSILSEDgvigfavdlvefdpkyepa 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1788 MEQTIKD--LQHRLDEAEQI------------------ALKGG--------------KKQLQKLEARVRELENELEAEQK 1833
Cdd:TIGR02169 616 FKYVFGDtlVVEDIEAARRLmgkyrmvtlegelfeksgAMTGGsraprggilfsrsePAELQRLRERLEGLKRELSSLQS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1834 RNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERAD 1913
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
650 660
....*....|....*....|....
gi 255918225 1914 IAESQVNKLRAKSRDIGAKKMHDE 1937
Cdd:TIGR02169 776 KLEEALNDLEARLSHSRIPEIQAE 799
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
837-1329 |
1.73e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 837 KIKPLLKSAETEKEMANMK---EEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQ----DNLNDAEE--RC 907
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAkkkaDEAKKAEEakKA 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 908 DQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVknltEEMAGL 987
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI----EEVMKL 1600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 988 DEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDlKLTQES 1067
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED-KKKAEE 1679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1068 IMDLENDKLQLEEKLKKKEFD---ISQQNSKIEDEQALALQLQKKLKENqarieeleeeleaertaRAKVEKLRsdlsRE 1144
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEakkAEELKKKEAEEKKKAEELKKAEEEN-----------------KIKAEEAK----KE 1738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1145 LEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEatlqhEATAAALRKKHADSVAELGeqidnlqrVKQKLEKEKS 1224
Cdd:PTZ00121 1739 AEEDKKKAEEA-----------KKDEEEKKKIAHLKKE-----EEKKAEEIRKEKEAVIEEE--------LDEEDEKRRM 1794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1225 EFKLELDDVTSNMEQIIK-----------AKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQL 1293
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANIIEggkegnlvindSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
|
490 500 510
....*....|....*....|....*....|....*.
gi 255918225 1294 EEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKN 1329
Cdd:PTZ00121 1875 DLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGK 1910
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1475-1920 |
1.78e-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: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1475 EARSLSTELFKLKNAYEESLEhletfKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEasLE 1554
Cdd:COG4913 226 AADALVEHFDDLERAHEALED-----AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1555 HEEGKILRAQLEFNQIKAEIERkLAEKDEEMEQAKRNH-LRMVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQ 1633
Cdd:COG4913 299 ELRAELARLEAELERLEARLDA-LREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1634 A----NRIASEAQKHLKNSQAHLKDTQLQLDDAV-------HANDDLKENIAIVERRNNLLQAELEELRAVVEqteRSRK 1702
Cdd:COG4913 378 SaeefAALRAEAAALLEALEEELEALEEALAEAEaalrdlrRELRELEAEIASLERRKSNIPARLLALRDALA---EALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1703 LAEQ------ELIETS----------ERVqlLHSQNTSL-------------INQKK----------------------- 1730
Cdd:COG4913 455 LDEAelpfvgELIEVRpeeerwrgaiERV--LGGFALTLlvppehyaaalrwVNRLHlrgrlvyervrtglpdperprld 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1731 ------KMESDLTQLQTEVEEAVQE------CRNAEE--KAKKAITDAAMMAEELKK-EQDTSAHLER---MKKNMEQTI 1792
Cdd:COG4913 533 pdslagKLDFKPHPFRAWLEAELGRrfdyvcVDSPEElrRHPRAITRAGQVKGNGTRhEKDDRRRIRSryvLGFDNRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1793 KDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQK--RNAESVKGMRKSERRIKELtyqtEEDKKNLMRLQDLV 1870
Cdd:COG4913 613 AALEAELAELEE-ELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL----EAELERLDASSDDL 687
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 255918225 1871 DKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVN 1920
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
916-1142 |
3.83e-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: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 916 QLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 995
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 996 KEKK----ALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDL 1071
Cdd:COG4942 104 EELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1072 ENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEE--LEEELEAERTARAKVEKLRSDLS 1142
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARleAEAAAAAERTPAAGFAALKGKLP 256
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1182-1840 |
4.97e-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: 61.66 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1182 EATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDvtsNMEQIIKAKANLEKVSRTLEDQANEY 1261
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKE---DHEKIQHLEEEYKKEINDKEKQVSLL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1262 RVKLEEAQRSLNDFTTqrakLQTENGELARQLEEKEAL----ISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQS 1337
Cdd:pfam05483 246 LIQITEKENKMKDLTF----LLEESRDKANQLEEKTKLqdenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1338 SRHDCDLLREQYEEEMEAkaelqrvLSKANSEVAQWRTKYETDaiqrTEELEEAKKKLAQRLQDAEEAVEAV----NAKC 1413
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEE-------LNKAKAAHSFVVTEFEAT----TCSLEELLRTEQQRLEKNEDQLKIItmelQKKS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1414 SSLEKTKhRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEES 1493
Cdd:pfam05483 391 SELEEMT-KFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1494 LEhletfkrenknlqeeisdlteqlgeggknvhELEKIRKQLEVEKLElqsaleeaEASLEHEEGKILRAQLEFNQIKAE 1573
Cdd:pfam05483 470 LK-------------------------------EVEDLKTELEKEKLK--------NIELTAHCDKLLLENKELTQEASD 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1574 IERKLAEKDEEMEQAKRNHLRMVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLK 1653
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1654 DTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKME 1733
Cdd:pfam05483 591 ILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISE 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1734 SDL----TQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKG 1809
Cdd:pfam05483 671 EKLleevEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSN 750
|
650 660 670
....*....|....*....|....*....|....
gi 255918225 1810 GKKQLQKLEARV---RELENELEAEQKRNAESVK 1840
Cdd:pfam05483 751 IKAELLSLKKQLeieKEEKEKLKMEAKENTAILK 784
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1100-1339 |
5.03e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1100 QALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnkkrEAEFQKMRRD 1179
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------------EQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1180 LEEATLQheatAAALRKKHADSVAELGEQIDNLQRVKQKlekekSEFKLELDdvTSNMEQIIKAKANLEKVSRTLEDQAN 1259
Cdd:COG4942 85 LAELEKE----IAELRAELEAQKEELAELLRALYRLGRQ-----PPLALLLS--PEDFLDAVRRLQYLKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1260 EYRVKLEEAQRSLNDFTTQRAKL-------QTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALA 1332
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELeallaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*..
gi 255918225 1333 HALQSSR 1339
Cdd:COG4942 234 AEAAAAA 240
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
898-1837 |
1.10e-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: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 898 DNLNDAEERCDQLIKNKiqleAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKdiddlelTLAKVEKEKHATENKV 977
Cdd:TIGR01612 769 NKINDYAKEKDELNKYK----SKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIK-------TISIKEDEIFKIINEM 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 978 KNLTEE-MAGLDEIIAKLTKEKKALQEAHQQ---ALDDLQAE--EDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLe 1051
Cdd:TIGR01612 838 KFMKDDfLNKVDKFINFENNCKEKIDSEHEQfaeLTNKIKAEisDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTL- 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1052 rakRKLEGDLKL---TQESIMDLENDKLQLEEKLKKK----------------EFDISQQNSKIEDEQALA--------- 1103
Cdd:TIGR01612 917 ---KKVDEYIKIcenTKESIEKFHNKQNILKEILNKNidtikesnlieksykdKFDNTLIDKINELDKAFKdaslndyea 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1104 -----LQLQKKLKENQARIEELEEELEAERTARA------KVEKLRSDLSR-------ELEEISERLEEAGGATSVQIEM 1165
Cdd:TIGR01612 994 knnelIKYFNDLKANLGKNKENMLYHQFDEKEKAtndieqKIEDANKNIPNieiaihtSIYNIIDEIEKEIGKNIELLNK 1073
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1166 NKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKlELDDVTSNMEQIIKAKA 1245
Cdd:TIGR01612 1074 EILEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALE-EIKKKSENYIDEIKAQI 1152
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1246 N-LEKVSRTLedQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGK---LSYTQQMEDL-KRQ 1320
Cdd:TIGR01612 1153 NdLEDVADKA--ISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKginLSYGKNLGKLfLEK 1230
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1321 LEEEGKAKNALAHALQSSRHDCDLLREQYEE-------EMEAKAELQrVLSKANSEvaqwRTKYETDAIQRTEELEEAKK 1393
Cdd:TIGR01612 1231 IDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEienemgiEMDIKAEME-TFNISHDD----DKDHHIISKKHDENISDIRE 1305
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1394 KLAQRLQDaeeaveavNAKCSSLEKTKHRLQNEIedlmVDVERSNAAAAALDKKQRNFDKILaewkqkyeesqselessq 1473
Cdd:TIGR01612 1306 KSLKIIED--------FSEESDINDIKKELQKNL----LDAQKHNSDINLYLNEIANIYNIL------------------ 1355
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1474 kearslstELFKLKNAYEESLEHLETFKRENKNLQEEISDlTEQLGEGGKNVHELEKIRKQLEveklelqSALEEAEASL 1553
Cdd:TIGR01612 1356 --------KLNKIKKIIDEVKEYTKEIEENNKNIKDELDK-SEKLIKKIKDDINLEECKSKIE-------STLDDKDIDE 1419
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1554 EHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRMVDSlqtslDAETRSRNEALRVKKKMEGDLNEMEIQLSQ 1633
Cdd:TIGR01612 1420 CIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADN-----KSQHILKIKKDNATNDHDFNINELKEHIDK 1494
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1634 ANRIASEAQKHLKNSQAH-LKDTQLQLDDAVHAND----DLKENIAIVERRNNLLQAELEELRAVV----EQTERSRKLA 1704
Cdd:TIGR01612 1495 SKGCKDEADKNAKAIEKNkELFEQYKKDVTELLNKysalAIKNKFAKTKKDSEIIIKEIKDAHKKFileaEKSEQKIKEI 1574
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1705 EQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQ--TEVEEAVQECRNAEEKAKKAITDAAMMAEE--LKKEQDTSAH 1780
Cdd:TIGR01612 1575 KKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLkiSDIKKKINDCLKETESIEKKISSFSIDSQDteLKENGDNLNS 1654
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*..
gi 255918225 1781 LERMKKNMEQTIKDLQHRldeaeqialkggKKQLQKLEARVRELENELEaEQKRNAE 1837
Cdd:TIGR01612 1655 LQEFLESLKDQKKNIEDK------------KKELDELDSEIEKIEIDVD-QHKKNYE 1698
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1671-1899 |
1.62e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1671 ENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQEC 1750
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1751 RNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNMEQTIKDLQHRLDE--AEQIALKGGKKQLQKLEARVREL 1824
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1825 ENELEAEQKR----NAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQlkvkayKRQAEEAEEQANTNLSKFR 1899
Cdd:COG4942 180 LAELEEERAAlealKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE------AEAAAAAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1065-1292 |
1.68e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1065 QESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRE 1144
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1145 LEEISERLEE-------AGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRkkhadsvaelgEQIDNLQRVKQ 1217
Cdd:COG4942 99 LEAQKEELAEllralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR-----------ADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255918225 1218 KLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQ 1292
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1075-1755 |
1.76e-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: 59.74 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1075 KLQLEEKLKKKEFDIsQQNSKIEDEQALALQ------------LQKKLKENQARIeeleeelEAERTARAKVEKLRSDLS 1142
Cdd:pfam05483 94 KVSIEAELKQKENKL-QENRKIIEAQRKAIQelqfenekvslkLEEEIQENKDLI-------KENNATRHLCNLLKETCA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1143 RELEEISERLEEAGGATSVQIEMNKKREaefqKMRRDLEEATLQHEATAAALRKKhadsvaelgeqidnLQRVKQKLEKE 1222
Cdd:pfam05483 166 RSAEKTKKYEYEREETRQVYMDLNNNIE----KMILAFEELRVQAENARLEMHFK--------------LKEDHEKIQHL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1223 KSEFKLELDDVtsnmeqiikakanlekvsrtlEDQANEYRVKLEEAQRSLNDFTTqrakLQTENGELARQLEEKEAL--- 1299
Cdd:pfam05483 228 EEEYKKEINDK---------------------EKQVSLLLIQITEKENKMKDLTF----LLEESRDKANQLEEKTKLqde 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1300 -ISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEME----AKAELQRVLSKANSEVAQWR 1374
Cdd:pfam05483 283 nLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEelnkAKAAHSFVVTEFEATTCSLE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1375 TKYETDAiQRTEELEEAKKKLAQRLQ----DAEEAVEAVNAKCSSLEKTKHRLqNEIEDLMVDVERSNAAAAALDKKQRN 1450
Cdd:pfam05483 363 ELLRTEQ-QRLEKNEDQLKIITMELQkkssELEEMTKFKNNKEVELEELKKIL-AEDEKLLDEKKQFEKIAEELKGKEQE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1451 F-------DKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGK 1523
Cdd:pfam05483 441 LifllqarEKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQE 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1524 NV----HELEKIRKQ---LEVEKLELQSALEEAEASL--EHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLR 1594
Cdd:pfam05483 521 DIinckKQEERMLKQienLEEKEMNLRDELESVREEFiqKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1595 MVDSLQTSLDAETRSRNEALRVKKKMEG-DLNEMEIQLSQAN-RIASEAQKH---LKNSQAHLKDTQLQ----LDDAVHA 1665
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGSAENkQLNAYEIKVNKLElELASAKQKFeeiIDNYQKEIEDKKISeeklLEEVEKA 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1666 NDDLKENIAIVERRNNLLQAELEELRAVVEQTERS------RKLAEQELIETSERVQ--LLHSQNTSLINQKKKMESDLT 1737
Cdd:pfam05483 681 KAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQydkiieERDSELGLYKNKEQEQssAKAALEIELSNIKAELLSLKK 760
|
730
....*....|....*...
gi 255918225 1738 QLQTEVEEAVQECRNAEE 1755
Cdd:pfam05483 761 QLEIEKEEKEKLKMEAKE 778
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1442-1882 |
1.83e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1442 AALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLtEQLGEG 1521
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1522 GKNVHELEKIRKQLEVEKLELQsALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRMVDSLQT 1601
Cdd:COG4717 128 LPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1602 SLDAETRSRNEALRVKKKMEGDLNEMEIQLsqanrIASEAQKHLKNSQAHLK--DTQLQLDDAVHANDDLKENIA----- 1674
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARLLLLiaAALLALLGLGGSLLSLILTIAgvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1675 ------IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQ 1748
Cdd:COG4717 282 vlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1749 ECRNAEEKAKKA----------ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKggkKQLQKLE 1818
Cdd:COG4717 362 ELQLEELEQEIAallaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE---EELEELE 438
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255918225 1819 ARVRELENELEAEQKRnaesvkgMRKSERRIKELTYQTEEDKKnLMRLQDLVDKLQLKVKAYKR 1882
Cdd:COG4717 439 EELEELEEELEELREE-------LAELEAELEQLEEDGELAEL-LQELEELKAELRELAEEWAA 494
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1188-1593 |
2.23e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1188 EATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFK---LELDDVTSNMEQIIKAKANLEKVSRTLED--QANEYR 1262
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAelqEELEELEEELEELEAELEELREELEKLEKllQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1263 VKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKlsytQQMEDLKRQLEEEgkAKNALAHALQSSRHdc 1342
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQ----EELEELLEQLSLA--TEEELQDLAEELEE-- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1343 dlLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYETDAIQrtEELEEAK------------------------------ 1392
Cdd:COG4717 204 --LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE--ERLKEARlllliaaallallglggsllsliltiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1393 -----------KKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQk 1461
Cdd:COG4717 280 flvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1462 yeesqSELESSQKEARSLSTELFKLKNA-YEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKI--RKQLEVE 1538
Cdd:COG4717 359 -----LEEELQLEELEQEIAALLAEAGVeDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEE 433
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255918225 1539 KLELQSALEEAEASLE--HEEGKILRAQLE-------FNQIKAEIERKLAEKDEEMEQAKRNHL 1593
Cdd:COG4717 434 LEELEEELEELEEELEelREELAELEAELEqleedgeLAELLQELEELKAELRELAEEWAALKL 497
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
888-1430 |
2.56e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 888 DLQLQVQAEQdNLNDAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDdlelTLAKVE 967
Cdd:PRK04863 528 RLRQQQRAER-LLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQ----RLAARA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 968 KEKHATENKVKNLTEEM-------AGLDEIIAKLTKEKKALQ------EAHQQALDD----LQ----AEEDKVNTL--TK 1024
Cdd:PRK04863 603 PAWLAAQDALARLREQSgeefedsQDVTEYMQQLLERERELTverdelAARKQALDEeierLSqpggSEDPRLNALaeRF 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1025 SKVKLEQQVDDLE-----------GSLEQEKKVRmDLERAKRKLEG------DLKLTQESIMDLENDKLQLEEKLKkkef 1087
Cdd:PRK04863 683 GGVLLSEIYDDVSledapyfsalyGPARHAIVVP-DLSDAAEQLAGledcpeDLYLIEGDPDSFDDSVFSVEELEK---- 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1088 DISQQNSKIedeqalalqlqkklkenQARIEELEEELEAERTARakvEKLRSDLSRELEEISERLEeaggatsvqiemnk 1167
Cdd:PRK04863 758 AVVVKIADR-----------------QWRYSRFPEVPLFGRAAR---EKRIEQLRAEREELAERYA-------------- 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1168 KREAEFQKMRR---DLEEATLQH---------EATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLelddvts 1235
Cdd:PRK04863 804 TLSFDVQKLQRlhqAFSRFIGSHlavafeadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSA------- 876
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1236 nMEQIIKAKANLEKvsRTLEDQANEYRVKLEEAQ----------RSLNDFTTQRAKLQTENGELA---RQLEEKEALISQ 1302
Cdd:PRK04863 877 -LNRLLPRLNLLAD--ETLADRVEEIREQLDEAEeakrfvqqhgNALAQLEPIVSVLQSDPEQFEqlkQDYQQAQQTQRD 953
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1303 LTRGK--LSYTQQM------EDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEvaqWR 1374
Cdd:PRK04863 954 AKQQAfaLTEVVQRrahfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSS---YD 1030
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1375 TKYET--DAIQRTEEL-----EEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDL 1430
Cdd:PRK04863 1031 AKRQMlqELKQELQDLgvpadSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNL 1093
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1237-1707 |
3.09e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1237 MEQIIKAKANLEKVS-RTLEDQANEYRvKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLtRGKLSYTQQME 1315
Cdd:COG4717 48 LERLEKEADELFKPQgRKPELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-REELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1316 DLKRQLEEEGKAKNALAhalqssrhDCDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTkyetdaiQRTEELEEAKKKL 1395
Cdd:COG4717 126 QLLPLYQELEALEAELA--------ELPERLEELEERLEELRELEEELEELEAELAELQE-------ELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1396 AQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDK------------ILAEWKQKYE 1463
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallaLLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1464 ESQSELESSQKEARSLS---TELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLG-EGGKNVHELEKIRKQLEvEK 1539
Cdd:COG4717 271 LILTIAGVLFLVLGLLAllfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIE-EL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1540 LELQSALEEAEASLEHEEGKILRAQLeFNQIKAEIERKLAEKDEEMEQAkRNHLRMVDSLQTSLDAETRSRNEALRvkkk 1619
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIAAL-LAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLE---- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1620 mEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHAN--DDLKENIAIVERRNNLLQAELEELRAVVEQT 1697
Cdd:COG4717 424 -ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALELL 502
|
490
....*....|
gi 255918225 1698 ERSRKLAEQE 1707
Cdd:COG4717 503 EEAREEYREE 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1014-1412 |
3.28e-08 |
|
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: 58.93 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1014 AEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQN 1093
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1094 SKIEDEQALALQLQKKLKENQARIEELeeeleaertaRAKVEKLRSDLSRELEEISERLEEAGGATSVQIEmNKKREAEF 1173
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKL----------EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE-ARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1174 QKMRRDLEEATLQHE-ATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSR 1252
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEiQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1253 TLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQltrgklsyTQQMEDLKRQLEEEGKAKNALA 1332
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE--------ELSLEDVQAELQRVEEEIRALE 971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1333 halqssrhDCDLLR-EQYEEEMEAKAELQRVLSKANSEvaqwrtkyETDAIQRTEELEEAKKKLAQrlqdaeEAVEAVNA 1411
Cdd:TIGR02169 972 --------PVNMLAiQEYEEVLKRLDELKEKRAKLEEE--------RKAILERIEEYEKKKREVFM------EAFEAINE 1029
|
.
gi 255918225 1412 K 1412
Cdd:TIGR02169 1030 N 1030
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1128-1613 |
3.87e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1128 RTARAKVEKLRsdlsrELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATL-----------QHEATAAALRK 1196
Cdd:COG4913 245 EDAREQIELLE-----PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELeelraelarleAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1197 KHADSVAELGEQIDNLQ-RVKQKLEKEKSEFKLELDDVTSN----MEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRS 1271
Cdd:COG4913 320 ALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRrarlEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1272 LNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEE-GKAKNAL------------------- 1331
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlGLDEAELpfvgelievrpeeerwrga 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1332 ----------------AHALQSSRH----------DCDLLREQYEEEMEAKAE---LQRVLSKANSEVAQW---RTKYET 1379
Cdd:COG4913 480 iervlggfaltllvppEHYAAALRWvnrlhlrgrlVYERVRTGLPDPERPRLDpdsLAGKLDFKPHPFRAWleaELGRRF 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1380 DAIQ--RTEELEEAKK---------------------KLAQRL---QDAEEAVEAvnakcssLEKTKHRLQNEIEDLMVD 1433
Cdd:COG4913 560 DYVCvdSPEELRRHPRaitragqvkgngtrhekddrrRIRSRYvlgFDNRAKLAA-------LEAELAELEEELAEAEER 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1434 VERSNAAAAALDKKQRNFDKIlaewkQKYEESQSELESSQKEARSLSTELFKLknayEESLEHLETFKRENKNLQEEISD 1513
Cdd:COG4913 633 LEALEAELDALQERREALQRL-----AEYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEE 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1514 LTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEegkiLRAQLEfnqikaeiERKLAEKDEEMEQakrnhl 1593
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE----LRALLE--------ERFAAALGDAVER------ 765
|
570 580
....*....|....*....|
gi 255918225 1594 RMVDSLQTSLDAETRSRNEA 1613
Cdd:COG4913 766 ELRENLEERIDALRARLNRA 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1216-1443 |
3.94e-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: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1216 KQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEE 1295
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1296 KEALISQLTRG--KLSYTQQMEDLKRQleeegKAKNALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQW 1373
Cdd:COG4942 102 QKEELAELLRAlyRLGRQPPLALLLSP-----EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1374 RTKYETDAIQRtEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAA 1443
Cdd:COG4942 177 EALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1666-1899 |
5.11e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.10 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1666 NDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRK--LAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEV 1743
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1744 EeAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNMEQTIKDLQHRLDEAEQIALKGGKKQ 1813
Cdd:COG3206 243 A-ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1814 LQKLEARVRELENELEAEQKRnaesVKGMRKSERRIKELTYQTEEDKKNLMRLQDlvdklqlkvkaykrQAEEAEEQANT 1893
Cdd:COG3206 322 LEALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVARELYESLLQ--------------RLEEARLAEAL 383
|
....*.
gi 255918225 1894 NLSKFR 1899
Cdd:COG3206 384 TVGNVR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1047-1282 |
5.50e-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: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1047 RMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEA 1126
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1127 ERTARAKVEKLRSDLSR--ELEEI--SERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEatlqheatAAALRKKHADSV 1202
Cdd:COG4942 102 QKEELAELLRALYRLGRqpPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE--------LAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1203 AELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSL--NDFTTQRA 1280
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTpaAGFAALKG 253
|
..
gi 255918225 1281 KL 1282
Cdd:COG4942 254 KL 255
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
865-1396 |
5.58e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 58.31 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 865 LEKSEARRKELEEKMVSLLQEKNDLQLQVQAE-QDNLNDAEERCDQLIKNKIQLEAKVKEMTERLEdeEEMNAELTAKKR 943
Cdd:pfam12128 356 LENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALE--SELREQLEAGKL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 944 KLEDECSELKKDIDDLELTLAKVEKEKHATENKvKNLTEEMAGLDEIIAKLTKEKKALQE-------AHQQALDDLQAEE 1016
Cdd:pfam12128 434 EFNEEEYRLKSRLGELKLRLNQATATPELLLQL-ENFDERIERAREEQEAANAEVERLQSelrqarkRRDQASEALRQAS 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1017 DKVNTLTKSKVKLEQQVDDLEGSL------------EQEKKV-------RMDLERAKRKLEGDLKLTQESI-MDLE---- 1072
Cdd:pfam12128 513 RRLEERQSALDELELQLFPQAGTLlhflrkeapdweQSIGKVispellhRTDLDPEVWDGSVGGELNLYGVkLDLKridv 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1073 NDKLQLEEKLKKKefdISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERL 1152
Cdd:pfam12128 593 PEWAASEEELRER---LDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1153 EEAGGA---------TSVQIEMN---KKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQ-RVKQKL 1219
Cdd:pfam12128 670 NKALAErkdsanerlNSLEAQLKqldKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRsGAKAEL 749
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1220 EKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQAneyrvKLEEAQRSLNDFttQRAKLQTENGELARQLEEKEAL 1299
Cdd:pfam12128 750 KALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIA-----VRRQEVLRYFDW--YQETWLQRRPRLATQLSNIERA 822
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1300 ISQLtRGKLsyTQQMEDLKR---QLEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEAK--AELQRVLSKANSEVAQWR 1374
Cdd:pfam12128 823 ISEL-QQQL--ARLIADTKLrraKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDAnsEQAQGSIGERLAQLEDLK 899
|
570 580
....*....|....*....|..
gi 255918225 1375 TKYETDAIQRTEELEEAKKKLA 1396
Cdd:pfam12128 900 LKRDYLSESVKKYVEHFKNVIA 921
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1199-1415 |
6.84e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1199 ADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQ 1278
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1279 RAKLQTENGELARQLEEKEAL-----------ISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLRE 1347
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255918225 1348 QYEEEMEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSS 1415
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
835-1305 |
7.81e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.60 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 835 YFKIKPLLKSAETE-KEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQA---EQDNLNDAEERCDQL 910
Cdd:PRK01156 168 YDKLKDVIDMLRAEiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNamdDYNNLKSALNELSSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 911 IKNKIQLEAKVKEMTERLEDEEEMNAELTA--------------KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENK 976
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYKEleerhmkiindpvyKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 977 VKNLTEEMAGLDEIIakltkEKKALQEAHQQALDDLQAEEDKVNTLTKS----KVKLE---------------------- 1030
Cdd:PRK01156 328 IKKLSVLQKDYNDYI-----KKKSRYDDLNNQILELEGYEMDYNSYLKSieslKKKIEeyskniermsafiseilkiqei 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1031 ----------------QQVDDLEGSLEQEKKV----RMDLERAKRKLEGDLK-------LTQESIMDL----ENDKLQLE 1079
Cdd:PRK01156 403 dpdaikkelneinvklQDISSKVSSLNQRIRAlrenLDELSRNMEMLNGQSVcpvcgttLGEEKSNHIinhyNEKKSRLE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1080 EKLKKKEFDISQQNSKIEDEQALALQLQK-----------KLKENQARIEELEEELEAERTARAKVEKLRSDL-SRELEE 1147
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYLESeeinksineynKIESARADLEDIKIKINELKDKHDKYEEIKNRYkSLKLED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1148 ISERLEEAGGATSV----QIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEK 1223
Cdd:PRK01156 563 LDSKRTSWLNALAVisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1224 SEFKlELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQL 1303
Cdd:PRK01156 643 ILIE-KLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDI 721
|
..
gi 255918225 1304 TR 1305
Cdd:PRK01156 722 NE 723
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1617-1850 |
8.23e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 8.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1617 KKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRAVVEQ 1696
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1697 TER--SRKLAEQELIETSERVQLLHSQNTS--LINQKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELK 1772
Cdd:COG4942 102 QKEelAELLRALYRLGRQPPLALLLSPEDFldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255918225 1773 KEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlkggkKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIK 1850
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAEL-----AELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1417-1922 |
9.66e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.34 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1417 EKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKnAYEESLEH 1496
Cdd:TIGR04523 137 KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK-KKIQKNKS 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1497 LET----FKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKA 1572
Cdd:TIGR04523 216 LESqiseLKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1573 EIERKLAEKDEEMEQAKRNHLRMVDS----LQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNS 1648
Cdd:TIGR04523 296 EISDLNNQKEQDWNKELKSELKNQEKkleeIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1649 QAHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQ 1728
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1729 KKKMESDLTQLQTEVEEAVQECRNAEEKAKKaitdaamMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALK 1808
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQ-------KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1809 GGKKQLQKlEARVRELENELEAEQKRNAESV--KGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEE 1886
Cdd:TIGR04523 529 LESEKKEK-ESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
490 500 510
....*....|....*....|....*....|....*.
gi 255918225 1887 AEEQANTNLSKFRKVQHELDEAEERADIAESQVNKL 1922
Cdd:TIGR04523 608 KEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1187-1911 |
1.04e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.54 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1187 HEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLE 1266
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1267 eaqrslNDFTTQRAKLQTENGELARqLEEKEALISQLTRGKLSYTQQMEDLKR-QLEEEGKAKNALAHALQssrhdcDLL 1345
Cdd:pfam12128 308 ------GELSAADAAVAKDRSELEA-LEDQHGAFLDADIETAAADQEQLPSWQsELENLEERLKALTGKHQ------DVT 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1346 REQYEEEMEAKAELQRVLSKANSEVAQwrtKYETDAIQRTEElEEAKKKLAQRLQDAEEAVEAvnakcsSLEKTKHRLQN 1425
Cdd:pfam12128 375 AKYNRRRSKIKEQNNRDIAGIKDKLAK---IREARDRQLAVA-EDDLQALESELREQLEAGKL------EFNEEEYRLKS 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1426 EIEDLMVdveRSNAAAAALDKK--QRNFDKILAEWKQKyeesqseLESSQKEARSLSTELFKLKNAYEESLEHLETFKRE 1503
Cdd:pfam12128 445 RLGELKL---RLNQATATPELLlqLENFDERIERAREE-------QEAANAEVERLQSELRQARKRRDQASEALRQASRR 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1504 NKNLQEEISDLTEQLGEGGKNVHEL---------EKIRKQLEVEKL---ELQSALEEAEASLEheegkilraqLEFNQIK 1571
Cdd:pfam12128 515 LEERQSALDELELQLFPQAGTLLHFlrkeapdweQSIGKVISPELLhrtDLDPEVWDGSVGGE----------LNLYGVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1572 AEIERKLAEKDEEMEQAKRnhlRMVDSLQTSLDAEtRSRNEALrvkkkmegdlnemEIQLSQANRIASEAQKHLKNSQAH 1651
Cdd:pfam12128 585 LDLKRIDVPEWAASEEELR---ERLDKAEEALQSA-REKQAAA-------------EEQLVQANGELEKASREETFARTA 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1652 LK---DTQLQLDDaVHANDDLKENIAIvERRNNLLQAELEELRAVVEQTERSRKLAEQELIETServqllhSQNTSLINQ 1728
Cdd:pfam12128 648 LKnarLDLRRLFD-EKQSEKDKKNKAL-AERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQK-------REARTEKQA 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1729 KKKMESDLTQLQtevEEAVQECRNAEEKAKKAITDA--AMMAEELKK---EQDTSAHLERMKKNMEQTIKDLQHRLDEA- 1802
Cdd:pfam12128 719 YWQVVEGALDAQ---LALLKAAIAARRSGAKAELKAleTWYKRDLASlgvDPDVIAKLKREIRTLERKIERIAVRRQEVl 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1803 --EQIALKGGKKQLQKLEARVRELEN---ELEAEQKRNAESVKGMRKS-ERRIKELTYQTEEDKKNLMRLQDLVDKL-QL 1875
Cdd:pfam12128 796 ryFDWYQETWLQRRPRLATQLSNIERaisELQQQLARLIADTKLRRAKlEMERKASEKQQVRLSENLRGLRCEMSKLaTL 875
|
730 740 750
....*....|....*....|....*....|....*.
gi 255918225 1876 KVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEER 1911
Cdd:pfam12128 876 KEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKK 911
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
863-1095 |
1.08e-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: 56.31 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 863 DALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMTERLedeeemnAELTAKK 942
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------AELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 943 RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTL 1022
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1023 TKSKVKLEQQVDDLEGSLEQEKKVRmdlERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSK 1095
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1040-1449 |
1.71e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1040 LEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQalalqLQKKLKENQARIEE 1119
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-----LEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1120 LEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHA 1199
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1200 DSVAELgeqidNLQRVKQKLEKEKSEFK-----LELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLND 1274
Cdd:COG4717 231 QLENEL-----EAAALEERLKEARLLLLiaaalLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1275 FTTQRAKLQT-ENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALahALQSSRHDCDLLREQY---- 1349
Cdd:COG4717 306 ELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAgved 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1350 EEEMEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKK-LAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIE 1428
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeLEEELEELEEELEELEEELEELREELAELEAELE 463
|
410 420
....*....|....*....|.
gi 255918225 1429 DLMVDVERSNAAAAALDKKQR 1449
Cdd:COG4717 464 QLEEDGELAELLQELEELKAE 484
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
917-1604 |
1.96e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.39 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 917 LEAKVKEMTERLEDEEEMNAELTAKKRkledecSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTK 996
Cdd:pfam12128 263 LHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLD 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 997 EKKALQEAHQQALDDLQAE-----------EDKVNTLT------KSKVKlEQQVDDLEGSLEQEKKVRMDLERAKRKLEG 1059
Cdd:pfam12128 337 ADIETAAADQEQLPSWQSElenleerlkalTGKHQDVTakynrrRSKIK-EQNNRDIAGIKDKLAKIREARDRQLAVAED 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1060 DLKlTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALAlqlQKKLKENQARIEELEEELEAERT-ARAKVEKLR 1138
Cdd:pfam12128 416 DLQ-ALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATA---TPELLLQLENFDERIERAREEQEaANAEVERLQ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1139 SDLsRELEEISERLEEAGGATSVQIEMNKKREAEFQKMrRDLEEATLQHeataaALRKKHADSVAELGEQIDNLQRVKQK 1218
Cdd:pfam12128 492 SEL-RQARKRRDQASEALRQASRRLEERQSALDELELQ-LFPQAGTLLH-----FLRKEAPDWEQSIGKVISPELLHRTD 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1219 LEKEKSE-----------FKLELDDVTSN----MEQIIKAKanLEKVSRTL----------EDQANEYRVKLEEAQRSLn 1273
Cdd:pfam12128 565 LDPEVWDgsvggelnlygVKLDLKRIDVPewaaSEEELRER--LDKAEEALqsarekqaaaEEQLVQANGELEKASREE- 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1274 dfTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEgkaKNALAHALQssrhdcDLLREQYEEEM 1353
Cdd:pfam12128 642 --TFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQ---LKQLDKKHQ------AWLEEQKEQKR 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1354 EAKAELQrvlskansevAQWRtkyetdaiqrteELEEAKK-KLAQRLQDAEEAVEAVNAKCSSLEKTKHRlqnEIEDLMV 1432
Cdd:pfam12128 711 EARTEKQ----------AYWQ------------VVEGALDaQLALLKAAIAARRSGAKAELKALETWYKR---DLASLGV 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1433 DVERsnaaAAALDKKQRNFDKILAEWKQKyeesqselessqkeaRSLSTELFKLKNayEESLEHLETFKRENKNLQEEIS 1512
Cdd:pfam12128 766 DPDV----IAKLKREIRTLERKIERIAVR---------------RQEVLRYFDWYQ--ETWLQRRPRLATQLSNIERAIS 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1513 DLTEQLgegGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILR-AQLEFNQIKAEIERKLAEKDEEMEQAKRN 1591
Cdd:pfam12128 825 ELQQQL---ARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKlATLKEDANSEQAQGSIGERLAQLEDLKLK 901
|
730
....*....|...
gi 255918225 1592 HLRMVDSLQTSLD 1604
Cdd:pfam12128 902 RDYLSESVKKYVE 914
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1237-1452 |
2.25e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1237 MEQIIKAK-ANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQR--AKLQTENGELARQLEEKEALISQLTRGKLSYTQQ 1313
Cdd:COG3206 162 LEQNLELRrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1314 MEDLKRQLEEEGKAKNALAHALQSSRhdcdlLREQYEEEMEAKAELQRVLSKANSEVAQWRtkyetdaiqrtEELEEAKK 1393
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALR-----------AQIAALRA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1394 KLAQRLQDAEEAVEAVNAkcsSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFD 1452
Cdd:COG3206 306 QLQQEAQRILASLEAELE---ALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
854-1295 |
2.97e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 55.60 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 854 MKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLiknkiqlEAKVKEMTERLEDEEE 933
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL-------QTEVDALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 934 MNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQA----- 1008
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTdtalt 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1009 -LDDLQAEEDKV-NTLTKSKVKLEQQVDDlegSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKE 1086
Cdd:pfam10174 440 tLEEALSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1087 FDISQQNSKIEDEQALALQLQKKLKENQarieeleeelEAERTARAKVEklRSDLSRELE-EISERLEEAGGA-TSVQIE 1164
Cdd:pfam10174 517 SKLKSLEIAVEQKKEECSKLENQLKKAH----------NAEEAVRTNPE--INDRIRLLEqEVARYKEESGKAqAEVERL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1165 MNKKREAEFQKMRRDLEEATLqhEATAAALRKKHADSVAEL--GEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIK 1242
Cdd:pfam10174 585 LGILREVENEKNDKDKKIAEL--ESLTLRQMKEQNKKVANIkhGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMG 662
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1243 AkanLEKVSRTLEdqanEYRVKLEEAQRSLNDFTTQRAKLQtenGELARQLEE 1295
Cdd:pfam10174 663 A---LEKTRQELD----ATKARLSSTQQSLAEKDGHLTNLR---AERRKQLEE 705
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1483-1929 |
3.22e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 55.25 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1483 LFKLKNAYEEsLEHLETFKRE--NKNLQEEISDLtEQLGEGGKNVHELEKIRKQ----LEVEKLELQSALEEAEASLEhe 1556
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1557 EGKILRAQLEFNqikaEIERKLAEKDEEMEQakrnhlrMVDSLQTSLDAETRSRNEALRVKKK----------------- 1619
Cdd:pfam06160 78 KYRFKKAKKALD----EIEELLDDIEEDIKQ-------ILEELDELLESEEKNREEVEELKDKyrelrktllanrfsygp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1620 ----MEGDLNEMEIQLSQANRiaseaqkhLKNSQAHL--KDTQLQLDDAVHANDDLKENI-AIVERRNNLLQAELEELRA 1692
Cdd:pfam06160 147 aideLEKQLAEIEEEFSQFEE--------LTESGDYLeaREVLEKLEEETDALEELMEDIpPLYEELKTELPDQLEELKE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1693 VVEQTERSR-KLAEQELIETSERVQLLHSQNTSLINQK--KKMESDLTQLQTEVEEaVQECRNAEEKAKKaitdaammae 1769
Cdd:pfam06160 219 GYREMEEEGyALEHLNVDKEIQQLEEQLEENLALLENLelDEAEEALEEIEERIDQ-LYDLLEKEVDAKK---------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1770 ELKKEQDT-SAHLERMKKNMEQTIKDLQH-----RLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMR 1843
Cdd:pfam06160 288 YVEKNLPEiEDYLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1844 KSERRIKELTYQTEEDKKNLMRL-------QDLVDKLQLKVKAYKRQAE----------------EAEEQANTNLSKFRK 1900
Cdd:pfam06160 368 EILEQLEEIEEEQEEFKESLQSLrkdeleaREKLDEFKLELREIKRLVEksnlpglpesyldyffDVSDEIEDLADELNE 447
|
490 500
....*....|....*....|....*....
gi 255918225 1901 VQHELDEAEERADIAESQVNKLRAKSRDI 1929
Cdd:pfam06160 448 VPLNMDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
841-1057 |
3.65e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 841 LLKSAETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAK 920
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 921 VKEMTERLEDEEEMNAELTAKKRKLEDECS-------------------------ELKKDIDDLELTLAKVEKEKHATEN 975
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPlalllspedfldavrrlqylkylapARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 976 KVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQ--EKKVRMDLERA 1053
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAaaERTPAAGFAAL 251
|
....
gi 255918225 1054 KRKL 1057
Cdd:COG4942 252 KGKL 255
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
833-1326 |
3.71e-07 |
|
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: 55.44 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 833 KLYFKIKPLLKSAETEKEMANMKEEFGRVKDALEKSE--ARRKELEEKMVSLLQEKNDL------QLQVQAEQDNLNDAE 904
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLdrklrkLDQEMEQLNHHTTTR 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 905 ERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKV 977
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 978 KNLTEEMAGLDEIIAKLTKekkalQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKL 1057
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCG-----SQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQT 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1058 EGDLkltQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIeeleeeleaeRTARAKVEKL 1137
Cdd:TIGR00606 690 EAEL---QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEI----------PELRNKLQKV 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1138 RSDLSRELEEISERlEEAGGATSVQIEMNKKREAEFQKMRRdLEEATLQHEataaalrKKHADSVAELgeQIDNLQRVKQ 1217
Cdd:TIGR00606 757 NRDIQRLKNDIEEQ-ETLLGTIMPEEESAKVCLTDVTIMER-FQMELKDVE-------RKIAQQAAKL--QGSDLDRTVQ 825
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1218 KLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANE---YRVKLEEAQRSLNDFTTQRAKLQTENGELARQLE 1294
Cdd:TIGR00606 826 QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElksEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIK 905
|
490 500 510
....*....|....*....|....*....|..
gi 255918225 1295 EKEALISQLTRGKLSYTQQMEDLKRQLEEEGK 1326
Cdd:TIGR00606 906 DAKEQDSPLETFLEKDQQEKEELISSKETSNK 937
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
842-1058 |
4.32e-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: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 842 LKSAETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLlqeknDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKV 921
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 922 KEMTERLEDEEEMNAELTAkkrklEDECSELKKDIDDLELTLAkvEKEKHATEN--KVKNLTEEMAGLdeiiakltkeKK 999
Cdd:COG3206 243 AALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL----------RA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1000 ALQEAHQQALDDLQAEedkVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLE 1058
Cdd:COG3206 306 QLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1358-1777 |
4.33e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1358 ELQRVLSKANSEVAQWRTKYET--DAIQRTEELEEAKKKLAQRLQDAEEAVEAVnakcsSLEKTKHRLQNEIEDLMVDVE 1435
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEEleELEEELEELEAELEELREELEKLEKLLQLL-----PLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1436 RSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSlstELFKLKNAYEESLEHLETFKRENKNLQEEISDLT 1515
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1516 EQLgEGGKNVHELEKIRKQLEVEK---------LELQSALEEAEASLEHEEGKI-LRAQLEFNQIKAEIERKLAEKDEEM 1585
Cdd:COG4717 227 EEL-EQLENELEAAALEERLKEARlllliaaalLALLGLGGSLLSLILTIAGVLfLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1586 EQAKRNHLRMVDSLQTSLDAETRSRNEALrvKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHA 1665
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDL--SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1666 NDDLKENIAIVERRNNL----------LQAELEELRAVVEQTERSR-----KLAEQELIETSERVQLLHSQNTSLINQKK 1730
Cdd:COG4717 384 EEELRAALEQAEEYQELkeeleeleeqLEELLGELEELLEALDEEEleeelEELEEELEELEEELEELREELAELEAELE 463
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 255918225 1731 KMESD--LTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT 1777
Cdd:COG4717 464 QLEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
865-1035 |
5.15e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 865 LEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMTERLE-DEEEMNAELTAKkr 943
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYEEQLGNVRNNK-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 944 kledECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKvntLT 1023
Cdd:COG1579 90 ----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE---LE 162
|
170
....*....|..
gi 255918225 1024 KSKVKLEQQVDD 1035
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1256-1457 |
6.49e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1256 DQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHAL 1335
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1336 QSSRHD-CDLLREQYeeEMEAKAELQRVLSKANSEVAQWRTKY----------ETDAIQRT-EELEEAKKKLAQRLQDAE 1403
Cdd:COG4942 100 EAQKEElAELLRALY--RLGRQPPLALLLSPEDFLDAVRRLQYlkylaparreQAEELRADlAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255918225 1404 EAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAE 1457
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
837-1186 |
9.36e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.35 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 837 KIKPLLKSAETEKEM-ANMKEEFGRVKDALEKSE-------------ARRKELEEKMVSLLQEKNDLQLQ----VQAEQD 898
Cdd:pfam15921 462 KVSSLTAQLESTKEMlRKVVEELTAKKMTLESSErtvsdltaslqekERAIEATNAEITKLRSRVDLKLQelqhLKNEGD 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 899 NLNDAEERCDQLiknKIQLEAK---VKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATEN 975
Cdd:pfam15921 542 HLRNVQTECEAL---KLQMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 976 KVKNLTEEMAGLDEIIAKLT-------KEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQ-EKKVR 1047
Cdd:pfam15921 619 KIRELEARVSDLELEKVKLVnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETtTNKLK 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1048 MDLERAKRKLE---GDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIED-EQALALQLQKK--LKENQARIEELE 1121
Cdd:pfam15921 699 MQLKSAQSELEqtrNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFlEEAMTNANKEKhfLKEEKNKLSQEL 778
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255918225 1122 EELEAERTARA-KVEKLRSDlSRELEEISERLEEAGGATSVQ------IEMNKKREAEFQKMRRDLEEATLQ 1186
Cdd:pfam15921 779 STVATEKNKMAgELEVLRSQ-ERRLKEKVANMEVALDKASLQfaecqdIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
848-1285 |
1.11e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 53.69 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 848 EKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLqlqVQAEQDN---LNDAEERCDQLIKNKI--------- 915
Cdd:PRK04778 90 EAEELNDKFRFRKAKHEINEIESLLDLIEEDIEQILEELQEL---LESEEKNreeVEQLKDLYRELRKSLLanrfsfgpa 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 916 --QLEAKVKEMTERLEDEEEMNAE---LTAKK--RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN----LTEEM 984
Cdd:PRK04778 167 ldELEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreLVEEG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 985 AGLDEIiaKLTKEKKALQEAHQQALDDLQAEE-DKVNTLTKskvKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKL 1063
Cdd:PRK04778 247 YHLDHL--DIEKEIQDLKEQIDENLALLEELDlDEAEEKNE---EIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEH 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1064 TQEsimdlENDKLQLEEKLKKKEFDISqqnskiEDEQALALQLQKKLKENQARIEELEEELeaertarAKVEKLRSDLSR 1143
Cdd:PRK04778 322 AKE-----QNKELKEEIDRVKQSYTLN------ESELESVRQLEKQLESLEKQYDEITERI-------AEQEIAYSELQE 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1144 ELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsvaelgeqidnLQRVKQKLEKEK 1223
Cdd:PRK04778 384 ELEEILKQLEEI-----------EKEQEKLSEMLQGLRKDELEAREKLERYRNK--------------LHEIKRYLEKSN 438
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255918225 1224 -----SEFKLELDDVTSNMEQiikakanlekvsrtLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTE 1285
Cdd:PRK04778 439 lpglpEDYLEMFFEVSDEIEA--------------LAEELEEKPINMEAVNRLLEEATEDVETLEEE 491
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
864-1569 |
1.31e-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: 53.67 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 864 ALEKSEARRKE-LEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKK 942
Cdd:pfam10174 46 ALRKEEAARISvLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 943 RKLEDECSELKKDIDDLELtlaKVEKEKHATENKvknlteemaglDEIIAKLtkekkaLQEAHQQALDDLQAEEDkvNTL 1022
Cdd:pfam10174 126 ERQAKELFLLRKTLEEMEL---RIETQKQTLGAR-----------DESIKKL------LEMLQSKGLPKKSGEED--WER 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1023 TKSKVKLEQQVDDLEGSLEQEKKVRMDL-ERAKRKLEG--------------DLKLTQESIMDLENDKLQLEEKLKKKEF 1087
Cdd:pfam10174 184 TRRIAEAEMQLGHLEVLLDQKEKENIHLrEELHRRNQLqpdpaktkalqtviEMKDTKISSLERNIRDLEDEVQMLKTNG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1088 DISQQNSKIEDEQALALQLQKKLKENqarieeleeeleaertaraKVEKLRSDLSR---ELEEISERLEEAGGATS---V 1161
Cdd:pfam10174 264 LLHTEDREEEIKQMEVYKSHSKFMKN-------------------KIDQLKQELSKkesELLALQTKLETLTNQNSdckQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1162 QIEMNKKREAEfqkmrRDLEEATLQHEATAAALRKKHADSVaeLGEQIDNLQRvkqkLEKEKSEFKLELDDVtSNMEQII 1241
Cdd:pfam10174 325 HIEVLKESLTA-----KEQRAAILQTEVDALRLRLEEKESF--LNKKTKQLQD----LTEEKSTLAGEIRDL-KDMLDVK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1242 KAKAN-LEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLtrgklsyTQQMEDLKRQ 1320
Cdd:pfam10174 393 ERKINvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERL-------KEQREREDRE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1321 LEEEgkaKNALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKK-----KL 1395
Cdd:pfam10174 466 RLEE---LESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKlenqlKK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1396 AQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKE 1475
Cdd:pfam10174 543 AHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVAN 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1476 ARSLSTELfKLKNAYEESLEHLETFKRENKNLQEEISDLTEqlgeggknvhELEKIRKQLEVEKLEL---QSALEEAEA- 1551
Cdd:pfam10174 623 IKHGQQEM-KKKGAQLLEEARRREDNLADNSQQLQLEELMG----------ALEKTRQELDATKARLsstQQSLAEKDGh 691
|
730 740
....*....|....*....|
gi 255918225 1552 --SLEHEEGKILRAQLEFNQ 1569
Cdd:pfam10174 692 ltNLRAERRKQLEEILEMKQ 711
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
849-1183 |
1.62e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 849 KEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQliKNKI-QLEAKVKEMTER 927
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQ--QEKIeRYQADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 928 LEDEE-------EMNAELTAKKRKLEDECSELKKDIDDL-------------------------------ELTLAKVEKE 969
Cdd:PRK04863 364 LEEQNevveeadEQQEENEARAEAAEEEVDELKSQLADYqqaldvqqtraiqyqqavqalerakqlcglpDLTADNAEDW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 970 KHATENKVKNLTEEMAGL-------DEIIAKLTKEKKALQ---------EAHQQALDDL-QAEEDKVntLTKSKVKLEQQ 1032
Cdd:PRK04863 444 LEEFQAKEQEATEELLSLeqklsvaQAAHSQFEQAYQLVRkiagevsrsEAWDVARELLrRLREQRH--LAEQLQQLRMR 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1033 VDDLEGSLEQEKkvrmDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKkkefDISQQnskIEDEQALALQLQKKLKE 1112
Cdd:PRK04863 522 LSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE----SLSES---VSEARERRMALRQQLEQ 590
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255918225 1113 NQARIEELEEELEAERTARAKVEKLRSDLSRELEEiSERLEEaggatsvQIEMNKKREAEFQKMRRDLEEA 1183
Cdd:PRK04863 591 LQARIQRLAARAPAWLAAQDALARLREQSGEEFED-SQDVTE-------YMQQLLERERELTVERDELAAR 653
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
845-1015 |
1.66e-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: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 845 AETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKiQLEAKVKEM 924
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 925 terledeeemnAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKhatENKVKNLTEEMAGLDEIIAKLTKEKKALQEA 1004
Cdd:COG1579 99 -----------ESLKRRISDLEDEILELMERIEELEEELAELEAEL---AELEAELEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|.
gi 255918225 1005 HQQALDDLQAE 1015
Cdd:COG1579 165 REELAAKIPPE 175
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1448-1922 |
1.75e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 52.92 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1448 QRNFDKI---LAEWKQKYeesqselessqkEARSLSTELFKLKNAY--EESLEHLETFKRENknlqEEISDlteqlgegg 1522
Cdd:PRK04778 24 RKRNYKRideLEERKQEL------------ENLPVNDELEKVKKLNltGQSEEKFEEWRQKW----DEIVT--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1523 knvHELEKIRKQL-EVEKL-------ELQSALEEAEASLEHEEGKILRAQLEFNQIKaEIERKLaekDEEMEQAKRNHlr 1594
Cdd:PRK04778 79 ---NSLPDIEEQLfEAEELndkfrfrKAKHEINEIESLLDLIEEDIEQILEELQELL-ESEEKN---REEVEQLKDLY-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1595 mvDSLQTSLDAETRSRNEALrvkKKMEGDLNEMEIQLSQANRIAS-----EAQKHLKNSQAHLKDTQLQLDDavhanddl 1669
Cdd:PRK04778 150 --RELRKSLLANRFSFGPAL---DELEKQLENLEEEFSQFVELTEsgdyvEAREILDQLEEELAALEQIMEE-------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1670 kenI-AIVERRNNLLQAELEELRAVVEQ-TERSRKLAEQELIETSERVQLLHSQNTSLINQK--KKMESDLTQLQTEVE- 1744
Cdd:PRK04778 217 ---IpELLKELQTELPDQLQELKAGYRElVEEGYHLDHLDIEKEIQDLKEQIDENLALLEELdlDEAEEKNEEIQERIDq 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1745 -----EAVQECRNAEEKAKKAITDAAMMAEELKKEqdTSAHLERMKKN-------------MEQTIKDLQHRLDEAEQiA 1806
Cdd:PRK04778 294 lydilEREVKARKYVEKNSDTLPDFLEHAKEQNKE--LKEEIDRVKQSytlneselesvrqLEKQLESLEKQYDEITE-R 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1807 LKGGKKQLQKLEARVRELENEL---EAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRlqdLVDKLQL-----KVK 1878
Cdd:PRK04778 371 IAEQEIAYSELQEELEEILKQLeeiEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKR---YLEKSNLpglpeDYL 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 255918225 1879 AYKRQAEEAEEQANTNLSKFR----KVQHELDEAEERADIAESQVNKL 1922
Cdd:PRK04778 448 EMFFEVSDEIEALAEELEEKPinmeAVNRLLEEATEDVETLEEETEEL 495
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
982-1870 |
1.85e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 982 EEMAGLDEIIAKLTKEK---KALQEAHQQALDDLQAEEDkvnTLTKSKVKLEQQVDDLEGSL----------EQEKKVRM 1048
Cdd:PRK04863 279 NERRVHLEEALELRRELytsRRQLAAEQYRLVEMARELA---ELNEAESDLEQDYQAASDHLnlvqtalrqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1049 DLERAKRKLEGDLKLTQESimdlENDKLQLEEKLKKKEFDISQQNSKIED-EQALALQLQKKLKENQARieeleeeleae 1127
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEA----DEQQEENEARAEAAEEEVDELKSQLADyQQALDVQQTRAIQYQQAV----------- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1128 rTARAKVEKLRSDLSRELEEISERLEEAggATSVQIEMNKKREAEfQKMRrDLEEATLQHEATAAALRKkhadsvaeLGE 1207
Cdd:PRK04863 421 -QALERAKQLCGLPDLTADNAEDWLEEF--QAKEQEATEELLSLE-QKLS-VAQAAHSQFEQAYQLVRK--------IAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1208 QID--NLQRVKQKLEKEKSEFKLELddvtsnmEQIIKAKANLEKVSRTLEDQANeyrvkleeAQRSLNDFTtQRAKLQTE 1285
Cdd:PRK04863 488 EVSrsEAWDVARELLRRLREQRHLA-------EQLQQLRMRLSELEQRLRQQQR--------AERLLAEFC-KRLGKNLD 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1286 NGELARQL-EEKEALISQLTRGKLSYTQQMEDLKRQLEEegkaknalahalqssrhdcdlLREQYEEeMEAKAELQRvls 1364
Cdd:PRK04863 552 DEDELEQLqEELEARLESLSESVSEARERRMALRQQLEQ---------------------LQARIQR-LAARAPAWL--- 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1365 KANSEVAQWRTkyetdaiQRTEELEEAKKKLAQRLQDAEEAVEAVNAKcSSLEKTKHRLQNEIEDLmvdverSNAAAAAL 1444
Cdd:PRK04863 607 AAQDALARLRE-------QSGEEFEDSQDVTEYMQQLLERERELTVER-DELAARKQALDEEIERL------SQPGGSED 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1445 DKKQRnfdkiLAEwkqkyeesqselessqKEARSLSTELFK---LKNA-YEESL----------EHLETFKRENKNLQEE 1510
Cdd:PRK04863 673 PRLNA-----LAE----------------RFGGVLLSEIYDdvsLEDApYFSALygparhaivvPDLSDAAEQLAGLEDC 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1511 ISDL------TEQLGEGGKNVHELEK------IRKQLEVEKLELQSALEEA--EASLEheegkILRAQLEfnqikaEIER 1576
Cdd:PRK04863 732 PEDLyliegdPDSFDDSVFSVEELEKavvvkiADRQWRYSRFPEVPLFGRAarEKRIE-----QLRAERE------ELAE 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1577 KLAEKDEEMEQAKRNHL---RMVDS-LQTSLDAE--------TRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKH 1644
Cdd:PRK04863 801 RYATLSFDVQKLQRLHQafsRFIGShLAVAFEADpeaelrqlNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRL 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1645 LKNS--------QAHLKDTQLQLDDAVHANDDLKEN---IAIVERRNNLLQA---ELEELRAVVEQTERSRKLAEQELIE 1710
Cdd:PRK04863 881 LPRLnlladetlADRVEEIREQLDEAEEAKRFVQQHgnaLAQLEPIVSVLQSdpeQFEQLKQDYQQAQQTQRDAKQQAFA 960
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1711 TSERVQLLH----SQNTSLINQkkkmESDLT-QLQTEVEEAVQECRNAEEKAKKA---ITDAAMMAEELKKEQDTsahLE 1782
Cdd:PRK04863 961 LTEVVQRRAhfsyEDAAEMLAK----NSDLNeKLRQRLEQAEQERTRAREQLRQAqaqLAQYNQVLASLKSSYDA---KR 1033
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1783 RMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAE---QKRNAES-VKGMRKSERRIKELTYQTEE 1858
Cdd:PRK04863 1034 QMLQELKQELQDLGVPADSGAEERARARRDELHARLSANRSRRNQLEKQltfCEAEMDNlTKKLRKLERDYHEMREQVVN 1113
|
970
....*....|..
gi 255918225 1859 DKKNLMRLQDLV 1870
Cdd:PRK04863 1114 AKAGWCAVLRLV 1125
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
971-1225 |
1.88e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 971 HATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQekkvrmdL 1050
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1051 ERAKRKLEGDLKLTQESIMDLeNDKLQLEEKLKKKEFDISQQNSkieDEQALALQLQKKLkeNQARieeleeeleaerta 1130
Cdd:COG4942 89 EKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDF---LDAVRRLQYLKYL--APAR-------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1131 RAKVEKLRSDLsRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsVAELGEQID 1210
Cdd:COG4942 149 REQAEELRADL-AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE----LAELQQEAE 223
|
250
....*....|....*
gi 255918225 1211 NLQRVKQKLEKEKSE 1225
Cdd:COG4942 224 ELEALIARLEAEAAA 238
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
845-1449 |
1.90e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.42 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 845 AETEKEMANMKEEFGRVKDALEKSEARRKELEEKmvslLQEKND-LQLQVQAEQdnLNDAEERCdqliknkiqlEAKVKE 923
Cdd:COG3096 295 FGARRQLAEEQYRLVEMARELEELSARESDLEQD----YQAASDhLNLVQTALR--QQEKIERY----------QEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 924 MTERLEDEEEMNAELT-------AKKRKLEDECSELKKDIDDL-------------------------------ELTLAK 965
Cdd:COG3096 359 LTERLEEQEEVVEEAAeqlaeaeARLEAAEEEVDSLKSQLADYqqaldvqqtraiqyqqavqalekaralcglpDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 966 VEKEKHATENKVKNLTEEMAGLDE--IIAKLTKEK--KALQ------------EAHQQALD------DLQAEEDKVNTlt 1023
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQklSVADAARRQfeKAYElvckiageversQAWQTAREllrryrSQQALAQRLQQ-- 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1024 kskvkLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLkltqESIMDLENDKLQLEEKLKkkefDISQQnskIEDEQALA 1103
Cdd:COG3096 517 -----LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQL----DAAEELEELLAELEAQLE----ELEEQ---AAEAVEQR 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1104 LQLQKKLKENQARIEELEEELEAERTARAKVEKLRsdlsrelEEISERLEEAGGATS-VQIEMNKKREAEFQKmrrdlEE 1182
Cdd:COG3096 581 SELRQQLEQLRARIKELAARAPAWLAAQDALERLR-------EQSGEALADSQEVTAaMQQLLEREREATVER-----DE 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1183 ATLQHEATAAALRKKHADSVAE------LGEQ---------------------------------IDNLQRVKQKL---- 1219
Cdd:COG3096 649 LAARKQALESQIERLSQPGGAEdprllaLAERlggvllseiyddvtledapyfsalygparhaivVPDLSAVKEQLagle 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1220 -------------------------------------------------------EKEKSEFKLELDDVTsnmEQIIKAK 1244
Cdd:COG3096 729 dcpedlyliegdpdsfddsvfdaeeledavvvklsdrqwrysrfpevplfgraarEKRLEELRAERDELA---EQYAKAS 805
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1245 ANLEKVSRTLED-------------------QANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTr 1305
Cdd:COG3096 806 FDVQKLQRLHQAfsqfvgghlavafapdpeaELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAN- 884
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1306 gkL----SYTQQMEDLKRQLEEEGKAKNALAH-------------ALQSSRHDCDLLREQYEeemEAKAELQRVLSK--A 1366
Cdd:COG3096 885 --LladeTLADRLEELREELDAAQEAQAFIQQhgkalaqleplvaVLQSDPEQFEQLQADYL---QAKEQQRRLKQQifA 959
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1367 NSEVAQWRT--KYEtDAIQRTEELEEAKKKLAQRLQDAE-------EAVEAVNAKCS-------SLeKTKHR-------- 1422
Cdd:COG3096 960 LSEVVQRRPhfSYE-DAVGLLGENSDLNEKLRARLEQAEearrearEQLRQAQAQYSqynqvlaSL-KSSRDakqqtlqe 1037
|
810 820
....*....|....*....|....*..
gi 255918225 1423 LQNEIEDLMVDVErSNAAAAALDKKQR 1449
Cdd:COG3096 1038 LEQELEELGVQAD-AEAEERARIRRDE 1063
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
653-677 |
2.08e-06 |
|
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: 49.65 E-value: 2.08e-06
10 20
....*....|....*....|....*
gi 255918225 653 HRENLNKLMTNLKTTHPHFVRCIIP 677
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
856-1408 |
2.09e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.13 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 856 EEFGRVKDALEKSEarrKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNK--IQLEAKVKEMTERLEDEEE 933
Cdd:TIGR01612 1111 DEINKIKDDIKNLD---QKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDdpEEIEKKIENIVTKIDKKKN 1187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 934 MNAELtakkRKLEDECSELKKDIDDLE---------------LTLAKVEKEKHATENKVKNLTEEMAGLDEIiakltKEK 998
Cdd:TIGR01612 1188 IYDEI----KKLLNEIAEIEKDKTSLEevkginlsygknlgkLFLEKIDEEKKKSEHMIKAMEAYIEDLDEI-----KEK 1258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 999 KALQEAHQQALDDLQAEEDKVNT--------LTKSKVKLEQQVDDLEGSLE--QEKKVRMDLERAKRKLEGDLKLTQE-- 1066
Cdd:TIGR01612 1259 SPEIENEMGIEMDIKAEMETFNIshdddkdhHIISKKHDENISDIREKSLKiiEDFSEESDINDIKKELQKNLLDAQKhn 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1067 --------------SIMDLENDKlQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKEN------QARIEELEEELEA 1126
Cdd:TIGR01612 1339 sdinlylneianiyNILKLNKIK-KIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDinleecKSKIESTLDDKDI 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1127 ERTARaKVEKLRSDLSRELEEISERLEEAGGATS------VQIEMNKKREAEFQKMRRDleEATLQHEATAAALrKKHAD 1200
Cdd:TIGR01612 1418 DECIK-KIKELKNHILSEESNIDTYFKNADENNEnvlllfKNIEMADNKSQHILKIKKD--NATNDHDFNINEL-KEHID 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1201 SVAELGEQIDnlqRVKQKLEKEKSEFKLELDDVTSNMEQ---------IIKAKANLEKVSRTLEDQANEYRVKLEEAQRS 1271
Cdd:TIGR01612 1494 KSKGCKDEAD---KNAKAIEKNKELFEQYKKDVTELLNKysalaiknkFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQK 1570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1272 LNDFTTQRAKLQTENGELARQ-------------LEEKEALISQLTRGKLSYTQQMEDLKRQ------------LEEEGK 1326
Cdd:TIGR01612 1571 IKEIKKEKFRIEDDAAKNDKSnkaaidiqlslenFENKFLKISDIKKKINDCLKETESIEKKissfsidsqdteLKENGD 1650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1327 AKNALAHALQSsrhdcdlLREQYEEEMEAKAELQRVLSKANS---EVAQWRTKYETDAIQRTEELEEAKKklaQRLQDAE 1403
Cdd:TIGR01612 1651 NLNSLQEFLES-------LKDQKKNIEDKKKELDELDSEIEKieiDVDQHKKNYEIGIIEKIKEIAIANK---EEIESIK 1720
|
....*
gi 255918225 1404 EAVEA 1408
Cdd:TIGR01612 1721 ELIEP 1725
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
862-1629 |
2.31e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.13 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 862 KDALEK--SEARRKELEEKMVSLLQEKNDLQLQVQAEQDNL------------NDAEERCDQLIKN----KIQLEAKVKE 923
Cdd:TIGR01612 976 INELDKafKDASLNDYEAKNNELIKYFNDLKANLGKNKENMlyhqfdekekatNDIEQKIEDANKNipniEIAIHTSIYN 1055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 924 MTERLEDEEEMNAELTAKK--RKLEDECSELKKDIDDLEL----TLAKVEKEKHATE-NKVKNlteEMAGLDEIIAKLTK 996
Cdd:TIGR01612 1056 IIDEIEKEIGKNIELLNKEilEEAEINITNFNEIKEKLKHynfdDFGKEENIKYADEiNKIKD---DIKNLDQKIDHHIK 1132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 997 EKKALQEAHQQALDDLQAEEDKVNTLTKSKVkleqQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQEsIMDLENDKL 1076
Cdd:TIGR01612 1133 ALEEIKKKSENYIDEIKAQINDLEDVADKAI----SNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNE-IAEIEKDKT 1207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1077 QLEEkLKKKEFDISQQNSKIEDEQalaLQLQKKLKENQARieeleeeleaertaraKVEKLRSDLSrELEEISERLEEAG 1156
Cdd:TIGR01612 1208 SLEE-VKGINLSYGKNLGKLFLEK---IDEEKKKSEHMIK----------------AMEAYIEDLD-EIKEKSPEIENEM 1266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1157 GatsvqIEMNKKREAEFQKMRRDLEE----ATLQHEATAAALRKKHADSVAELGEQID------NLQRVKQKLEKEKSEF 1226
Cdd:TIGR01612 1267 G-----IEMDIKAEMETFNISHDDDKdhhiISKKHDENISDIREKSLKIIEDFSEESDindikkELQKNLLDAQKHNSDI 1341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1227 KLELDDVTsNMEQIIKakanLEKVSRTLeDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGElARQLEEKEALISQLTRG 1306
Cdd:TIGR01612 1342 NLYLNEIA-NIYNILK----LNKIKKII-DEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD-DINLEECKSKIESTLDD 1414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1307 K--LSYTQQMEDLKRQ-LEEEGKA----KNA-------------LAHALQSSRHDCDLLREQYEEEMEAKA-ELQRVLSK 1365
Cdd:TIGR01612 1415 KdiDECIKKIKELKNHiLSEESNIdtyfKNAdennenvlllfknIEMADNKSQHILKIKKDNATNDHDFNInELKEHIDK 1494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1366 ANsevaqwrtKYETDAIQRTEELEEAKKKLAQRLQDAEEAVE-----AVNAKCSSLEKTKHRLQNEIEDL----MVDVER 1436
Cdd:TIGR01612 1495 SK--------GCKDEADKNAKAIEKNKELFEQYKKDVTELLNkysalAIKNKFAKTKKDSEIIIKEIKDAhkkfILEAEK 1566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1437 SNAAAAALDKKQRNFDKILAewkqKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLetfkRENKNLQEEISDLT- 1515
Cdd:TIGR01612 1567 SEQKIKEIKKEKFRIEDDAA----KNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCL----KETESIEKKISSFSi 1638
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1516 ----EQLGEGGKNVHELEKIRKQLEVEKlelqSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRN 1591
Cdd:TIGR01612 1639 dsqdTELKENGDNLNSLQEFLESLKDQK----KNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKE 1714
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 255918225 1592 HLRMV-DSLQTSLDAETRSRN----EALRVKKKMEGDLNEMEI 1629
Cdd:TIGR01612 1715 EIESIkELIEPTIENLISSFNtndlEGIDPNEKLEEYNTEIGD 1757
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
863-1089 |
2.48e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.32 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 863 DALEKSeaRRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEErcdqliKNKIQLEAKVKEMTERLEDEEEMNAELTakk 942
Cdd:PHA02562 169 DKLNKD--KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRK------KNGENIARKQNKYDELVEEAKTIKAEIE--- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 943 rKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL----------------DEIIAKLTKEKKALQ---E 1003
Cdd:PHA02562 238 -ELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYekggvcptctqqisegPDRITKIKDKLKELQhslE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1004 AHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLK 1083
Cdd:PHA02562 317 KLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
|
....*.
gi 255918225 1084 KKEFDI 1089
Cdd:PHA02562 397 ELVKEK 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1354-1589 |
3.41e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1354 EAKAELQRVLSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMvd 1433
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAE--------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1434 vERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISD 1513
Cdd:COG4942 90 -KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255918225 1514 LTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAK 1589
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1508-1731 |
3.56e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1508 QEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEI---ERKLAEKDEE 1584
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaelEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1585 MEQAKRNHLRMVDSLQTSldaetrSRNEALRVKKKMEgDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVH 1664
Cdd:COG4942 99 LEAQKEELAELLRALYRL------GRQPPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255918225 1665 ANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKK 1731
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1752-1938 |
4.57e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1752 NAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEqIALKGGKKQLQKLEARVRELE---NEL 1828
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEIS-SELPELREELEKLEKEVKELEelkEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1829 EAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQlKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEA 1908
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190
....*....|....*....|....*....|
gi 255918225 1909 EERADIAESQVNKLRAKSRDIGAKKMHDEE 1938
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKE 349
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1393-1898 |
4.92e-06 |
|
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: 51.56 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1393 KKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESS 1472
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1473 QKEARSLSTELFKLKNAYEESLehLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEAS 1552
Cdd:TIGR04523 287 EKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1553 LEHEEGKILRAQLEFNQIKAEIErKLAEKDEEMEQAKRNHLRMVDSLQTSLDaetrsrnealrvKKKMEGDLNEMEIQLS 1632
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIK------------KLQQEKELLEKEIERL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1633 QANRIASEAQ-KHLKNSQAHLKDTQLQLDDAVhanDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIET 1711
Cdd:TIGR04523 432 KETIIKNNSEiKDLTNQDSVKELIIKNLDNTR---ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1712 SERVQLLHSQNTSLINQKKKMESDLTQLQTEVeeavqecRNAEEKAKKaitdaamMAEELKKEQdtsahLERMKKNMEQT 1791
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKI-------SDLEDELNK-------DDFELKKEN-----LEKEIDEKNKE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1792 IKDLQHrldeaEQIALKGGKKQLQklearvrELENELEAEQKrnaESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVD 1871
Cdd:TIGR04523 570 IEELKQ-----TQKSLKKKQEEKQ-------ELIDQKEKEKK---DLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
490 500
....*....|....*....|....*..
gi 255918225 1872 KLQLKVKAYKRQAEEAEEQANTNLSKF 1898
Cdd:TIGR04523 635 NIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1134-1426 |
5.03e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.66 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1134 VEKLRSDLSRELEEISERLEEAggatsvQIEMNKKREAEFQKMRRDLEEATLQHEAT---AAALRKKHADSVAELGEQID 1210
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQE------RLRQEKEEKAREVERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERERELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1211 NLQRVKQKLEKEK---SEFKLELDDVTSNMEQIIKAKANLEKVSRTLEdQANEYRVKLEEAQRSLNDFTTQRAKLQTENg 1287
Cdd:pfam17380 352 RIRQEERKRELERirqEEIAMEISRMRELERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIRAEQ- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1288 ELARQL------EEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEAKAE--- 1358
Cdd:pfam17380 430 EEARQRevrrleEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQami 509
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255918225 1359 --------LQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNE 1426
Cdd:pfam17380 510 eeerkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESE 585
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1479-1697 |
5.40e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1479 LSTELFKLKNAYEESLEHLETFKRENK--NLQEEISDLTEQLGeggknvhELEKIRKQLEVEKLELQSALEEAEASLEHE 1556
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLS-------ELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1557 EGKI--LRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRMVdSLQTSLDA-ETRSRNEALRVKKKMEGDLNEMEIQLSQ 1633
Cdd:COG3206 253 PDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVI-ALRAQIAAlRAQLQQEAQRILASLEAELEALQAREAS 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255918225 1634 ANRIASEAQKHLKNsqahLKDTQLQLddavhanDDLKENIAIVERRNNLLQAELEELRAVVEQT 1697
Cdd:COG3206 332 LQAQLAQLEARLAE----LPELEAEL-------RRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
931-1426 |
6.66e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 931 EEEMNAELTAKKRKLEDECSELKKDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALqEAHQQALD 1010
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1011 DLQAEEDKVNTLTKSKVKLEQqvddlegsLEQEKKVRMDLERAKRKLEGDLKLTQESI-MDLENDKLQLEEKLKKKEFDI 1089
Cdd:COG4717 130 LYQELEALEAELAELPERLEE--------LEERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1090 SQQNSKIEDEQALALQLQKKLKENQARIEELeeeleaertaraKVEKLRSDLSRELEEISERLeeAGGATSVQIEMNKKR 1169
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQL------------ENELEAAALEERLKEARLLL--LIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1170 EAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVK----QKLEKEKSEFKLELDDVTSNMEQIIKAKA 1245
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEeleeEELEELLAALGLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1246 NLEKVSRTLEDQANEYRVKLEEAQRSlNDFTTQRAKLQTENGELARQLEEKEALisqltrgklsyTQQMEDLKRQLEEEG 1325
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEEYQEL-----------KEELEELEEQLEELL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1326 KAKNALAHAlqssrHDCDLLREQYEEEMEAKAELQRVLSKANSEVAqwRTKYETDAIQRTEELEEAKKKLAQRLQDAEEA 1405
Cdd:COG4717 416 GELEELLEA-----LDEEELEEELEELEEELEELEEELEELREELA--ELEAELEQLEEDGELAELLQELEELKAELREL 488
|
490 500
....*....|....*....|....
gi 255918225 1406 VEAVNAKC---SSLEKTKHRLQNE 1426
Cdd:COG4717 489 AEEWAALKlalELLEEAREEYREE 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1670-1927 |
6.76e-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: 51.60 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1670 KENIAIVE--RRNNLLQAELEELRAVVEQ-------TERsRKLAEQELIETSERVQLLHSQNTSLINQKKKMesdltQLQ 1740
Cdd:TIGR02168 135 KRSYSIIEqgKISEIIEAKPEERRAIFEEaagiskyKER-RKETERKLERTRENLDRLEDILNELERQLKSL-----ERQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1741 TEVEEAVQECRNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEAR 1820
Cdd:TIGR02168 209 AEKAERYKELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEELRLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1821 VRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRK 1900
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
250 260
....*....|....*....|....*..
gi 255918225 1901 VQHELDEAEERADIAESQVNKLRAKSR 1927
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLE 382
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
957-1369 |
6.91e-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: 51.38 E-value: 6.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 957 DDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDL-------QAEEDKVN-TLTKSKVK 1028
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLrrlfdekQSEKDKKNkALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1029 LEQQVDDLEGsleQEKKVRMDLERAKRKLEGDLKltqESIMDLENDKLQLEEKLKKKEFDISQQnskIEDEQALALQLQK 1108
Cdd:pfam12128 680 ANERLNSLEA---QLKQLDKKHQAWLEEQKEQKR---EARTEKQAYWQVVEGALDAQLALLKAA---IAARRSGAKAELK 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1109 KLKENQARieeleeeleaERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHE 1188
Cdd:pfam12128 751 ALETWYKR----------DLASLGVDPDVIAKLKREIRTLERKIERI-----------AVRRQEVLRYFDWYQETWLQRR 809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1189 ----ATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEqiiKAKANLEKVSRTLEDQ-ANEYRV 1263
Cdd:pfam12128 810 prlaTQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLR---GLRCEMSKLATLKEDAnSEQAQG 886
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1264 KLEEAQRSLNDFttqRAKLQTENGELARQLEEKEALISQLTRGKLSYTqqMEDLKRQLEEEGKAKNALAHALQSSRHDCD 1343
Cdd:pfam12128 887 SIGERLAQLEDL---KLKRDYLSESVKKYVEHFKNVIADHSGSGLAET--WESLREEDHYQNDKGIRLLDYRKLVPYLEQ 961
|
410 420
....*....|....*....|....*.
gi 255918225 1344 LLREQYEEEMEAKAELQRVLSKANSE 1369
Cdd:pfam12128 962 WFDVRVPQSIMVLREQVSILGVDLTE 987
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1258-1930 |
7.07e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1258 ANEYRVKLEEA---QRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTrgklsytQQMEDLKRQLEeegKAKNALAHA 1334
Cdd:PRK04863 278 ANERRVHLEEAlelRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLE-------QDYQAASDHLN---LVQTALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1335 LQSSRHDCDL--LREQYEEEMEA-------KAELQRVLSKANSEVAQWRTKY----------ETDAIQ------------ 1383
Cdd:PRK04863 348 EKIERYQADLeeLEERLEEQNEVveeadeqQEENEARAEAAEEEVDELKSQLadyqqaldvqQTRAIQyqqavqalerak 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1384 ----------------------RTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKtkhrlqneiedLMVDVERSNAAA 1441
Cdd:PRK04863 428 qlcglpdltadnaedwleefqaKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRK-----------IAGEVSRSEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1442 AALDK-----KQRNFDKILAEWKQKYEESQSELESSqKEARSLSTELFKLKNAYEESLEHLETFKREnknLQEEISDLTE 1516
Cdd:PRK04863 497 VARELlrrlrEQRHLAEQLQQLRMRLSELEQRLRQQ-QRAERLLAEFCKRLGKNLDDEDELEQLQEE---LEARLESLSE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1517 QLGEGGKNVHELEKIRKQL--EVEKLELQS-ALEEAEASLEHeegkiLRAQ-----------LEFNQIKAEIERKLAEKD 1582
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLqaRIQRLAARApAWLAAQDALAR-----LREQsgeefedsqdvTEYMQQLLERERELTVER 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1583 EEMEQAKRNHLRMVDSLQTSLDAE-TRSRNEALRVKKKMEGDLNEmEIQLSQANRIA---------------SEAQKHLK 1646
Cdd:PRK04863 648 DELAARKQALDEEIERLSQPGGSEdPRLNALAERFGGVLLSEIYD-DVSLEDAPYFSalygparhaivvpdlSDAAEQLA 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1647 NSQAHLKDTQL------QLDDAVHANDDLKENI----------------------AIVERRNNLLQAELEELravveqTE 1698
Cdd:PRK04863 727 GLEDCPEDLYLiegdpdSFDDSVFSVEELEKAVvvkiadrqwrysrfpevplfgrAAREKRIEQLRAEREEL------AE 800
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1699 RSRKLAEQelietSERVQLLHSQNTSLINQKKKM------ESDLTQLQT---EVEEAVQECRNAEEKAKKAITDAAMMAE 1769
Cdd:PRK04863 801 RYATLSFD-----VQKLQRLHQAFSRFIGSHLAVafeadpEAELRQLNRrrvELERALADHESQEQQQRSQLEQAKEGLS 875
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1770 ELKKEQDTSAHLERmkKNMEQTIKDLQHRLDEAEQ----IALKGGK-KQLQKLEARVRELENELEAEQKRNAESVKGMRK 1844
Cdd:PRK04863 876 ALNRLLPRLNLLAD--ETLADRVEEIREQLDEAEEakrfVQQHGNAlAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRD 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1845 SERRIKELTY--------QTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAE 1916
Cdd:PRK04863 954 AKQQAFALTEvvqrrahfSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKR 1033
|
810
....*....|....
gi 255918225 1917 SQVNKLRAKSRDIG 1930
Cdd:PRK04863 1034 QMLQELKQELQDLG 1047
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1341-1911 |
7.51e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1341 DCDLLREQYEEEMEAKAELQRVLSKANSE---VAQWRTKYETDAIQRTEELEE------AKKKLAQRLQDAEEAV----E 1407
Cdd:pfam05483 58 DCHYQEGLKDSDFENSEGLSRLYSKLYKEaekIKKWKVSIEAELKQKENKLQEnrkiieAQRKAIQELQFENEKVslklE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1408 AVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTEL-FKL 1486
Cdd:pfam05483 138 EEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMhFKL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1487 KNAYEEsLEHLET-FKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQL--EVEKLELQSALEEAEASLEHEEGKILRA 1563
Cdd:pfam05483 218 KEDHEK-IQHLEEeYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESrdKANQLEEKTKLQDENLKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1564 QLEfnQIKAEIERKLAEK---DEEMEQAKRNHLRMVDSLQTSLDAETRSRNEALRVkkkmegdLNEMEIQLSQANRIASE 1640
Cdd:pfam05483 297 ELE--DIKMSLQRSMSTQkalEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFV-------VTEFEATTCSLEELLRT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1641 AQKHLKNSQAHLKDTQLQLDDAvhaNDDLKEniaiVERRNNLLQAELEELRAVVeqTERSRKLAEQELIET-SERVQLLH 1719
Cdd:pfam05483 368 EQQRLEKNEDQLKIITMELQKK---SSELEE----MTKFKNNKEVELEELKKIL--AEDEKLLDEKKQFEKiAEELKGKE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1720 SQNTSLINQKKK----MESDLTQLQT-------EVEEAVQECRNAEEKAKKAITDAAMMAEELKK-EQDTSAHLERMKKN 1787
Cdd:pfam05483 439 QELIFLLQAREKeihdLEIQLTAIKTseehylkEVEDLKTELEKEKLKNIELTAHCDKLLLENKElTQEASDMTLELKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1788 MEqtikDLQHRLDEAEQIAlkggkKQLQKLEARVRELENELEA---EQKRNAESVK-GMRKSERRIKELTYQTEEDKKNL 1863
Cdd:pfam05483 519 QE----DIINCKKQEERML-----KQIENLEEKEMNLRDELESvreEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQM 589
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255918225 1864 MRLQDL--------------VDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEER 1911
Cdd:pfam05483 590 KILENKcnnlkkqienknknIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK 651
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1155-1384 |
7.73e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1155 AGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAAlRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVT 1234
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1235 SNMEQIIKA----KANLEKVSRTLEDQANEYRVKL-------EEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQL 1303
Cdd:COG4942 90 KEIAELRAEleaqKEELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1304 TRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYETDAIQ 1383
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
.
gi 255918225 1384 R 1384
Cdd:COG4942 250 A 250
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1253-1411 |
8.25e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1253 TLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAK--NA 1330
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1331 LAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVN 1410
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
.
gi 255918225 1411 A 1411
Cdd:COG1579 174 P 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1474-1934 |
8.32e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1474 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASL 1553
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1554 EheegkilraqlefnqiKAEIERKLAEKDEEMEQAKRNHlrmvdslqtsldaetRSRNEALRVKKKMEGDLNEMEIQLSQ 1633
Cdd:COG4717 133 E----------------LEALEAELAELPERLEELEERL---------------EELRELEEELEELEAELAELQEELEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1634 ANRIASEAQKHlknsqaHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSE 1713
Cdd:COG4717 182 LLEQLSLATEE------ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1714 RVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKKNMEQT 1791
Cdd:COG4717 256 AALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1792 IKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAE-QKRNAESVKGMRKS----------ERRIKELTYQTEEDK 1860
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlAEAGVEDEEELRAAleqaeeyqelKEELEELEEQLEELL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1861 KNLMRLQDLVDKLQLKVKA--YKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIA------ESQVNKLRAKSRDIGAK 1932
Cdd:COG4717 416 GELEELLEALDEEELEEELeeLEEELEELEEELEELREELAELEAELEQLEEDGELAellqelEELKAELRELAEEWAAL 495
|
..
gi 255918225 1933 KM 1934
Cdd:COG4717 496 KL 497
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1474-1619 |
1.04e-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: 48.77 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1474 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDL-------TEQLGEGGKN------VHELEKIRKQ---LEV 1537
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearikkyEEQLGNVRNNkeyealQKEIESLKRRisdLED 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1538 EKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNhlrmVDSLQTSLDAETRSRNEALRVK 1617
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE----REELAAKIPPELLALYERIRKR 186
|
..
gi 255918225 1618 KK 1619
Cdd:COG1579 187 KN 188
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
887-1517 |
1.41e-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: 50.44 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 887 NDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMnaELTAKKRKLEDECSELKKDIDDLEltlAKV 966
Cdd:TIGR01612 1486 NELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSAL--AIKNKFAKTKKDSEIIIKEIKDAH---KKF 1560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 967 EKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAhQQALDDLqaeEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKV 1046
Cdd:TIGR01612 1561 ILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDI-QLSLENF---ENKFLKISDIKKKINDCLKETESIEKKISSF 1636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1047 RMDLERAKRKLEGDLKLT-QESIMDLENDKLQLEEKlkKKEFDisQQNSKIEdeqALALQLQKKLKENQARIEELEEEle 1125
Cdd:TIGR01612 1637 SIDSQDTELKENGDNLNSlQEFLESLKDQKKNIEDK--KKELD--ELDSEIE---KIEIDVDQHKKNYEIGIIEKIKE-- 1707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1126 aerTARAKVEKLRSdLSRELEEISERLEEAGGATSVQ-IEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAE 1204
Cdd:TIGR01612 1708 ---IAIANKEEIES-IKELIEPTIENLISSFNTNDLEgIDPNEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITY 1783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1205 lgEQIDNLQRVKQ----KLEKEKSEFKLELDDVTSN-MEQIIKA-KANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQ 1278
Cdd:TIGR01612 1784 --DEIKNTRINAQneflKIIEIEKKSKSYLDDIEAKeFDRIINHfKKKLDHVNDKFTKEYSKINEGFDDISKSIENVKNS 1861
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1279 raklQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEeegKAKNALAHALQSSRhDCDLLREQYEE-----EM 1353
Cdd:TIGR01612 1862 ----TDENLLFDILNKTKDAYAGIIGKKYYSYKDEAEKIFINIS---KLANSINIQIQNNS-GIDLFDNINIAilsslDS 1933
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1354 EAKAELQRVLSKAN-SEV-AQWRTKYET-----DAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNE 1426
Cdd:TIGR01612 1934 EKEDTLKFIPSPEKePEIyTKIRDSYDTlldifKKSQDLHKKEQDTLNIIFENQQLYEKIQASNELKDTLSDLKYKKEKI 2013
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1427 IEDLMVDVERSNAAAAaLDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKN 1506
Cdd:TIGR01612 2014 LNDVKLLLHKFDELNK-LSCDSQNYDTILELSKQDKIKEKIDNYEKEKEKFGIDFDVKAMEEKFDNDIKDIEKFENNYKH 2092
|
650
....*....|.
gi 255918225 1507 LQEEISDLTEQ 1517
Cdd:TIGR01612 2093 SEKDNHDFSEE 2103
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1474-1679 |
1.55e-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: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1474 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASL 1553
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1554 EHEEGKI---LRAQLEFNQ-------IKAEIERKLAEKDEEMEQAKRNHLRMVDSLQTSLDAETRSRNEALRVKKKMEGD 1623
Cdd:COG4942 100 EAQKEELaelLRALYRLGRqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255918225 1624 LNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKENIAIVERR 1679
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1505-1938 |
1.59e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.21 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1505 KNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALE-EAEASLEHEEGKILRAQLEFNQIK-AEIERKLAEKD 1582
Cdd:pfam10174 174 KKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHrRNQLQPDPAKTKALQTVIEMKDTKiSSLERNIRDLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1583 EEmeqakrnhlrmVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDA 1662
Cdd:pfam10174 254 DE-----------VQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDC 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1663 VHANDDLKENIAIVERRNNLLQAELEELRAVVEQ-----TERSRKLAE---------------QELIETSER-VQLLHSQ 1721
Cdd:pfam10174 323 KQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEkesflNKKTKQLQDlteekstlageirdlKDMLDVKERkINVLQKK 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1722 NTSLINQKKKMESDLTQLQTEVEEAVQECRNAEekakkaiTDAAMMAEELKKEQDTsahLERMKknmEQTIKDLQHRLDE 1801
Cdd:pfam10174 403 IENLQEQLRDKDKQLAGLKERVKSLQTDSSNTD-------TALTTLEEALSEKERI---IERLK---EQREREDRERLEE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1802 AEQI--ALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQlkvka 1879
Cdd:pfam10174 470 LESLkkENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH----- 544
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1880 ykrQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKKmHDEE 1938
Cdd:pfam10174 545 ---NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEK-NDKD 599
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1498-1853 |
1.70e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.51 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1498 ETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQsalEEAEASLEHEEGKILRAQLEFNQIKAEIERK 1577
Cdd:pfam07888 69 EQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS---EEKDALLAQRAAHEARIRELEEDIKTLTQRV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1578 LaEKDEEMEQAKRNHLRMVDSLQtsldaETRSRNEALRVKkkmegdlneMEIQLSQANRIASEAQKhLKNSQAHLKDTQL 1657
Cdd:pfam07888 146 L-ERETELERMKERAKKAGAQRK-----EEEAERKQLQAK---------LQQTEEELRSLSKEFQE-LRNSLAQRDTQVL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1658 QLDDAVHAnddLKENIAIVERRNNLLQAELEELRAVveqtersrklaeQELIETSER-VQLLHSQNTSLINQKKKMESDL 1736
Cdd:pfam07888 210 QLQDTITT---LTQKLTTAHRKEAENEALLEELRSL------------QERLNASERkVEGLGEELSSMAAQRDRTQAEL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1737 TQLQTEVEE----------AVQECRNAEEKAKKAITDAAMMAEElkKEQDTSAHLERMKKNMEQTIKDLQH------RLD 1800
Cdd:pfam07888 275 HQARLQAAQltlqladaslALREGRARWAQERETLQQSAEADKD--RIEKLSAELQRLEERLQEERMEREKlevelgREK 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1801 EAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELT 1853
Cdd:pfam07888 353 DCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
920-1533 |
1.73e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 920 KVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT---K 996
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSsleD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 997 EKKALQEAHQQALDDLQAEEDKVNtltkskvkleqqvdDLEGSLEQEKKVRMDLERAKRklegdlkltqESIMDLENDKL 1076
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNN--------------YYKELEERHMKIINDPVYKNR----------NYINDYFKYKN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1077 QLEEKLKKKEfDISQQNSKIEDeqalalqLQKKLKENQArieeleeeleaERTARAKVEKLRSDLSRELEEISERLEEAG 1156
Cdd:PRK01156 306 DIENKKQILS-NIDAEINKYHA-------IIKKLSVLQK-----------DYNDYIKKKSRYDDLNNQILELEGYEMDYN 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1157 GATSVQIEMNKKREAEFQKMRR---DLEEATLQHEATAAALRKKHadsvAELGEQIDNLQRVKQKLEKEKSEFKLELDDV 1233
Cdd:PRK01156 367 SYLKSIESLKKKIEEYSKNIERmsaFISEILKIQEIDPDAIKKEL----NEINVKLQDISSKVSSLNQRIRALRENLDEL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1234 TSNMEqIIKAKANLEKVSRTLEDQANEYRVKL--EEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYT 1311
Cdd:PRK01156 443 SRNME-MLNGQSVCPVCGTTLGEEKSNHIINHynEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEY 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1312 QQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEAKAElqrVLSKANSEvaqwRTKYETDAIQ-RTEELEE 1390
Cdd:PRK01156 522 NKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRT---SWLNALAV----ISLIDIETNRsRSNEIKK 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1391 AKKKLAQRLQDAEEAVEAVNakcSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELE 1470
Cdd:PRK01156 595 QLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE 671
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1471 SSQKeARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRK 1533
Cdd:PRK01156 672 ITSR-INDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1380-1925 |
2.01e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1380 DAIQRTEELEEAKKKLaqrlqdaEEAVEAVNAKCSSLEKTKHRLQNEIEDlmvdVERSNAAAAALDKKQRNFDKILAEWK 1459
Cdd:PRK01156 156 DEILEINSLERNYDKL-------KDVIDMLRAEISNIDYLEEKLKSSNLE----LENIKKQIADDEKSHSITLKEIERLS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1460 QKYEESQSELESSQKEARSLSTeLFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGE--GGKNVHELEKIRKQLEV 1537
Cdd:PRK01156 225 IEYNNAMDDYNNLKSALNELSS-LEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiiNDPVYKNRNYINDYFKY 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1538 EK--LELQSALEEAEASLEHEEGKILRAQlEFNQIKAEIERKLAEKDE------EMEQAKRNHLRMVDSLQTSLDAETRS 1609
Cdd:PRK01156 304 KNdiENKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKKSRYDDlnnqilELEGYEMDYNSYLKSIESLKKKIEEY 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1610 RNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKENIAIVERRN--------- 1680
Cdd:PRK01156 383 SKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttl 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1681 ---------NLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTS-LINQKKKMESDLTQLqTEVEEAVQEC 1750
Cdd:PRK01156 463 geeksnhiiNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADL-EDIKIKINEL 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1751 RNAEEKAKKAITDAAMMAEELKKEQDTSaHLERMKKNMEQTIKDLQHRLDEAeqialkggKKQLQKLEARVRELENELEA 1830
Cdd:PRK01156 542 KDKHDKYEEIKNRYKSLKLEDLDSKRTS-WLNALAVISLIDIETNRSRSNEI--------KKQLNDLESRLQEIEIGFPD 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1831 EQKRNAESVKGMrKSERRIKELTYQTEEDKKNLMrlqdlvDKLQLKVKAYKRQA---EEAEEQANTNLSKFRKVQHELDE 1907
Cdd:PRK01156 613 DKSYIDKSIREI-ENEANNLNNKYNEIQENKILI------EKLRGKIDNYKKQIaeiDSIIPDLKEITSRINDIEDNLKK 685
|
570
....*....|....*...
gi 255918225 1908 AEERADIAESQVNKLRAK 1925
Cdd:PRK01156 686 SRKALDDAKANRARLEST 703
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1543-1932 |
2.22e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1543 QSALEEAEASLEHEEGKILRAQLefnqikAEIERKLAEKDEEMEQAKRNHLRMVDSLQTSLD--AETRSRNEALRVkkkM 1620
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKDLHERL------NGLESELAELDEEIERYEEQREQARETRDEADEvlEEHEERREELET---L 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1621 EGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRAVVEQTERS 1700
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1701 RKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVE---EAVQECRNAEEKAKKAITDAAmmaEELKKEQDT 1777
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEdrrEEIEELEEEIEELRERFGDAP---VDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1778 SAHLERMKKNMEQTIKDLqhrldEAEqialkggkkqLQKLEARVRELENELEA-------EQKRNAESVKGMRKSERRIK 1850
Cdd:PRK02224 414 LEELREERDELREREAEL-----EAT----------LRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1851 ELTYQTEEDKKNLMRLQDLVDKLQlkvkaykrQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIG 1930
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
..
gi 255918225 1931 AK 1932
Cdd:PRK02224 551 AE 552
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
842-1096 |
2.39e-05 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 49.39 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 842 LKSAETEKEMANMKEEFGRVKDALEKSEARR----KELEEKMVSLLQEKNDLQLQVQAeqdnlNDAEERCDQLIKNKIQL 917
Cdd:pfam18971 596 FNKAVAEAKSTGNYDEVKKAQKDLEKSLRKRehleKEVEKKLESKSGNKNKMEAKAQA-----NSQKDEIFALINKEANR 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 918 EAKVKEMTERLEDeeeMNAELTAKKRKLEDECSELKKDIDDLE----LTLAKVEKEKHATENKVKNLteemaGLD-EIIA 992
Cdd:pfam18971 671 DARAIAYTQNLKG---IKRELSDKLEKISKDLKDFSKSFDEFKngknKDFSKAEETLKALKGSVKDL-----GINpEWIS 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 993 KLTKEKKALQEAHQQALDDL----QAEEDKVNTLtkSKVKLEQQVDDLEGSLEQEKKVrmdlerakRKLEGDLKLTQESI 1068
Cdd:pfam18971 743 KVENLNAALNEFKNGKNKDFskvtQAKSDLENSV--KDVIINQKVTDKVDNLNQAVSV--------AKAMGDFSRVEQVL 812
|
250 260
....*....|....*....|....*....
gi 255918225 1069 MDLEN-DKLQLEEKLKKKEFDISQQNSKI 1096
Cdd:pfam18971 813 ADLKNfSKEQLAQQAQKNEDFNTGKNSEL 841
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1746-1931 |
2.50e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1746 AVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELE 1825
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-ELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1826 NELEAEQKRNAESVKGMRKSERR---------------IKELTY----------QTEEDKKNLMRLQDLVDKLQLKVKAY 1880
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQpplalllspedfldaVRRLQYlkylaparreQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255918225 1881 KRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGA 1931
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
923-1338 |
2.53e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.91 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 923 EMTERLEDEEEMNAELTAKKRKLEDECSEL---KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKK 999
Cdd:pfam19220 14 EMADRLEDLRSLKADFSQLIEPIEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1000 ALQEAHQQAldDLQAEEDKVNTLTKskvklEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLE 1079
Cdd:pfam19220 94 KLEAALREA--EAAKEELRIELRDK-----TAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1080 EKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARieeleeeleaERTARAKVEKLRSDLSRELEEiSERLEEAggat 1159
Cdd:pfam19220 167 ERLALLEQENRRLQALSEEQAAELAELTRRLAELETQ----------LDATRARLRALEGQLAAEQAE-RERAEAQ---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1160 svqiemnkkreaefqkmrRDLEEATLQHEATAAALRKKHADSVAELGEQIdnLQRVKQKLeKEKSEfklELDDVTSNMEQ 1239
Cdd:pfam19220 232 ------------------LEEAVEAHRAERASLRMKLEALTARAAATEQL--LAEARNQL-RDRDE---AIRAAERRLKE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1240 IIKAKANLEKVSRTLEDQANEYRVKLEEAQRslndfttQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKR 1319
Cdd:pfam19220 288 ASIERDTLERRLAGLEADLERRTQQFQEMQR-------ARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTK 360
|
410
....*....|....*....
gi 255918225 1320 QLEEEGKAKNALAHALQSS 1338
Cdd:pfam19220 361 RFEVERAALEQANRRLKEE 379
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1486-1937 |
2.58e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1486 LKNAYEESLEHLETFK-RENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEvEKLELQSALEEAEASLEHEEGKILRAQ 1564
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1565 --LEFNQIKAEIERKLAEKDEEMEQAKRNHlrmvdslqtsldaetRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQ 1642
Cdd:COG4717 126 qlLPLYQELEALEAELAELPERLEELEERL---------------EELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1643 KHlknsqaHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQN 1722
Cdd:COG4717 191 EE------ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1723 TSLINQKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKKNMEQTIKDLQHRLD 1800
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1801 EAEQIalkggKKQLQKLEARVRELE-NELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNlmRLQDLVDKLQLKVKA 1879
Cdd:COG4717 345 RIEEL-----QELLREAEELEEELQlEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKE--ELEELEEQLEELLGE 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 255918225 1880 YKRQAEEAEEQANTnlSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKKMHDE 1937
Cdd:COG4717 418 LEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1475-1831 |
2.67e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.91 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1475 EARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLE 1554
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1555 HEEGKILRAQLEFNQ---IKAEIERKLAEKDEEME------QAKRNHLRMVDSLQTSLDAETRSRNEALRV----KKKME 1621
Cdd:pfam19220 101 EAEAAKEELRIELRDktaQAEALERQLAAETEQNRaleeenKALREEAQAAEKALQRAEGELATARERLALleqeNRRLQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1622 GDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLddaVHANDDLKENIAIVERRNNLLQAE-------LEELRAVV 1694
Cdd:pfam19220 181 ALSEEQAAELAELTRRLAELETQLDATRARLRALEGQL---AAEQAERERAEAQLEEAVEAHRAEraslrmkLEALTARA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1695 EQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQEcRNAEEKAKKAITD-AAMMAEELKk 1773
Cdd:pfam19220 258 AATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQ-FQEMQRARAELEErAEMLTKALA- 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 255918225 1774 eqDTSAHLERMkknmEQTIKDLQHRLDEAEQIALKggkkQLQKLEARVRELENELEAE 1831
Cdd:pfam19220 336 --AKDAALERA----EERIASLSDRIAELTKRFEV----ERAALEQANRRLKEELQRE 383
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1286-1625 |
2.86e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.31 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1286 NGELARQLEEKEALISQ--LTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQssrhdcdlLREQYEEEMEAKAE--LQR 1361
Cdd:COG5022 779 HGFRLRRLVDYELKWRLfiKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKK--------LRETEEVEFSLKAEvlIQK 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1362 VLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLaQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIE-DLMVDVERSNAA 1440
Cdd:COG5022 851 FGRSLKAKKRFSLLKKETIYLQSAQRVELAERQL-QELKIDVKSISSLKLVNLELESEIIELKKSLSsDLIENLEFKTEL 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1441 AAALDKKQRNFDKILAEWKQKYEESQSELESSQKeaRSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGE 1520
Cdd:COG5022 930 IARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVE--SKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQ 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1521 GGKnVHELEKIRKQLEVEKLELQSAleEAEASLEHEEGKILR--AQLEFNQIKAeiERKLAEKDEEMEQAKRNHLRmvDS 1598
Cdd:COG5022 1008 YGA-LQESTKQLKELPVEVAELQSA--SKIISSESTELSILKplQKLKGLLLLE--NNQLQARYKALKLRRENSLL--DD 1080
|
330 340
....*....|....*....|....*..
gi 255918225 1599 LQTSLDAETRSRNEALRVKKKMEGDLN 1625
Cdd:COG5022 1081 KQLYQLESTENLLKTINVKDLEVTNRN 1107
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
936-1160 |
2.97e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 936 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAE 1015
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1016 EDKVNTLT-----KSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDIS 1090
Cdd:COG3883 99 GGSVSYLDvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1091 QQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATS 1160
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
893-1115 |
3.32e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 893 VQAEqDNLNDAEERCDQLIKNKIQLEAKVKEMTERLEdeeemnaELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHA 972
Cdd:COG3883 12 AFAD-PQIQAKQKELSELQAELEAAQAELDALQAELE-------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 973 TENKVKNLTEEM----------------AGLDEIIAKLTKEKKaLQEAHQQALDDLQAEedkvntltksKVKLEQQVDDL 1036
Cdd:COG3883 84 RREELGERARALyrsggsvsyldvllgsESFSDFLDRLSALSK-IADADADLLEELKAD----------KAELEAKKAEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1037 EGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQA 1115
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1383-1613 |
3.51e-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: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1383 QRTEELEEAKKKLAQ---RLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWK 1459
Cdd:COG4942 24 EAEAELEQLQQEIAElekELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1460 QKYeesQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLgeggknvHELEKIRKQLEVEK 1539
Cdd:COG4942 104 EEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-------AELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255918225 1540 LELQSALEEAEAslehEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRMVDSLQtSLDAETRSRNEA 1613
Cdd:COG4942 174 AELEALLAELEE----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA-RLEAEAAAAAER 242
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
873-1225 |
3.64e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 873 KELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSEL 952
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 953 KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQ 1032
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1033 VDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKE 1112
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1113 NQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1192
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350
....*....|....*....|....*....|...
gi 255918225 1193 ALRKKHADSVAELGEQIDNLQRVKQKLEKEKSE 1225
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1630-1838 |
3.85e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1630 QLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRA-VVEQTERSRKLAEQEL 1708
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1709 IE---TSERVQLLHSQNTS-LINQKKKMeSDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsahLERM 1784
Cdd:COG3883 97 RSggsVSYLDVLLGSESFSdFLDRLSAL-SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE------LEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255918225 1785 KKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENELEAEQKRNAES 1838
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSA--------EEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1280-1649 |
3.95e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.35 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1280 AKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEAKAEL 1359
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1360 qrvlskanSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSna 1439
Cdd:pfam07888 114 --------SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT-- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1440 aaaaldkkqrnfdkilaewkqkyeesqselessQKEARSLSTELFKLKNAYEESLEHLETfkrenknLQEEISDLTEQLG 1519
Cdd:pfam07888 184 ---------------------------------EEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1520 EGGKNVHELEKIRKQL---------------------------------EVEKLELQSA---LEEAEASLEHEEGKILRA 1563
Cdd:pfam07888 224 TAHRKEAENEALLEELrslqerlnaserkveglgeelssmaaqrdrtqaELHQARLQAAqltLQLADASLALREGRARWA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1564 QlefnqiKAEIERKLAEKDEE-MEQAKRNHLRMVDSLQtsldaETRSRNEALRVKKKMEGDLNemEIQLSQANRIASEAQ 1642
Cdd:pfam07888 304 Q------ERETLQQSAEADKDrIEKLSAELQRLEERLQ-----EERMEREKLEVELGREKDCN--RVQLSESRRELQELK 370
|
....*..
gi 255918225 1643 KHLKNSQ 1649
Cdd:pfam07888 371 ASLRVAQ 377
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
847-1117 |
4.56e-05 |
|
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: 48.60 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 847 TEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDN--LNDAEERCDQLIKNKIQLEAKVKEm 924
Cdd:pfam09731 159 VKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPplLDAAPETPPKLPEHLDNVEEKVEK- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 925 TERLEDEEEMNAELTAKKRklEDECSELKKDIDDLELTLAKVEKEKHATENKVknLTEEMAGLDEIIAKLTKEKKALQEA 1004
Cdd:pfam09731 238 AQSLAKLVDQYKELVASER--IVFQQELVSIFPDIIPVLKEDNLLSNDDLNSL--IAHAHREIDQLSKKLAELKKREEKH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1005 HQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESImdleNDKLQLEEKLKK 1084
Cdd:pfam09731 314 IERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAH----EEHLKDVLVEQE 389
|
250 260 270
....*....|....*....|....*....|....*.
gi 255918225 1085 KEFDISQQ---NSKIEDEQALalqLQKKLKENQARI 1117
Cdd:pfam09731 390 IELQREFLqdiKEKVEEERAG---RLLKLNELLANL 422
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1434-1836 |
4.72e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1434 VERSNAAAAALDKKQRNFDKILAEwKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEhLETFKRENKNLQEEISD 1513
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1514 LTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHL 1593
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1594 RMVDSLQTSLDAETRSRNEAL------------RVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDD 1661
Cdd:COG4717 231 QLENELEAAALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1662 AVHANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQ--ELIETSERVQLLHSQNTSLINQKKKMESDLTQL 1739
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaeELEEELQLEELEQEIAALLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1740 QTEVEEAVQ---ECRNAEEKAKKAITDAAMMAEELKKEQ--DTSAHLERMKKNMEQTIKDLQHRLDEAE-QIALKGGKKQ 1813
Cdd:COG4717 391 LEQAEEYQElkeELEELEEQLEELLGELEELLEALDEEEleEELEELEEELEELEEELEELREELAELEaELEQLEEDGE 470
|
410 420
....*....|....*....|...
gi 255918225 1814 LQKLEARVRELENELEAEQKRNA 1836
Cdd:COG4717 471 LAELLQELEELKAELRELAEEWA 493
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1735-1933 |
5.29e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1735 DLTQLQTEVEEAvQECRNAEEKAKKAitdaammAEELKKEQDTSAHLERMKK-----NMEQTIKDLQHRLDEAEQiALKG 1809
Cdd:COG4913 236 DLERAHEALEDA-REQIELLEPIREL-------AERYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRA-ELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1810 GKKQLQKLEARVRELENEL-EAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKV----KAYKRQA 1884
Cdd:COG4913 307 LEAELERLEARLDALREELdELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLpasaEEFAALR 386
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 255918225 1885 EEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKK 1933
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1191-1590 |
5.30e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.41 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1191 AAALRKKHADSVAELGEQIDNLQRVKQKL-EKEKSEFKLELDDVTSN--MEQIIKAKANLEKVSRTLEDQAnEYRVKLEE 1267
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELeELSARESDLEQDYQAASdhLNLVQTALRQQEKIERYQEDLE-ELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1268 AQRSLNDFTTQRAKLQTENgELARqlEEKEALISQLTrgklsytqqmeDLKRQLEEegkaknalahalQSSRhdcdllRE 1347
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARL-EAAE--EEVDSLKSQLA-----------DYQQALDV------------QQTR------AI 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1348 QYEEEMEAKAELQRVLSKAN---SEVAQWRTKYETDAIQRTEELEEakkkLAQRLQDAEEAveavnakcssleKTKHRLQ 1424
Cdd:COG3096 414 QYQQAVQALEKARALCGLPDltpENAEDYLAAFRAKEQQATEEVLE----LEQKLSVADAA------------RRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1425 NEIEDLMVD-VERSNA--AAAALDKKQRNFdKILAE----WKQKYEESQSELESSqKEARSLSTELFKLKNAYEESLEHL 1497
Cdd:COG3096 478 YELVCKIAGeVERSQAwqTARELLRRYRSQ-QALAQrlqqLRAQLAELEQRLRQQ-QNAERLLEEFCQRIGQQLDAAEEL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1498 ETFKREnknLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQS------ALEEAEASLEHEEGKIL---RAQLEFN 1568
Cdd:COG3096 556 EELLAE---LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArapawlAAQDALERLREQSGEALadsQEVTAAM 632
|
410 420
....*....|....*....|..
gi 255918225 1569 QIKAEIERKLAEKDEEMEQAKR 1590
Cdd:COG3096 633 QQLLEREREATVERDELAARKQ 654
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1141-1793 |
6.59e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1141 LSRELEEISERLEEaggaTSVQIEMNKKR-EAEFQKMRRDLEeaTLQHEATAAALRKKHADSVAELGE---QIDNLQRVK 1216
Cdd:pfam10174 128 QAKELFLLRKTLEE----MELRIETQKQTlGARDESIKKLLE--MLQSKGLPKKSGEEDWERTRRIAEaemQLGHLEVLL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1217 QKLEKEKSEFKLEL---------DDVTSNMEQIIKAK----ANLEKVSRTLEDQAN-------------EYRVKLEEAQR 1270
Cdd:pfam10174 202 DQKEKENIHLREELhrrnqlqpdPAKTKALQTVIEMKdtkiSSLERNIRDLEDEVQmlktngllhtedrEEEIKQMEVYK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1271 SLNDFttqrakLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLE---EEGKAKNALAHALQSsrhDCDLLRE 1347
Cdd:pfam10174 282 SHSKF------MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEvlkESLTAKEQRAAILQT---EVDALRL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1348 QYEEEmeakaelQRVLSKansevaqwrtkyETDAIQRteeLEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEI 1427
Cdd:pfam10174 353 RLEEK-------ESFLNK------------KTKQLQD---LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1428 EDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKyEESQSELESSQKEARSLSTElfklknayeESLEHLETFKRENKNL 1507
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEA-LSEKERIIERLKEQREREDR---------ERLEELESLKKENKDL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1508 QEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEH--EEGKILRAQLEFNQIKAEIERK---LAEKD 1582
Cdd:pfam10174 481 KEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQkkEECSKLENQLKKAHNAEEAVRTnpeINDRI 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1583 EEMEQAKRNHLRMVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDA 1662
Cdd:pfam10174 561 RLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEE 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1663 VHANDDlkeniaivERRNNLLQAELEELRAVVEQTersrklaEQELIETSERV----QLLHSQNTSLIN----QKKKMEs 1734
Cdd:pfam10174 641 ARRRED--------NLADNSQQLQLEELMGALEKT-------RQELDATKARLsstqQSLAEKDGHLTNlraeRRKQLE- 704
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1735 dltqlqtEVEEAVQECRNAEEKAKKA-ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIK 1793
Cdd:pfam10174 705 -------EILEMKQEALLAAISEKDAnIALLELSSSKKKKTQEEVMALKREKDRLVHQLK 757
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1399-1830 |
7.38e-05 |
|
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: 47.76 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1399 LQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDkkqrNFDKILAEWKQKYEESQselessqKEARS 1478
Cdd:pfam05622 2 LSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLE----SGDDSGTPGGKKYLLLQ-------KQLEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1479 LSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLT-------------------------------------EQLGEG 1521
Cdd:pfam05622 71 LQEENFRLETARDDYRIKCEELEKEVLELQHRNEELTslaeeaqalkdemdilressdkvkkleatvetykkklEDLGDL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1522 GKNVHELEK---------------------IRKQLEVEKLELQsaleEAEASLEHEEGKILRAQLEFNQIKA-------E 1573
Cdd:pfam05622 151 RRQVKLLEErnaeymqrtlqleeelkkanaLRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKLEEklealqkE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1574 IERKLAEKD---EEMEQAKRNHLRMVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKhlKNSQA 1650
Cdd:pfam05622 227 KERLIIERDtlrETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQE--GSYRE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1651 HLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRavveqtersRKLAEQElietservqllhSQNTSLINQKK 1730
Cdd:pfam05622 305 RLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQ---------KALQEQG------------SKAEDSSLLKQ 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1731 KMESDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---TIKDLQHRLDEA 1802
Cdd:pfam05622 364 KLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPA 443
|
490 500
....*....|....*....|....*...
gi 255918225 1803 EQIALKGGKKQLQKLEARVRELENELEA 1830
Cdd:pfam05622 444 SPPEIQALKNQLLEKDKKIEHLERDFEK 471
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1050-1204 |
7.86e-05 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 47.83 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1050 LERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKkefdISQQNSKIEDEQALALQLQKKLKENQARIEELeeeleaert 1129
Cdd:COG1193 502 IERARELLGEESIDVEKLIEELERERRELEEEREE----AERLREELEKLREELEEKLEELEEEKEEILEK--------- 568
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255918225 1130 ARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAE 1204
Cdd:COG1193 569 AREEAEEILREARKEAEELIRELREA-----------QAEEEELKEARKKLEELKQELEEKLEKPKKKAKPAKPP 632
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1238-1886 |
9.37e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.49 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1238 EQIIKAKANLEKvsrtLEDQANEYRVKLEEAQRSLNdfTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDL 1317
Cdd:PRK10246 191 EQHKSARTELEK----LQAQASGVALLTPEQVQSLT--ASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1318 KRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANS------EVAQWRTKYETDAIQRTEELEEA 1391
Cdd:PRK10246 265 ALQQALAAEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEvntrlqSTMALRARIRHHAAKQSAELQAQ 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1392 KKKLAQRLQDAE------EAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNA------------AAAALDK--KQRNF 1451
Cdd:PRK10246 345 QQSLNTWLAEHDrfrqwnNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltadeVAAALAQhaEQRPL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1452 DKILAEWKQKYEESQSELESSQKEARSLSTELFKLKnayeeslEHLETFKRENKNLQEEISDLteqlgeggKNVHELEKI 1531
Cdd:PRK10246 425 RQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRN-------AALNEMRQRYKEKTQQLADV--------KTICEQEAR 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1532 RKQLEVEKLELQS-------------------------------ALEEAEASLEhEEGKILRAQLE--FNQIK------- 1571
Cdd:PRK10246 490 IKDLEAQRAQLQAgqpcplcgstshpaveayqalepgvnqsrldALEKEVKKLG-EEGAALRGQLDalTKQLQrdeseaq 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1572 --AEIERKLAEKDEEMEQAKRNHLRMVDSLQTSLDAETRSRNE--ALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKN 1647
Cdd:PRK10246 569 slRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQlrLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLT 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1648 SQAHLKDTQLQLDDA---VHANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTS 1724
Cdd:PRK10246 649 ALAGYALTLPQEDEEaswLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLS 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1725 LINQKKKMESDLTQLQTEVEEAVQECRNAEEK---AKKAITDAAMMAEElkkeqdTSAHLERMKKNMEQTIKDLQHRLDE 1801
Cdd:PRK10246 729 LHSQLQTLQQQDVLEAQRLQKAQAQFDTALQAsvfDDQQAFLAALLDEE------TLTQLEQLKQNLENQRQQAQTLVTQ 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1802 AEQialkggkKQLQKLEARVRELENELEAE--QKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVdklqLKVKA 1879
Cdd:PRK10246 803 TAQ-------ALAQHQQHRPDGLDLTVTVEqiQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALM----QQIAQ 871
|
....*..
gi 255918225 1880 YKRQAEE 1886
Cdd:PRK10246 872 ATQQVED 878
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1088-1302 |
1.05e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1088 DISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEaggatsvqiemnk 1167
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1168 kREAEFQKMRRDLEEATLQHEATAAALrkkHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANL 1247
Cdd:COG3883 84 -RREELGERARALYRSGGSVSYLDVLL---GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255918225 1248 EKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQ 1302
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
845-1251 |
1.12e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.81 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 845 AETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEM 924
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 925 TERLEdeeemnaELTAKKRKLEDECSelkkdidDLELTLAKVEKEKHatenkvknlteemagldeiiaKLTKEKKALQEA 1004
Cdd:pfam07888 156 KERAK-------KAGAQRKEEEAERK-------QLQAKLQQTEEELR---------------------SLSKEFQELRNS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1005 HQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGdlkLTQE-SIMDLENDKLQLEekLK 1083
Cdd:pfam07888 201 LAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG---LGEElSSMAAQRDRTQAE--LH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1084 KKEFDISQQNSKIEDeqaLALQLqkklkenqarieeleeeleaeRTARAKVEKLRSDLSRELEEISERLEeaggatsvqi 1163
Cdd:pfam07888 276 QARLQAAQLTLQLAD---ASLAL---------------------REGRARWAQERETLQQSAEADKDRIE---------- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1164 emnkKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKL---EKEKSEFKLELDDVtsnMEQI 1240
Cdd:pfam07888 322 ----KLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLrvaQKEKEQLQAEKQEL---LEYI 394
|
410
....*....|.
gi 255918225 1241 IKAKANLEKVS 1251
Cdd:pfam07888 395 RQLEQRLETVA 405
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1689-1873 |
1.15e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1689 ELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAEEKAKK---AITDAA 1765
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1766 MMAEELKKE--------------QDTSAHLERMKKNMEQtIKDLQHRLDEAE--QIALKGGKKQLQKLEARVRELENELE 1829
Cdd:PHA02562 269 SKIEQFQKVikmyekggvcptctQQISEGPDRITKIKDK-LKELQHSLEKLDtaIDELEEIMDEFNEQSKKLLELKNKIS 347
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 255918225 1830 AEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKL 1873
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1599-1934 |
1.20e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.20 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1599 LQTSLDAETRSRNEALR----VKKKMEGDLNEMEIQLSQANR-IASEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKENI 1673
Cdd:PLN02939 65 LQSNTDENGQLENTSLRtvmeLPQKSTSSDDDHNRASMQRDEaIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1674 AIVER--------------RNNLLQAELEELRAVVEQTERSRKLAEQELIetseRVQLLHSQntsLINQKKKMESDLTQL 1739
Cdd:PLN02939 145 LLLNQarlqaledlekiltEKEALQGKINILEMRLSETDARIKLAAQEKI----HVEILEEQ---LEKLRNELLIRGATE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1740 QTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTS---AHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQK 1816
Cdd:PLN02939 218 GLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDC 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1817 LEARVRELENELEAEQKRNAESV---KGMRKSERRIKELTYQTEEDKKNLMRLQdLVDKLQLKVKAYKRQAEEAEEQANT 1893
Cdd:PLN02939 298 WWEKVENLQDLLDRATNQVEKAAlvlDQNQDLRDKVDKLEASLKEANVSKFSSY-KVELLQQKLKLLEERLQASDHEIHS 376
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 255918225 1894 nlskfrKVQHELDEAEERADIAESQVNKLRAKSRDIGAKKM 1934
Cdd:PLN02939 377 ------YIQLYQESIKEFQDTLSKLKEESKKRSLEHPADDM 411
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1058-1292 |
1.21e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1058 EGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEEleeeleaertARAKVEKL 1137
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE----------AEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1138 RSDLSRELEEISERLEEAG------GATSV-----QIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsVAELG 1206
Cdd:COG3883 85 REELGERARALYRSGGSVSyldvllGSESFsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAK----LAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1207 EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTEN 1286
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
....*.
gi 255918225 1287 GELARQ 1292
Cdd:COG3883 241 AAAASA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
845-1016 |
1.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 845 AETEKEMANMKEEfgrVKDALEKSEARRKELEEKMVSLLQEKNDLQ-LQVQAEQDNLNDAEERCDQLikNKIqleakVKE 923
Cdd:COG3883 61 EALQAEIDKLQAE---IAEAEAEIEERREELGERARALYRSGGSVSyLDVLLGSESFSDFLDRLSAL--SKI-----ADA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 924 MTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQE 1003
Cdd:COG3883 131 DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
170
....*....|...
gi 255918225 1004 AHQQALDDLQAEE 1016
Cdd:COG3883 211 AAAAAAAAAAAAA 223
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1571-1809 |
1.35e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1571 KAEIERKLAEKDEEMEQAKRNHlrmvDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQA 1650
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEE----KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1651 HLKDtQLQLDDAVHANDDLK-----ENIAIVERRNNLLQAELEELRAVVEQTERSRklaeqelietservQLLHSQNTSL 1725
Cdd:COG4942 105 ELAE-LLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADL--------------AELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1726 INQKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQI 1805
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....
gi 255918225 1806 ALKG 1809
Cdd:COG4942 250 ALKG 253
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1573-1902 |
1.35e-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: 47.27 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1573 EIERKLAEKDEEMEQAKRNHLRMVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLsqANRIASEAQKHLKNSQAHL 1652
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL--YLDYLKLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1653 KDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKM 1732
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1733 ESDLTQLQT-----EVEEAVQECRNAEEKAKKaitdAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAL 1807
Cdd:pfam02463 327 EKELKKEKEeieelEKELKELEIKREAEEEEE----EELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1808 KGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEA 1887
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
330
....*....|....*
gi 255918225 1888 EEQANTNLSKFRKVQ 1902
Cdd:pfam02463 483 QEQLELLLSRQKLEE 497
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1342-1554 |
1.37e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1342 CDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKH 1421
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1422 RLQNEIEDLM------VDVER----SNAAAAALDKKQRNFDKILAEWKQKYEESQSELESS-------QKEARSLSTELF 1484
Cdd:PRK05771 118 ELEQEIERLEpwgnfdLDLSLllgfKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvvLKELSDEVEEEL 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255918225 1485 KlKNAYEE-SLEHLETFKRENKNLQEEISDLTEQLGEggkNVHELEKIRKQLEVEKL----ELQSALEEAEASLE 1554
Cdd:PRK05771 198 K-KLGFERlELEEEGTPSELIREIKEELEEIEKERES---LLEELKELAKKYLEELLalyeYLEIELERAEALSK 268
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
891-1061 |
1.38e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 891 LQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEK 970
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 971 HatenkVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQE-KKVRMD 1049
Cdd:COG1579 90 E-----YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAElEELEAE 164
|
170
....*....|..
gi 255918225 1050 LERAKRKLEGDL 1061
Cdd:COG1579 165 REELAAKIPPEL 176
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
972-1329 |
1.42e-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: 46.87 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 972 ATENKVKNLTEEMAGLDEIIaKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRM-DL 1050
Cdd:COG5185 202 GTVNSIKESETGNLGSESTL-LEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSkRL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1051 ERAKRKLEGDLKLTQESIMDLE------------NDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIE 1118
Cdd:COG5185 281 NENANNLIKQFENTKEKIAEYTksidikkateslEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1119 ELEEELEAERTARAKVEKLRSdLSRELEEISERLEEAGGATSVQIEMNKKREA--------EFQKMRRDLEEATLQHEAT 1190
Cdd:COG5185 361 EEIENIVGEVELSKSSEELDS-FKDTIESTKESLDEIPQNQRGYAQEILATLEdtlkaadrQIEELQRQIEQATSSNEEV 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1191 AAALRKKHADSVAELGEQIDNLQ-RVKQKLEKEKSEFKLELDDVTSNMEQIIKA----KANLEKVSRTLEDQANEYRVKL 1265
Cdd:COG5185 440 SKLLNELISELNKVMREADEESQsRLEEAYDEINRSVRSKKEDLNEELTQIESRvstlKATLEKLRAKLERQLEGVRSKL 519
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1266 EEAQRSLNDFTTQRAKLQTENGELARQLEEK---------EALISQLTRGKLSYTQQMEDLKRQLEEEGKAKN 1329
Cdd:COG5185 520 DQVAESLKDFMRARGYAHILALENLIPASELiqasnaktdGQAANLRTAVIDELTQYLSTIESQQAREDPIPD 592
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1486-1932 |
1.46e-04 |
|
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: 47.02 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1486 LKNAYEESLEHLETFKRENKNLQEEISDLTEQLGeggKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEgkilraql 1565
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIE---KMILAFEELRVQAENARLEMHFKLKEDHEKIQHLE-------- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1566 efNQIKAEIERKLAEKDEEMEQAKRNHLRMVDslQTSLDAETRSRNEALRVKKKMEGDlnemeiQLSQANriasEAQKHL 1645
Cdd:pfam05483 229 --EEYKKEINDKEKQVSLLLIQITEKENKMKD--LTFLLEESRDKANQLEEKTKLQDE------NLKELI----EKKDHL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1646 KnsqAHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQ-LLHSQNTS 1724
Cdd:pfam05483 295 T---KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEeLLRTEQQR 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1725 LIN---QKKKMESDLTQLQTEVEEAVQECRNAE---EKAKKAITDAAMMAEELKKEQDTSahlERMKKNMEQTIKDLQHR 1798
Cdd:pfam05483 372 LEKnedQLKIITMELQKKSSELEEMTKFKNNKEvelEELKKILAEDEKLLDEKKQFEKIA---EELKGKEQELIFLLQAR 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1799 LDEAE--QIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLK 1876
Cdd:pfam05483 449 EKEIHdlEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQ 528
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255918225 1877 VKAYKRQAE---EAEEQANTNLSKFRK--------VQHELDEAEERADIAESQVNKLRAKSRDIGAK 1932
Cdd:pfam05483 529 EERMLKQIEnleEKEMNLRDELESVREefiqkgdeVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
844-1794 |
1.60e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.97 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 844 SAETEKEMANMKEEFGRVKDALEkseaRRKELEEKMVSLLQEKNDlqlQVQAEQDNLNDAEERCDQLIKNKIqlEAKVKE 923
Cdd:TIGR01612 478 SYDIKKDIDENSKQDNTVKLILM----RMKDFKDIIDFMELYKPD---EVPSKNIIGFDIDQNIKAKLYKEI--EAGLKE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 924 MTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKE-------KHATENKVKNLTEEmaglDEIIAKLTK 996
Cdd:TIGR01612 549 SYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEiiyinklKLELKEKIKNISDK----NEYIKKAID 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 997 EKKALqEAHQQALDDL-QAEEDKVNTLTKSKVKLEQQVDDlegslEQEKKVRMDLERAKRKLEgdlKLTQESIMDLENDK 1075
Cdd:TIGR01612 625 LKKII-ENNNAYIDELaKISPYQVPEHLKNKDKIYSTIKS-----ELSKIYEDDIDALYNELS---SIVKENAIDNTEDK 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1076 LQLEEkLKKKefdISQQNSKIEDEQALALQLQKKLKENQarieeleeELEAERTARAKVEKLRSDLSRELEEISERLEEA 1155
Cdd:TIGR01612 696 AKLDD-LKSK---IDKEYDKIQNMETATVELHLSNIENK--------KNELLDIIVEIKKHIHGEINKDLNKILEDFKNK 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1156 GGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADS---VAELGEQIDNLQRVKQKLEKEKSEFKLELDD 1232
Cdd:TIGR01612 764 EKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAkqnYDKSKEYIKTISIKEDEIFKIINEMKFMKDD 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1233 VTSNMEQIIKAKANLEKVSRTLEDQANEY--RVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKlSY 1310
Cdd:TIGR01612 844 FLNKVDKFINFENNCKEKIDSEHEQFAELtnKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVD-EY 922
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1311 TQQMEDLKRQLEEEGKAKNALAHALQSSR---HDCDLLREQYEEEME-----AKAELQRVLSKA--------NSEVAQW- 1373
Cdd:TIGR01612 923 IKICENTKESIEKFHNKQNILKEILNKNIdtiKESNLIEKSYKDKFDntlidKINELDKAFKDAslndyeakNNELIKYf 1002
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1374 -------RTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVN-AKCSSLEKTKHRLQNEI----EDLMVDV-ERSNAA 1440
Cdd:TIGR01612 1003 ndlkanlGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEiAIHTSIYNIIDEIEKEIgkniELLNKEIlEEAEIN 1082
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1441 AAALDK-----KQRNFDKILAEWKQKYEesqselessqKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISdlt 1515
Cdd:TIGR01612 1083 ITNFNEikeklKHYNFDDFGKEENIKYA----------DEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIK--- 1149
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1516 eqlgeggKNVHELEKIrkqleVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEI-ERKLAEKDE-EMEQAKRNHL 1593
Cdd:TIGR01612 1150 -------AQINDLEDV-----ADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLnEIAEIEKDKtSLEEVKGINL 1217
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1594 RMVDSLQT----SLDAEtrsrnealrvKKKMEGDLNEMEIQLSQANRIASEAQKhLKNSQAHLKDTQLQLDDAVHANDDL 1669
Cdd:TIGR01612 1218 SYGKNLGKlfleKIDEE----------KKKSEHMIKAMEAYIEDLDEIKEKSPE-IENEMGIEMDIKAEMETFNISHDDD 1286
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1670 KENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEqelIETSERVQLLHSQ-NTSLINQKKKMESDLTQLQT-----EV 1743
Cdd:TIGR01612 1287 KDHHIISKKHDENISDIREKSLKIIEDFSEESDIND---IKKELQKNLLDAQkHNSDINLYLNEIANIYNILKlnkikKI 1363
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|.
gi 255918225 1744 EEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKD 1794
Cdd:TIGR01612 1364 IDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDD 1414
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
994-1251 |
1.76e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 994 LTKEKKALQEAhQQALDDLQAEEDKVNTLTKSKVkLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLEN 1073
Cdd:COG3206 184 LPELRKELEEA-EAALEEFRQKNGLVDLSEEAKL-LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1074 DklQLEEKLKKKEFDISQQnskiedeqaLAlQLQKKLKENQARIeeleeeleaeRTARAKVEKLRSDLSRELEEISERLE 1153
Cdd:COG3206 262 S--PVIQQLRAQLAELEAE---------LA-ELSARYTPNHPDV----------IALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1154 eaggatsVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRkkhadsvaELGEQIDNLQRVKQKLEKEKSEFKLELDDV 1233
Cdd:COG3206 320 -------AELEALQAREASLQAQLAQLEARLAELPELEAELR--------RLEREVEVARELYESLLQRLEEARLAEALT 384
|
250
....*....|....*...
gi 255918225 1234 TSNMEQIIKAKANLEKVS 1251
Cdd:COG3206 385 VGNVRVIDPAVVPLKPVS 402
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1675-1921 |
1.98e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1675 IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIEtserVQLLHSQNTSLinqKKKMESDLTQLQTEVEEAVQEcrnAE 1754
Cdd:PRK00409 503 IIEEAKKLIGEDKEKLNELIASLEELERELEQKAEE----AEALLKEAEKL---KEELEEKKEKLQEEEDKLLEE---AE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1755 EKAKKAItdaammaEELKKEQDtsahlermkknmeQTIKDLQHRLD-EAEQIALKGGKKQLQKLEARVRELENELEAEQK 1833
Cdd:PRK00409 573 KEAQQAI-------KEAKKEAD-------------EIIKELRQLQKgGYASVKAHELIEARKRLNKANEKKEKKKKKQKE 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1834 RNAESVKGMrkserRIKELTY-QTEE-----DKKNLMrLQDLVDKLQLK---VKAYKRQAEEAEEQANTNLSKFRKVQHE 1904
Cdd:PRK00409 633 KQEELKVGD-----EVKYLSLgQKGEvlsipDDKEAI-VQAGIMKMKVPlsdLEKIQKPKKKKKKKPKTVKPKPRTVSLE 706
|
250
....*....|....*..
gi 255918225 1905 LDEAEERADIAESQVNK 1921
Cdd:PRK00409 707 LDLRGMRYEEALERLDK 723
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1003-1187 |
2.03e-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: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1003 EAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQekkvrmdLERAKRKLEGDLKLTQESIMDLENDKLQLEEKL 1082
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1083 KKKEfdiSQQNSKIEDEQALALQ-----LQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGG 1157
Cdd:COG1579 76 KKYE---EQLGNVRNNKEYEALQkeiesLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180 190
....*....|....*....|....*....|
gi 255918225 1158 ATSVQIEmnkKREAEFQKMRRDLEEATLQH 1187
Cdd:COG1579 153 ELEAELE---ELEAEREELAAKIPPELLAL 179
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
869-1336 |
2.20e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 46.28 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 869 EARRKELEEKMVSLLQEKNDLQLQVQAEQDNLndaeercdQLIKNKIQLEAkvKEMTERLEDEEEMNAELTAKKRKLede 948
Cdd:pfam07111 241 ELERQELLDTMQHLQEDRADLQATVELLQVRV--------QSLTHMLALQE--EELTRKIQPSDSLEPEFPKKCRSL--- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 949 cseLKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTL------ 1022
Cdd:pfam07111 308 ---LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLqmelsr 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1023 -TKSKVKLEQQVDDLEgslEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKefdisqqnskiedeQA 1101
Cdd:pfam07111 385 aQEARRRQQQQTASAE---EQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKV--------------HT 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1102 LALQLQKKLKENQARIEELEEELEaertarakVEKLRSDLSRELEEISE---RL--EEAGGATSVQIEMNKKREaEFQKM 1176
Cdd:pfam07111 448 IKGLMARKVALAQLRQESCPPPPP--------APPVDADLSLELEQLREernRLdaELQLSAHLIQQEVGRARE-QGEAE 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1177 RRDLEEATLQHEATAaalrKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELddvtsNMEQIIKAKANLEKVSRT--- 1253
Cdd:pfam07111 519 RQQLSEVAQQLEQEL----QRAQESLASVGQQLEVARQGQQESTEEAASLRQEL-----TQQQEIYGQALQEKVAEVetr 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1254 LEDQANEYRVKLEEAQR-------SLNDFTTQRAKLQTENGELARQLEEkealisqltrgklSYTQQMEDLKRQLEEEGK 1326
Cdd:pfam07111 590 LREQLSDTKRRLNEARReqakavvSLRQIQHRATQEKERNQELRRLQDE-------------ARKEEGQRLARRVQELER 656
|
490
....*....|
gi 255918225 1327 AKNALAHALQ 1336
Cdd:pfam07111 657 DKNLMLATLQ 666
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1131-1430 |
2.22e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1131 RAKVEKLRSDLSRELEEISERLEEAggATSVQiemnkkreaEFQKMRRDLEEATLQH---------EATAAALRKKHADS 1201
Cdd:COG3096 780 RAAREKRLEELRAERDELAEQYAKA--SFDVQ---------KLQRLHQAFSQFVGGHlavafapdpEAELAALRQRRSEL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1202 VAELGEQIDNLQRVKQKLEKEKSEFKL------------------ELDDVTSNMEQIIKAKANLEKVSRTLEdqaneyrv 1263
Cdd:COG3096 849 ERELAQHRAQEQQLRQQLDQLKEQLQLlnkllpqanlladetladRLEELREELDAAQEAQAFIQQHGKALA-------- 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1264 KLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLT-----RGKLSYtqqmEDLKRQLEEEGKAKNALAHALQSS 1338
Cdd:COG3096 921 QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSevvqrRPHFSY----EDAVGLLGENSDLNEKLRARLEQA 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1339 RHDCDLLREQYEEEMEAKAELQRVLSKANSevaQWRTKYET--DAIQRTEELE-----EAKKKLAQRLQDAEEAVEAVNA 1411
Cdd:COG3096 997 EEARREAREQLRQAQAQYSQYNQVLASLKS---SRDAKQQTlqELEQELEELGvqadaEAEERARIRRDELHEELSQNRS 1073
|
330
....*....|....*....
gi 255918225 1412 KCSSLEKTKHRLQNEIEDL 1430
Cdd:COG3096 1074 RRSQLEKQLTRCEAEMDSL 1092
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
971-1336 |
2.56e-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: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 971 HATENKVKNLTEEMAGLDEIiakLTKEKKALQEAHQQALDDLQAEEDK---------VNTLTKSKVKLEQQVDDLEGSLE 1041
Cdd:NF033838 36 HAEEVRGGNNPTVTSSGNES---QKEHAKEVESHLEKILSEIQKSLDKrkhtqnvalNKKLSDIKTEYLYELNVLKEKSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1042 QE--KKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKK---------------------EFDISQQNSKIED 1098
Cdd:NF033838 113 AEltSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQkeedrrnyptntyktleleiaESDVEVKKAELEL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1099 EQALALQLQKKLKENQARIEELEEELEAERTARAKVEKlrsdlsrelEEISERLEEAGGATSVQIEMNKKREAEFQKMRR 1178
Cdd:NF033838 193 VKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDR---------EKAEEEAKRRADAKLKEAVEKNVATSEQDKPKR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1179 DLEEATLQHEATAAALRKKHADSVAELGEQidNLQRVKQKLEKEKSEFKLELDDVTSnmeqiiKAKANLEKVSR------ 1252
Cdd:NF033838 264 RAKRGVLGEPATPDKKENDAKSSDSSVGEE--TLPSPSLKPEKKVAEAEKKVEEAKK------KAKDQKEEDRRnyptnt 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1253 --TLEDQANEYRVKLEEAQRSLndfTTQRAKlQTENGELARQ----LEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGK 1326
Cdd:NF033838 336 ykTLELEIAESDVKVKEAELEL---VKEEAK-EPRNEEKIKQakakVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDK 411
|
410
....*....|
gi 255918225 1327 AKNALAHALQ 1336
Cdd:NF033838 412 VKEKPAEQPQ 421
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
870-1024 |
2.57e-04 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 44.57 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 870 ARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQL---------------IKNKI--------QLEAKVKEMTE 926
Cdd:pfam15934 41 ENKNEQEQQLKEFTVQNQRLACQIDNLHETLKDRDHQIKQLqsmitgysdisennrLKEEIhdlkqkncVQARVVRKMGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 927 RLEDEEEMNAELTAKKRKL----EDECSELK---KDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLdeiiakltKEKK 999
Cdd:pfam15934 121 ELKGQEEQRVELCDKYESLlgsfEEQCQELKranRRVQSLQTRLSQVEKLQEELRTERKILREEVIAL--------KEKD 192
|
170 180
....*....|....*....|....*....
gi 255918225 1000 ALQEAHQQALDD----LQAEEDKVNTLTK 1024
Cdd:pfam15934 193 AKSNGRERALQDqlkcCQTEIEKSRTLIR 221
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1527-1743 |
2.64e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1527 ELEKIRKQLEVEKLELQSALEEAEASLEH-----------EEGKILRAQLefnqikAEIERKLAEKDEEMEQAKRNhlrm 1595
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlsEEAKLLLQQL------SELESQLAEARAELAEAEAR---- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1596 VDSLQTSLDAETRSRNEALR--VKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHAN-DDLKEN 1672
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAE 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255918225 1673 IAIVERRNNLLQAELEELRAVVEQTERsrklAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEV 1743
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1050-1588 |
2.73e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1050 LERAKRKLEGDLKLTQESIMDLENdklqLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERT 1129
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1130 A--------------RAKVEKLRSDLSRELEE---ISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1192
Cdd:PRK01156 240 AlnelssledmknryESEIKTAESDLSMELEKnnyYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1193 ALRKKHADSVAELGEQIDNLQRVKQKleKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSL 1272
Cdd:PRK01156 320 EINKYHAIIKKLSVLQKDYNDYIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1273 NDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEE-EGKAKNALAH---ALQSSRHdcdlLREQ 1348
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMlNGQSVCPVCGttlGEEKSNH----IINH 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1349 YEEEM----EAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQ-------------RLQDAEEAVEAVNA 1411
Cdd:PRK01156 474 YNEKKsrleEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESaradledikikinELKDKHDKYEEIKN 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1412 KCSSLEKTKHRLQNEiEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYE 1491
Cdd:PRK01156 554 RYKSLKLEDLDSKRT-SWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLN 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1492 ESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQL---EVEKLELQSALEEAEASLEHEEG--KILRAQL- 1565
Cdd:PRK01156 633 NKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIndiEDNLKKSRKALDDAKANRARLEStiEILRTRIn 712
|
570 580
....*....|....*....|...
gi 255918225 1566 EFNQIKAEIERKLaEKDEEMEQA 1588
Cdd:PRK01156 713 ELSDRINDINETL-ESMKKIKKA 734
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1350-1461 |
2.90e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1350 EEEMEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIED 1429
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQE 125
|
90 100 110
....*....|....*....|....*....|..
gi 255918225 1430 lmvdversnaaaaaLDKKQRNFDKILAEWKQK 1461
Cdd:PRK12704 126 --------------LEKKEEELEELIEEQLQE 143
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1687-1911 |
2.93e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1687 LEELRAVVEQTERSRKlAEQELIETSERVQLLhsqntslinqkkkmeSDLTQLQTEVEEAVQECRNAEE-----KAKKAI 1761
Cdd:COG4913 224 FEAADALVEHFDDLER-AHEALEDAREQIELL---------------EPIRELAERYAAARERLAELEYlraalRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1762 TDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEaEQKRNAESVkg 1841
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE-ERERRRARL-- 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255918225 1842 mrksERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRK----VQHELDEAEER 1911
Cdd:COG4913 365 ----EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRelreLEAEIASLERR 434
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1386-1921 |
3.08e-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: 45.79 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1386 EELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKhrlqNEIEDLMVDVERsnaaaAALDKKQRNFDKILAEWKQKyees 1465
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTK----RLIEELKLNLER-----AQTEEAQAKQDSELAKLRVE---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1466 QSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVH-------ELEKIRKQLEVE 1538
Cdd:pfam05701 109 EMEQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEeavsaskEIEKTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1539 KLELQSALEEAEAS-LEHEEGKIlRAQLEFNQIKAEIERKLAEKDEEMEQAkRNHLRMVDSLQTSLDAetrsrNEALRVK 1617
Cdd:pfam05701 189 LIATKESLESAHAAhLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-----ASALLLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1618 KK------MEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDdavHANDDLKENIAIVERrnnlLQAELEELR 1691
Cdd:pfam05701 262 LKaelaayMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIE---KAKDEVNCLRVAAAS----LRSELEKEK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1692 AVVEQTERSRKLA-------EQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAITDa 1764
Cdd:pfam05701 335 AELASLRQREGMAsiavsslEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEE- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1765 ammAEELKKEQDT-SAHLERMKKNMEQTIkdlqhrldEAEQIALkggkkqlqkleARVRELEnelEAEQKRNAESVKGMR 1843
Cdd:pfam05701 414 ---AEQAKAAASTvESRLEAVLKEIEAAK--------ASEKLAL-----------AAIKALQ---ESESSAESTNQEDSP 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255918225 1844 KSerrikeLTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNK 1921
Cdd:pfam05701 469 RG------VTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIALEKAEK 540
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
863-1068 |
3.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 863 DALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEErcdqliknkiQLEAKVKEMTERLEDEEEMNAELTAKK 942
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA----------ELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 943 RKLEDECSELKK---DIDDLELTLAkvekEKHATE--NKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEED 1017
Cdd:COG3883 86 EELGERARALYRsggSVSYLDVLLG----SESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255918225 1018 KVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESI 1068
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1551-1864 |
3.34e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 45.40 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1551 ASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHL--RMVDSLQTSLDAETRSRNEALRVKkkmeGDLNEMe 1628
Cdd:pfam05667 206 PSLLERNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLlkRIAEQLRSAALAGTEATSGASRSA----QDLAEL- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1629 iqLSQANRIASEAQKHLKNSQ-AHLKDTQLQLDDAVHANDDLKENIAIVERRNNLlQAELEELRAVVEQTERSRKLAEQE 1707
Cdd:pfam05667 281 --LSSFSGSSTTDTGLTKGSRfTHTEKLQFTNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1708 LietservqllhsqntslinqkKKMESDLTQLQTEVEEavQECRNAEEKAKKAItdAAMMAEELKkeqDTSAHLERMKKN 1787
Cdd:pfam05667 358 I---------------------KKLESSIKQVEEELEE--LKEQNEELEKQYKV--KKKTLDLLP---DAEENIAKLQAL 409
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1788 MEQTIKDLQH--RLDEAEQIALkggkkqLQKLEaRVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLM 1864
Cdd:pfam05667 410 VDASAQRLVElaGQWEKHRVPL------IEEYR-ALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLV 481
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
913-1182 |
3.63e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 913 NKIQLEAKVKEM-TERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDeiI 991
Cdd:pfam17380 285 SERQQQEKFEKMeQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRE--L 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 992 AKLTKEKKALQEAHQQALDDLQAEEDKVN--------TLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAK----RKLEG 1059
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELERLQMERQQKNervrqeleAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARqrevRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1060 DLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQAlalqlQKKLKENQARiEELEEELEAERTARAKVEKLRS 1139
Cdd:pfam17380 443 ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKR-----DRKRAEEQRR-KILEKELEERKQAMIEEERKRK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 255918225 1140 DLSRELEEIS------ERLEEAGGATSVQIEMNKKREAEfQKMRRDLEE 1182
Cdd:pfam17380 517 LLEKEMEERQkaiyeeERRREAEEERRKQQEMEERRRIQ-EQMRKATEE 564
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
991-1172 |
3.91e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 991 IAKLTKEKKaLQEAHQQALDDLQAEEDKVNTLTKSKVkleqqvddlegsLEQEKKVrmdlERAKRKLEGDLKLTQESIMD 1070
Cdd:PRK12704 24 VRKKIAEAK-IKEAEEEAKRILEEAKKEAEAIKKEAL------------LEAKEEI----HKLRNEFEKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1071 LENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEEleaertARAKVEKLrSDLSRE------ 1144
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE------QLQELERI-SGLTAEeakeil 159
|
170 180
....*....|....*....|....*...
gi 255918225 1145 LEEISERLEEAGGATSVQIEMNKKREAE 1172
Cdd:PRK12704 160 LEKVEEEARHEAAVLIKEIEEEAKEEAD 187
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1029-1285 |
4.26e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1029 LEQQVDDLEGSL----EQEKKVRMDLERAKRKLEgDLKlTQESIMDLENDKLQLEEKLKkkefdisqqnskiedeqalal 1104
Cdd:COG3206 166 LELRREEARKALefleEQLPELRKELEEAEAALE-EFR-QKNGLVDLSEEAKLLLQQLS--------------------- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1105 QLQKKLKENQARIeeleeeleaeRTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnkkreaEFQKMRRDLEEAT 1184
Cdd:COG3206 223 ELESQLAEARAEL----------AEAEARLAALRAQLGSGPDALPELLQSP----------------VIQQLRAQLAELE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1185 LQHEATAAALRKKHADsVAELGEQIDNL-QRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRV 1263
Cdd:COG3206 277 AELAELSARYTPNHPD-VIALRAQIAALrAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
250 260
....*....|....*....|....*
gi 255918225 1264 ---KLEEAQRSLNDFTTQRAKLQTE 1285
Cdd:COG3206 356 lerEVEVARELYESLLQRLEEARLA 380
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1424-1924 |
4.36e-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: 45.12 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1424 QNEIEDLMVDVERSNAAAAALDKKQRNFDKILAewKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLEtfkRE 1503
Cdd:pfam05557 20 QMELEHKRARIELEKKASALKRQLDRESDRNQE--LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL---NE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1504 NKNLQEEISDLTEQLGEggknvhELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQlEFNQIKAEIERKLAEKDE 1583
Cdd:pfam05557 95 KESQLADAREVISCLKN------ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS-EAEQLRQNLEKQQSSLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1584 EMEQAKRNHLRMvdSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIaSEAQKHLKNSQAHLKDTQLQLDDAv 1663
Cdd:pfam05557 168 AEQRIKELEFEI--QSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNEN-IENKLLLKEEVEDLKRKLEREEKY- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1664 handdlKENIAIVERRNNLLQAELEELravvEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEV 1743
Cdd:pfam05557 244 ------REEAATLELEKEKLEQELQSW----VKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1744 EEAVQECRNAEEKakkaITDAAMMAEELK--------------KEQD-TSAHLERMKK--NMEQTIKDLQHRLDEAEQIA 1806
Cdd:pfam05557 314 RELEQELAQYLKK----IEDLNKKLKRHKalvrrlqrrvllltKERDgYRAILESYDKelTMSNYSPQLLERIEEAEDMT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1807 LKgGKKQLQKLEARVRELENELEAeQKRNAESVKGMRKSERRiKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEE 1886
Cdd:pfam05557 390 QK-MQAHNEEMEAQLSVAEEELGG-YKQQAQTLERELQALRQ-QESLADPSYSKEEVDSLRRKLETLELERQRLREQKNE 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 255918225 1887 AEE-------QANTNLSKFRKVQHELDEAEERADIAESQVNKLRA 1924
Cdd:pfam05557 467 LEMelerrclQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQA 511
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
841-1091 |
4.37e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 44.67 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 841 LLKSAETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQ---------EKNDLQLQVQAEQDNLNDAEERCDQLI 911
Cdd:pfam15742 99 VLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQQKLEHAHKvcltdtcilEKKQLEERIKEASENEAKLKQQYQEEQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 912 KNKIQLEAKVKEMTERLEDeeemnaeLTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEemagLDEII 991
Cdd:pfam15742 179 QKRKLLDQNVNELQQQVRS-------LQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQE----LSEKL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 992 AKLTKEKKALQEAHQQALDDLQAEEDKVNtltkskvkleqqvddlegslEQEKKVRMDLERAKRKLEGDLKLTQESIMDL 1071
Cdd:pfam15742 248 SSLQQEKEALQEELQQVLKQLDVHVRKYN--------------------EKHHHHKAKLRRAKDRLVHEVEQRDERIKQL 307
|
250 260
....*....|....*....|
gi 255918225 1072 ENDKLQLEEKLKKKEFDISQ 1091
Cdd:pfam15742 308 ENEIGILQQQSEKEKAFQKQ 327
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
904-1079 |
4.72e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 44.62 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 904 EERCDQLIKNKIQLEAKVKEMTErleDEEEMNAELTakkrkledECSELKKDIDDLELTL-AKVEKEKHATENKVKNLTE 982
Cdd:smart00787 136 EWRMKLLEGLKEGLDENLEGLKE---DYKLLMKELE--------LLNSIKPKLRDRKDALeEELRQLKQLEDELEDCDPT 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 983 EMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKV-RMDLERAKRKLEGDL 1061
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFtFKEIEKLKEQLKLLQ 284
|
170
....*....|....*...
gi 255918225 1062 KLTQESIMDLENDKLQLE 1079
Cdd:smart00787 285 SLTGWKITKLSGNTLSMT 302
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
962-1172 |
4.88e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 962 TLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLE 1041
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1042 ------QEKKVRMD--------------LERA---KRKLEGDLKLTQEsimdLENDKLQLEEKLKKKEFDISQQNSKIED 1098
Cdd:COG3883 90 eraralYRSGGSVSyldvllgsesfsdfLDRLsalSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255918225 1099 EQALALQLQKKLKENQARIeelEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAE 1172
Cdd:COG3883 166 LEAAKAELEAQQAEQEALL---AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
936-1073 |
4.98e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 44.28 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 936 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEII-AKLTKEKKALQeahQQALDDLQA 1014
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALkDLLTDEGGAIA---RKEIKDLQK 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255918225 1015 EEDKVNTLTKSKVK-----LEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLEN 1073
Cdd:cd22656 187 ELEKLNEEYAAKLKakideLKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEK 250
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1298-1580 |
5.31e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 45.00 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1298 ALISQLTRGKLSYTQQMEDLKRQLEEE--GKAKNALAHALQSSRHDcdlLREQYEEEMEAKAELQRVLSKANSEVAQWRT 1375
Cdd:NF033838 88 ALNKKLSDIKTEYLYELNVLKEKSEAEltSKTKKELDAAFEQFKKD---TLEPGKKVAEATKKVEEAEKKAKDQKEEDRR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1376 KYETDAIqRTEELEEAKKKLaqRLQDAEEAVEAVNAKCSSLEKTkhrlqneIEDLMVDVERSNAAAAALDKKQRnfDKIL 1455
Cdd:NF033838 165 NYPTNTY-KTLELEIAESDV--EVKKAELELVKEEAKEPRDEEK-------IKQAKAKVESKKAEATRLEKIKT--DREK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1456 AEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQL-----------GEGGKN 1524
Cdd:NF033838 233 AEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSVGEETLpspslkpekkvAEAEKK 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255918225 1525 VHELEK----------------IRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAE 1580
Cdd:NF033838 313 VEEAKKkakdqkeedrrnyptnTYKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAE 384
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
861-997 |
5.34e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 861 VKDALEKSEARRKELEEKmvsllqeknDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTA 940
Cdd:COG2433 378 IEEALEELIEKELPEEEP---------EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255918225 941 KKRKL----------EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLtEEMAGLDE--------IIAKLTKE 997
Cdd:COG2433 449 ELSEArseerreirkDREISRLDREIERLERELEEERERIEELKRKLERL-KELWKLEHsgelvpvkVVEKFTKE 522
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1133-1396 |
5.83e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1133 KVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKmrrDLEEATLQHEataaalrkkhaDSVAELGEQIDNL 1212
Cdd:PRK05771 47 KLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIK---DVEEELEKIE-----------KEIKELEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1213 QRVKQKLEKEKSE------FKLELDDVTSN-MEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTE 1285
Cdd:PRK05771 113 ENEIKELEQEIERlepwgnFDLDLSLLLGFkYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1286 NGELARQLEEKEALISqlTRGKLSytQQMEDLKRQLEEEGKAKNALAHALqssrhdCDLLREQYEEEMEAKAELQRVLSK 1365
Cdd:PRK05771 193 VEEELKKLGFERLELE--EEGTPS--ELIREIKEELEEIEKERESLLEEL------KELAKKYLEELLALYEYLEIELER 262
|
250 260 270
....*....|....*....|....*....|....*..
gi 255918225 1366 ANSEVAQWRTKYeTDAIQ------RTEELEEAKKKLA 1396
Cdd:PRK05771 263 AEALSKFLKTDK-TFAIEgwvpedRVKKLKELIDKAT 298
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1704-1891 |
5.96e-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: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1704 AEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT-SAHLE 1782
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1783 RMKKNMEQT-----------IKDLQHRLDEAEQIAlKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKE 1851
Cdd:COG3883 94 ALYRSGGSVsyldvllgsesFSDFLDRLSALSKIA-DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 255918225 1852 LTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQA 1891
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1235-1449 |
6.67e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1235 SNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTrgklsytQQM 1314
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR-------EEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1315 EDLKRQLEEEGKAKNALAhALQSSRHDCDLLReqyeeemeaKAELQRVLSKANSEVAQwrtkyetDAIQRTEELEEAKKK 1394
Cdd:COG3883 89 GERARALYRSGGSVSYLD-VLLGSESFSDFLD---------RLSALSKIADADADLLE-------ELKADKAELEAKKAE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255918225 1395 LAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQR 1449
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1495-1933 |
6.81e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.51 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1495 EHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSAL--------EEAEASLEHEEGKILRAQLE 1566
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1567 FNQIKAEIERKLAEKDEEMEQAKRNHLRMVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLK 1646
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1647 NSQAHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLI 1726
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1727 NQKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIA 1806
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1807 LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEE 1886
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 255918225 1887 AEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKK 1933
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1170-1332 |
7.33e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1170 EAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQrvkQKLEKEKSEFK---------------LE----- 1229
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEIAEAE---AEIEERREELGeraralyrsggsvsyLDvllgs 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1230 --LDDVTSNMEQIIK-AKANLEKVSRTLEDQAnEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRG 1306
Cdd:COG3883 112 esFSDFLDRLSALSKiADADADLLEELKADKA-ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170 180
....*....|....*....|....*.
gi 255918225 1307 KLSYTQQMEDLKRQLEEEGKAKNALA 1332
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
845-1000 |
7.95e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 845 AETEKEMANMKEEfgRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEErcdQLIKNKIQLEAKVKEM 924
Cdd:PRK12704 45 EEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE---LLEKREEELEKKEKEL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 925 TERLEDEEEMNAELTAKKRKLEDE---CSELKKDiDDLELTLAKVEKE-KHATENKVKNLTEEmagldeiiAKLTKEKKA 1000
Cdd:PRK12704 120 EQKQQELEKKEEELEELIEEQLQElerISGLTAE-EAKEILLEKVEEEaRHEAAVLIKEIEEE--------AKEEADKKA 190
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1282-1587 |
8.29e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.76 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1282 LQTENGELARQLEEKEALIS-QLTRGKLSYTQQMEDLKRQLEEEGKAKnalahalqssrhdcdllreqyeeemeAKAELQ 1360
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGaEPSRLYSLYEKEIEDLRRQLDTLTVER--------------------------ARLQLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1361 rvLSKANSEVAQWRTKYETDAIQRTEeLEEAKKKLAQRLQDAEEAVEAVNAKCSSLE------KTKHR-----LQNEIED 1429
Cdd:pfam00038 77 --LDNLRLAAEDFRQKYEDELNLRTS-AENDLVGLRKDLDEATLARVDLEAKIESLKeelaflKKNHEeevreLQAQVSD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1430 LMVDVERSNAaaaaldkKQRNFDKILAEWKQKYEEsqselessqkearslstelfkLKNAYEESLEhlETFKRENKNLQE 1509
Cdd:pfam00038 154 TQVNVEMDAA-------RKLDLTSALAEIRAQYEE---------------------IAAKNREEAE--EWYQSKLEELQQ 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255918225 1510 EISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQ 1587
Cdd:pfam00038 204 AAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMAR 281
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
983-1161 |
8.34e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 983 EMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEgslEQEKKVRMDLERAK-----RKL 1057
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE---ARIKKYEEQLGNVRnnkeyEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1058 EGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEEleaertARAKVEKL 1137
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE------LEAEREEL 168
|
170 180
....*....|....*....|....
gi 255918225 1138 RSDLSRELEEISERLEEAGGATSV 1161
Cdd:COG1579 169 AAKIPPELLALYERIRKRKNGLAV 192
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1790-1932 |
9.64e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1790 QTIKDLQHRLDEAEQIA--LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQ 1867
Cdd:COG1579 7 RALLDLQELDSELDRLEhrLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255918225 1868 DL--VDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAK 1932
Cdd:COG1579 87 NNkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1605-1888 |
9.98e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.09 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1605 AETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQahlkDTQLQLDDAvhaNDDLKENIAIVERRNNLLQ 1684
Cdd:pfam02029 39 NEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEAL----ERQKEFDPT---IADEKESVAERKENNEEEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1685 AELEELRAVVEQTERSRKLAEQELIETSERVQLLHsQNTSLINQKKKMESDLTQLQTEVE------EAVQECRNAEEKAK 1758
Cdd:pfam02029 112 NSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWS-TEVRQAEEEGEEEEDKSEEAEEVPtenfakEEVKDEKIKKEKKV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1759 KAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDL----QHRLDEAEQIALKGGKKQLQKLEARVRELENElEAEQKR 1834
Cdd:pfam02029 191 KYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQgglsQSQEREEEAEVFLEAEQKLEELRRRRQEKESE-EFEKLR 269
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255918225 1835 NA--------ESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAE 1888
Cdd:pfam02029 270 QKqqeaelelEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRRAEAAE 331
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1768-1919 |
1.02e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1768 AEELKKEQDTSAHLERMKKNMEQTIKDLQhrldeaeqialkggkKQLQKLEARVRELENELEAEQKRNAES---VKGMRK 1844
Cdd:COG2433 391 PEEEPEAEREKEHEERELTEEEEEIRRLE---------------EQVERLEAEVEELEAELEEKDERIERLereLSEARS 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1845 SERR-------IKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRqAEEAEEQANT----NLSKFRKvqHELDEAEERAD 1913
Cdd:COG2433 456 EERReirkdreISRLDREIERLERELEEERERIEELKRKLERLKE-LWKLEHSGELvpvkVVEKFTK--EAIRRLEEEYG 532
|
....*.
gi 255918225 1914 IAESQV 1919
Cdd:COG2433 533 LKEGDV 538
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
867-1015 |
1.08e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 867 KSEARRKELEEKMVSLLQEKNdlqlqvqaeqdnlNDAEErcdqlIKNKIQLEAK--VKEMTERLEDE-EEMNAELTAKKR 943
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAK-------------KEAEA-----IKKEALLEAKeeIHKLRNEFEKElRERRNELQKLEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 944 KLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAK----------LTKEkkalqEAHQQALDDLQ 1013
Cdd:PRK12704 90 RLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEqlqelerisgLTAE-----EAKEILLEKVE 164
|
..
gi 255918225 1014 AE 1015
Cdd:PRK12704 165 EE 166
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
976-1223 |
1.14e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 976 KVKNLTEEMAGLD----EIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEgslEQEKKVRMDLE 1051
Cdd:PHA02562 175 KIRELNQQIQTLDmkidHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELT---DELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1052 rakrKLEGDL-KLTQESI-MDLENDKLQLEEKLKKK-------EFDISQQNSKIEDEQALALQLQKKLKENQARIEELEE 1122
Cdd:PHA02562 252 ----DPSAALnKLNTAAAkIKSKIEQFQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1123 ELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKmrrdleeatlqheatAAALRKKHADSV 1202
Cdd:PHA02562 328 IMDEFNEQSKKLLELKNKISTNKQSLITLVDKA-----------KKVKAAIEE---------------LQAEFVDNAEEL 381
|
250 260
....*....|....*....|.
gi 255918225 1203 AELGEQIDNLQRVKQKLEKEK 1223
Cdd:PHA02562 382 AKLQDELDKIVKTKSELVKEK 402
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1329-1889 |
1.19e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1329 NALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYE--TDAIQRTEELEEAKKKLAQRLQDAEEAV 1406
Cdd:PRK01156 186 DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDMKNRYESEIKTAESDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1407 EAVNAKCSSLEKTKHRLqNEIEDLMVDVERSNAAAAALDKKQ-RNFDKILAEWK---QKYEESQSELEssqkEARSLSTE 1482
Cdd:PRK01156 266 SMELEKNNYYKELEERH-MKIINDPVYKNRNYINDYFKYKNDiENKKQILSNIDaeiNKYHAIIKKLS----VLQKDYND 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1483 LFKLKNAYEE---SLEHLETFKRENKNLQEEISDLTEQLGEGGKNVH----ELEKIRKQLEVEKLELQSALEEAEASLEH 1555
Cdd:PRK01156 341 YIKKKSRYDDlnnQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIErmsaFISEILKIQEIDPDAIKKELNEINVKLQD 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1556 EEGKILraqlEFNQIKAEIERKLAEKDEEMEQAKRNHLRMVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQAN 1635
Cdd:PRK01156 421 ISSKVS----SLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDID 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1636 riasEAQKHLKNSQAHLkdtqlqlddavhANDDLKENIAiVERRNNLLQAELEELRaVVEQTERSRKLAEQELIE--TSE 1713
Cdd:PRK01156 497 ----EKIVDLKKRKEYL------------ESEEINKSIN-EYNKIESARADLEDIK-IKINELKDKHDKYEEIKNryKSL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1714 RVQLLHSQNTSLINQKKKMES-DLTQLQTEVEEAVQECRNAEEKakkaitdaamMAEELKKEQDTSAHLERMKKNMEQTI 1792
Cdd:PRK01156 559 KLEDLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESR----------LQEIEIGFPDDKSYIDKSIREIENEA 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1793 KDLQHRLDEAEqiALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDK 1872
Cdd:PRK01156 629 NNLNNKYNEIQ--ENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEI 706
|
570
....*....|....*..
gi 255918225 1873 LQLKVKAYKRQAEEAEE 1889
Cdd:PRK01156 707 LRTRINELSDRINDINE 723
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1779-1925 |
1.21e-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: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1779 AHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKRNAESVK--GMRKSERRIKELTYQT 1856
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1857 EEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1925
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1189-1372 |
1.25e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1189 ATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELD----DVTSNMEQIIKAKANLEKVSRTLEDQANEYRVK 1264
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelqaELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1265 LEEAQR---------------SLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKN 1329
Cdd:COG3883 92 ARALYRsggsvsyldvllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255918225 1330 ALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQ 1372
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1434-1707 |
1.28e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.79 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1434 VERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARslstelFKLKNAYEESLEHLETfkrENKNLQEEISD 1513
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAA------AEAEQELEESKRETET---GIQNLTAEIEQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1514 LTEQLGEGgknvheLEKIRKqlEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHL 1593
Cdd:COG5185 348 GQESLTEN------LEAIKE--EIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1594 RMVDSLQTSLDAETRSRNEALRVKKKMEGDLNEM--EIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKE 1671
Cdd:COG5185 420 RQIEELQRQIEQATSSNEEVSKLLNELISELNKVmrEADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKA 499
|
250 260 270
....*....|....*....|....*....|....*.
gi 255918225 1672 NiaiVERRNNLLQAELEELRAVVEQTERSRKLAEQE 1707
Cdd:COG5185 500 T---LEKLRAKLERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
852-1175 |
1.49e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 852 ANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMTERLEDE 931
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 932 EEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAH-QQALD 1010
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1011 DLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDIS 1090
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1091 QQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKRE 1170
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
....*
gi 255918225 1171 AEFQK 1175
Cdd:COG4372 347 LVGLL 351
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1006-1870 |
1.50e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1006 QQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAkrklEGDLKLTQESimdlendkLQLEEKLKKK 1085
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAA----SDHLNLVQTA--------LRQQEKIERY 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1086 EFDISQQNSKIEDEQALALQLQKKLKENQARieeleeeleaERTARAKVEKLRSDLSReleeiserLEEAggatsvqIEM 1165
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEAR----------LEAAEEEVDSLKSQLAD--------YQQA-------LDV 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1166 NKKREAEFQKMRRDLEEATLQHEA---TAAALRKKHADSVAELGEQIDNLQRVKQKLekeksefklelDDVTSNMEQIIK 1242
Cdd:COG3096 408 QQTRAIQYQQAVQALEKARALCGLpdlTPENAEDYLAAFRAKEQQATEEVLELEQKL-----------SVADAARRQFEK 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1243 AKANLEKVSRTLE-DQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTR------GKLSYTQQME 1315
Cdd:COG3096 477 AYELVCKIAGEVErSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEfcqrigQQLDAAEELE 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1316 DLKRQLEEEGKAKNALAHALQSSRHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTkyetdaiQRTEELEEAKKKL 1395
Cdd:COG3096 557 ELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLRE-------QSGEALADSQEVT 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1396 AQRLQDAEEAVEAVNAKcSSLEKTKHRLQNEIEDLmvdversNAAAAALDKKQRNfdkiLAEwkqkyeesqselessqKE 1475
Cdd:COG3096 630 AAMQQLLEREREATVER-DELAARKQALESQIERL-------SQPGGAEDPRLLA----LAE----------------RL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1476 ARSLSTELFK---LKNA-YEESL----------EHLETFKRENKNLQEEISDLteQLGEGGKN--------VHELEK--- 1530
Cdd:COG3096 682 GGVLLSEIYDdvtLEDApYFSALygparhaivvPDLSAVKEQLAGLEDCPEDL--YLIEGDPDsfddsvfdAEELEDavv 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1531 -------IR----------------KQLEVEKLELQsALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEME- 1586
Cdd:COG3096 760 vklsdrqWRysrfpevplfgraareKRLEELRAERD-ELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAEl 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1587 QAKRNHLRMVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMeiqLSQANRIASEaqkHLknsQAHLKDTQLQLDDAVHAN 1666
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL---LPQANLLADE---TL---ADRLEELREELDAAQEAQ 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1667 DDLKEN---IAIVERRNNLLQ---AELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLT-QL 1739
Cdd:COG3096 910 AFIQQHgkaLAQLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSDLNeKL 989
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1740 QTEVEEAVQECRNAEEKAKKA---ITDAAMMAEELKKEQDTSAhleRMKKNMEQTIKDLQHRLD-EAEQIAlKGGKKQLQ 1815
Cdd:COG3096 990 RARLEQAEEARREAREQLRQAqaqYSQYNQVLASLKSSRDAKQ---QTLQELEQELEELGVQADaEAEERA-RIRRDELH 1065
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1816 KLEARVRELENELEAE-QKRNAES---VKGMRKSERRIKELTYQTEEDKKNLMRLQDLV 1870
Cdd:COG3096 1066 EELSQNRSRRSQLEKQlTRCEAEMdslQKRLRKAERDYKQEREQVVQAKAGWCAVLRLA 1124
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
875-1112 |
1.51e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 875 LEEKMVSLLQEKNDLQLqVQAEQDNLNDAEERcdqlIKNKIQLEAKVKEMTERLEDEeeMNAELTAKKRKLEDECSELKK 954
Cdd:PRK05771 14 LKSYKDEVLEALHELGV-VHIEDLKEELSNER----LRKLRSLLTKLSEALDKLRSY--LPKLNPLREEKKKVSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 955 DIDDLELTLAKVEKEkhatenkVKNLTEEMAGLDEIIAKLTKEKKALQ--EAHQQALDDLQAEED---KVNTLTKSKVKL 1029
Cdd:PRK05771 87 LIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvFVGTVPEDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1030 EQQVDDLEGSLEQEKK------VRMDLERAKRKLEGDLKLTQESIMDLENDKLqLEEKLKKKEFDISQQNSKIEDeqala 1103
Cdd:PRK05771 160 LKLESDVENVEYISTDkgyvyvVVVVLKELSDEVEEELKKLGFERLELEEEGT-PSELIREIKEELEEIEKERES----- 233
|
....*....
gi 255918225 1104 lqLQKKLKE 1112
Cdd:PRK05771 234 --LLEELKE 240
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1383-1591 |
1.58e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1383 QRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAaaaLDKKQRNFDKIL-AEWKQK 1461
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE---IEERREELGERArALYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1462 YEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEggknvheLEKIRKQLEVEKLE 1541
Cdd:COG3883 100 GSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-------LEALKAELEAAKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 255918225 1542 LQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRN 1591
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
889-1161 |
1.63e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 889 LQLQVQAEQDNLNDAEER--------CDQLIKNkiqLEAKVKEMTERLEDEEEMNAELTAKKR----KLEDECSELKKDI 956
Cdd:PHA02562 160 LDISVLSEMDKLNKDKIRelnqqiqtLDMKIDH---IQQQIKTYNKNIEEQRKKNGENIARKQnkydELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 957 DDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQ-----QALDDlqaEEDKVNTLTKSKVKLEQ 1031
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVcptctQQISE---GPDRITKIKDKLKELQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1032 QVDDLEGSLEQEKKVRMDLERAKRKlegdlkltqesIMDLENDklqleeklkkkefdISQQNSKIEDEQALALQLQKKLK 1111
Cdd:PHA02562 314 SLEKLDTAIDELEEIMDEFNEQSKK-----------LLELKNK--------------ISTNKQSLITLVDKAKKVKAAIE 368
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1112 ENQARIEELEEELEAERTARAKVEKLRSDLSRELEE---ISERLEEAGGATSV 1161
Cdd:PHA02562 369 ELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHrgiVTDLLKDSGIKASI 421
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1684-1925 |
1.68e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.38 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1684 QAELEELRAVVEQTERSRKLAE-QELietseRVQLLHSQNTSLINQKKK---------MESDLTQLQTEVEEAVQECrnA 1753
Cdd:PLN03188 973 QDELEHYRNFYDMGEREVLLEEiQDL-----RSQLQYYIDSSLPSARKRnsllkltysCEPSQAPPLNTIPESTDES--P 1045
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1754 EEKAKK-------AITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQK---------- 1816
Cdd:PLN03188 1046 EKKLEQerlrwteAESKWISLAEELRTELDASRALAEKQKHELDTEKRCAEELKEAMQMAMEGHARMLEQyadleekhiq 1125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1817 LEARVRELENELEAEQKrnAESVKGMRKSERRI-----KELTYQTEEDKKNLMRLQDLVDKLQLKVkaykRQAEEAEEQA 1891
Cdd:PLN03188 1126 LLARHRRIQEGIDDVKK--AAARAGVRGAESKFinalaAEISALKVEREKERRYLRDENKSLQAQL----RDTAEAVQAA 1199
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 255918225 1892 NTNLSKFRKVQHELDEAEERADIAE-------SQVNKLRAK 1925
Cdd:PLN03188 1200 GELLVRLKEAEEALTVAQKRAMDAEqeaaeayKQIDKLKRK 1240
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
926-1155 |
1.78e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 926 ERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATEnkvKNLTEEM---------AGLDEIIAKLTK 996
Cdd:PRK11637 75 AQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQE---RLLAAQLdaafrqgehTGLQLILSGEES 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 997 EKKALQEAHQQALDdlQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENdkl 1076
Cdd:PRK11637 152 QRGERILAYFGYLN--QARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLES--- 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1077 qleeKLKKkefdisqqnskieDEQALAlqlqkKLKENQARIEELEEELEAERTARAKVEklrsdlSRELEEISERLEEA 1155
Cdd:PRK11637 227 ----SLQK-------------DQQQLS-----ELRANESRLRDSIARAEREAKARAERE------AREAARVRDKQKQA 277
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1022-1429 |
1.93e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1022 LTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQ-----NSKI 1096
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQaelnrLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1097 EDEQALALQLQKKLKENQARiEELEEELEAERTARAKVEKLRSDLSR---ELEEISERLEE----AGGATSVQIEMNKKR 1169
Cdd:pfam05557 84 YLEALNKKLNEKESQLADAR-EVISCLKNELSELRRQIQRAELELQStnsELEELQERLDLlkakASEAEQLRQNLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1170 E--AEFQKMRRDLEEATLQHEATAAALRKKHAD--SVAEL----------GEQIDNLQRVKQKLEKEKSEFKLELDDVTS 1235
Cdd:pfam05557 163 SslAEAEQRIKELEFEIQSQEQDSEIVKNSKSElaRIPELekelerlrehNKHLNENIENKLLLKEEVEDLKRKLEREEK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1236 NMEQIIKAKANLEKVSRTLE-----DQANEYRVKLEEAQRSLNDFTTQRAK-LQTENGELARQLEEKEALISQLTRGKLS 1309
Cdd:pfam05557 243 YREEAATLELEKEKLEQELQswvklAQDTGLNLRSPEDLSRRIEQLQQREIvLKEENSSLTSSARQLEKARRELEQELAQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1310 YTQQMEDLKRQLEEEGKAKNALAHALQSSRHDCDLLR---EQYEEEMeakaelqrvlskANSEVAQWRTKYETDAIQRTE 1386
Cdd:pfam05557 323 YLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRailESYDKEL------------TMSNYSPQLLERIEEAEDMTQ 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 255918225 1387 ELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEK--TKHRLQNEIED 1429
Cdd:pfam05557 391 KMQAHNEEMEAQLSVAEEELGGYKQQAQTLERelQALRQQESLAD 435
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
955-1085 |
1.96e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 955 DIDDLELTLAKVEKEKHATENkvknltEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVD 1034
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1035 DLEGSLEQEKKVRMDLERAKRKLEGDL------------------KLTQEsimdlENDKL-QLEEKLKKK 1085
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLLREEVteediaevvsrwtgipvgKLLEG-----EREKLlNLEEELHER 550
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
767-1112 |
2.12e-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: 43.01 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 767 FKAGLLGLLEEMR---------DERLSRIITRIQaqargqlmRIEFKKIVERRDALLVIQWNIRAFMGVKNWPWMKLYF- 836
Cdd:pfam15818 5 FKTSLLEALEELRmrreaetqyEEQIGKIIVETQ--------ELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCAl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 837 ---KIKPLLKSAETEKEMANMKEEFgrvkDALEKSearrKELEEKMVSLLQEKndLQLQVQAEQD---NLNDAEeRCDQL 910
Cdd:pfam15818 77 eeeKGKYQLATEIKEKEIEGLKETL----KALQVS----KYSLQKKVSEMEQK--LQLHLLAKEDhhkQLNEIE-KYYAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 911 IKNKIQLeakVKEMTERLE----DEEEMNAELTAKKRKLEDECSELKKDIDDL--ELTLAKVE-KEKHATEN-------- 975
Cdd:pfam15818 146 ITGQFGL---VKENHGKLEqnvqEAIQLNKRLSALNKKQESEICSLKKELKKVtsDLIKSKVTcQYKMGEENinltikeq 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 976 KVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEgslEQEKKVRMDLERAKR 1055
Cdd:pfam15818 223 KFQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALK---ENNQTLERDNELQRE 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 255918225 1056 KLegdlKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKE 1112
Cdd:pfam15818 300 KV----KENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1270-1797 |
2.23e-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: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1270 RSLNDFttqrakLQTENGELARQLEEKEALI--SQLTRGKLSYTQQMEDLKRQLEEEgkAKNALAHALQSSRHDCDLLRE 1347
Cdd:COG3096 214 RSLRDY------LLPENSGVRKAFQDMEAALreNRMTLEAIRVTQSDRDLFKHLITE--ATNYVAADYMRHANERRELSE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1348 QyeeEMEAKAELQRVLSKANSEvaQWRTKYETDAIqrtEELEEAKKKLAQRLQDAEEAVEAVnakcssleKTKHRLQNEI 1427
Cdd:COG3096 286 R---ALELRRELFGARRQLAEE--QYRLVEMAREL---EELSARESDLEQDYQAASDHLNLV--------QTALRQQEKI 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1428 EDLMVDVErsnAAAAALDKKQrnfdKILAEWKQKYEESQSELESSQKEARSLSTELFKlknaYEESLEHLETfkrenKNL 1507
Cdd:COG3096 350 ERYQEDLE---ELTERLEEQE----EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD----YQQALDVQQT-----RAI 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1508 QEEisdlteqlgeggKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEgkilraqlEFNQIKAEIERKLAekdeeMEQ 1587
Cdd:COG3096 414 QYQ------------QAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQ--------QATEEVLELEQKLS-----VAD 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1588 AKRNHLRMVDSLQTSLDAETrSRNEALRVKKKMEGDLNEMEIQLSQANRIA---SEAQKHL---KNSQAHLKDTQLQLDD 1661
Cdd:COG3096 469 AARRQFEKAYELVCKIAGEV-ERSQAWQTARELLRRYRSQQALAQRLQQLRaqlAELEQRLrqqQNAERLLEEFCQRIGQ 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1662 AVHANDDLKENIAiverrnnLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLInqkkKMESDLTQLQT 1741
Cdd:COG3096 548 QLDAAEELEELLA-------ELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL----AAQDALERLRE 616
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1742 EVEEAVQECRnaeekakkAITDAamMAEELKKEQDTSA---HLERMKKNMEQTIKDLQH 1797
Cdd:COG3096 617 QSGEALADSQ--------EVTAA--MQQLLEREREATVerdELAARKQALESQIERLSQ 665
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
865-1036 |
2.49e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.00 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 865 LEKSEARRKELEEKMVSLLQEkndLQLQVQAEQDNLN------DAEERCDQLIKNKIQLEAK-VKEMTERLEDEEEMNAE 937
Cdd:PLN03188 1049 LEQERLRWTEAESKWISLAEE---LRTELDASRALAEkqkhelDTEKRCAEELKEAMQMAMEgHARMLEQYADLEEKHIQ 1125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 938 LTAKKRKLEDECSELKKD-------------IDDL--ELTLAKVEKEKHAT----ENK-----VKNLTEEMAGLDEIIAK 993
Cdd:PLN03188 1126 LLARHRRIQEGIDDVKKAaaragvrgaeskfINALaaEISALKVEREKERRylrdENKslqaqLRDTAEAVQAAGELLVR 1205
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255918225 994 LTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDL 1036
Cdd:PLN03188 1206 LKEAEEALTVAQKRAMDAEQEAAEAYKQIDKLKRKHENEISTL 1248
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1564-1838 |
2.72e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.73 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1564 QLEFNQIKAEIERklAEKDEEMEQAKrnhlrMVDSLQTSLDAetrsrnealrvkkkmegdLNEMEIQLSQANriasEAQK 1643
Cdd:PRK10929 22 APDEKQITQELEQ--AKAAKTPAQAE-----IVEALQSALNW------------------LEERKGSLERAK----QYQQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1644 HLKNSQAHLKDTQLQLDDAVHANDDLKENIAIVERRNNLLQAE---LEELRAVVEQTERSRKLAE-------------QE 1707
Cdd:PRK10929 73 VIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSsqlLEKSRQAQQEQDRAREISDslsqlpqqqtearRQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1708 LIETSERVQLLHSQNTSLinqkkkMESDLTQLQteveeavqecrnAEEKAKKAITDaammaeELKkeqdtsahLERMKKN 1787
Cdd:PRK10929 153 LNEIERRLQTLGTPNTPL------AQAQLTALQ------------AESAALKALVD------ELE--------LAQLSAN 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 255918225 1788 MEQTIKDLQHRLdeaeqialkgGKKQLQKLEARVRELENELEAEQKRNAES 1838
Cdd:PRK10929 201 NRQELARLRSEL----------AKKRSQQLDAYLQALRNQLNSQRQREAER 241
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1607-1861 |
2.90e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1607 TRSRNEALRVKKKMEGDLNEMEIQLSQANRIAS------EAQKHLKNSQAHLKDTQLQLDDAVHANDDLKENIAIVERRN 1680
Cdd:pfam15905 52 TARKVKSLELKKKSQKNLKESKDQKELEKEIRAlvqergEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1681 NLLQAELEELRAVVEQTERSRKLA--EQELIETSERvqlLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAEEKAK 1758
Cdd:pfam15905 132 LELTRVNELLKAKFSEDGTQKKMSslSMELMKLRNK---LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1759 -----------------KAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlkggKKQLQKLEARV 1821
Cdd:pfam15905 209 stekekieeksetekllEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL----SKQIKDLNEKC 284
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 255918225 1822 RELENELEAEQKRNAESVKGMRKSERRIKE-LTYQTEEDKK 1861
Cdd:pfam15905 285 KLLESEKEELLREYEEKEQTLNAELEELKEkLTLEEQEHQK 325
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
898-1756 |
2.95e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 898 DNLNDAEERcDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATEnKV 977
Cdd:COG3096 272 DYMRHANER-RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQE-KI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 978 KNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKL 1057
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1058 EGDlKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIED---EQALALQLQKKLKENQARIEELEEELEAERTARAKV 1134
Cdd:COG3096 430 GLP-DLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAarrQFEKAYELVCKIAGEVERSQAWQTARELLRRYRSQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1135 EKL--RSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKmRRDLEEatlqHEATAAALRKKHADSVAELGEQIDNL 1212
Cdd:COG3096 509 ALAqrLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEE----LLAELEAQLEELEEQAAEAVEQRSEL 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1213 QRvkqklekeksefklELDDVTsnmeQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKL-------QTE 1285
Cdd:COG3096 584 RQ--------------QLEQLR----ARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLlerereaTVE 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1286 NGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEE---------------------GKAKNAL--------AHALQ 1336
Cdd:COG3096 646 RDELAARKQALESQIERLSQPGGAEDPRLLALAERLGGVllseiyddvtledapyfsalyGPARHAIvvpdlsavKEQLA 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1337 SsRHDC--DLLREQYEEE------MEAKAELQRVLSKanSEVAQWR-TKYETDAI-------QRTEELEEAKKKLAQRLQ 1400
Cdd:COG3096 726 G-LEDCpeDLYLIEGDPDsfddsvFDAEELEDAVVVK--LSDRQWRySRFPEVPLfgraareKRLEELRAERDELAEQYA 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1401 DAEEAVEavnaKCSSLEKTKHRLQNE------IEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESqselessqK 1474
Cdd:COG3096 803 KASFDVQ----KLQRLHQAFSQFVGGhlavafAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQL--------K 870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1475 EARSLsteLFKLknayeesLEHLETFKRENknLQEEISDLTEQLGEGGKNVHELEKIRKQLEveKLE-LQSALEEAEASL 1553
Cdd:COG3096 871 EQLQL---LNKL-------LPQANLLADET--LADRLEELREELDAAQEAQAFIQQHGKALA--QLEpLVAVLQSDPEQF 936
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1554 EHEEGKILRAQLEFNQIKAEIErklaekdeEMEQ--AKRNHLRMVDSLQtsLDAETRSRNEALRVKkkmegdLNEMEIQL 1631
Cdd:COG3096 937 EQLQADYLQAKEQQRRLKQQIF--------ALSEvvQRRPHFSYEDAVG--LLGENSDLNEKLRAR------LEQAEEAR 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1632 SQANRIASEAQKHLknSQAHlkDTQLQLDDAVHA-NDDLKEniaiverrnnlLQAELEEL--RAVVEQTERSRklaeqel 1708
Cdd:COG3096 1001 REAREQLRQAQAQY--SQYN--QVLASLKSSRDAkQQTLQE-----------LEQELEELgvQADAEAEERAR------- 1058
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 255918225 1709 ietsERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAEEK 1756
Cdd:COG3096 1059 ----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERD 1102
|
|
| ycf1 |
CHL00204 |
Ycf1; Provisional |
827-999 |
2.96e-03 |
|
Ycf1; Provisional
Pssm-ID: 214395 [Multi-domain] Cd Length: 1832 Bit Score: 42.78 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 827 KNWPWMKLYFKIKPLLKSAETEKE------MANMKEE--FGRVKDALEKSEARRKELEEKMVSLlQEKNDLQLQVQAEQD 898
Cdd:CHL00204 866 KPWHRSKLRSSHKDRMKKKKKKKNdfcfltVWGMETElpFGSPRKRPSFFEPIFKELKKKIRKF-KKKYFLVLKILKERT 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 899 N--LNDAEERCDQLIKNKIQLEAKVKEMTERledeeemNAELTAKKRKLeDECSELKKDIDDL-------ELTLAKVEKE 969
Cdd:CHL00204 945 KlfLKVSKETKKWIIKSFLFLKRIIKELSKR-------NPILLFGLREI-YELNETKKEKDSIisnqmihESSVQIRSME 1016
|
170 180 190
....*....|....*....|....*....|...
gi 255918225 970 ---KHATENKVKNLTEEMAGLDEIIAKLTKEKK 999
Cdd:CHL00204 1017 wtnSSLTEKKIKDLTDRTKTIRNQIEKITKEKK 1049
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
837-1058 |
3.56e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 837 KIKPLLKSAETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQ 916
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 917 LEAKVKEMTERLEDEEEMnAELTAKKRKLEDECSELKKDIDDleltLAKVEKEKHATenkvknLTEEMAGLDEIIAKLTK 996
Cdd:PRK02224 577 LNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREA----LAELNDERRER------LAEKRERKRELEAEFDE 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255918225 997 EK-KALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLE 1058
Cdd:PRK02224 646 ARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVE 708
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1229-1448 |
3.89e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1229 ELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTrgkl 1308
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1309 sytqqmedlkRQLEEEGKAKNALAhALQSSRHDCDLLR--EQYEEEMEAKAELQRVLSKANSEVAQwrtkYETDAIQRTE 1386
Cdd:COG3883 93 ----------RALYRSGGSVSYLD-VLLGSESFSDFLDrlSALSKIADADADLLEELKADKAELEA----KKAELEAKLA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255918225 1387 ELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQ 1448
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1538-1911 |
3.99e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1538 EKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERK-LAEKDEEME-QAKRNHLRMVdslqtsldaetrsrNEALR 1615
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELsARESDLEQDyQAASDHLNLV--------------QTALR 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1616 VKKKME---GDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDavhanddLKENIAIVERRNNLLQaeleelra 1692
Cdd:COG3096 345 QQEKIEryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDS-------LKSQLADYQQALDVQQ-------- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1693 vveqterSRKLAEQELIETSERVQ-LLHSQNTSLINqkkkMESDLTQLQTEVEEAVQECRNAEEK-----AKKAITDAAM 1766
Cdd:COG3096 410 -------TRAIQYQQAVQALEKARaLCGLPDLTPEN----AEDYLAAFRAKEQQATEEVLELEQKlsvadAARRQFEKAY 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1767 MA-EELKKEQDTSAHLERMKKNMEQTiKDLQHRLDeaeqialkggkkQLQKLEARVRELENELEAEQKrnaesvkgmrkS 1845
Cdd:COG3096 479 ELvCKIAGEVERSQAWQTARELLRRY-RSQQALAQ------------RLQQLRAQLAELEQRLRQQQN-----------A 534
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255918225 1846 ERRIKELTYQTEEDKKNLMRLQDLVDKLQLkvkaykrQAEEAEEQANTNLSKFRKVQHELDEAEER 1911
Cdd:COG3096 535 ERLLEEFCQRIGQQLDAAEELEELLAELEA-------QLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1599-1924 |
4.09e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1599 LQTSLDAETRSRNEALR----VKKKMEGDLNEMEIQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHANDDLKENIA 1674
Cdd:pfam07888 32 LQNRLEECLQERAELLQaqeaANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1675 IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNae 1754
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRS-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1755 ekakkaitdaamMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQ--IALKGGKKQLQKLEARVRELENELEAeQ 1832
Cdd:pfam07888 190 ------------LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeAENEALLEELRSLQERLNASERKVEG-L 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1833 KRNAESVKGMRksERRIKELTYQTEEDKKNLMRLQDLvdKLQLKVKAYKRQAEEAEEQANTNLSKFR--KVQHELDEAEE 1910
Cdd:pfam07888 257 GEELSSMAAQR--DRTQAELHQARLQAAQLTLQLADA--SLALREGRARWAQERETLQQSAEADKDRieKLSAELQRLEE 332
|
330
....*....|....
gi 255918225 1911 RADIAESQVNKLRA 1924
Cdd:pfam07888 333 RLQEERMEREKLEV 346
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
915-1222 |
4.24e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.15 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 915 IQLEAKVKEMTERLEDEEEMNAELTakKRKLEDECSELKKDIDdLELTLAKvekEKHATENKVKNLTEEMA--------- 985
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPS--ELALNEMIEKLKKEID-LEYTEAV---IAMGLQERLENLREEFSkansqdqlm 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 986 --GLDEIIAKLTKE-KKALQEAhqQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVR--MDLERAKRKLEGD 1060
Cdd:PLN03229 506 hpVLMEKIEKLKDEfNKRLSRA--PNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKevMDRPEIKEKMEAL 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1061 LKLTQESIMDLENDklqLEEKLKKKefdISQQNSKIEDEQA-----LALQLQKKLKENQARIEELEEELEaertaRAKVE 1135
Cdd:PLN03229 584 KAEVASSGASSGDE---LDDDLKEK---VEKMKKEIELELAgvlksMGLEVIGVTKKNKDTAEQTPPPNL-----QEKIE 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1136 KLRSDLSRELEEISE-----------RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATlqheaTAAALRKKHADSVAE 1204
Cdd:PLN03229 653 SLNEEINKKIERVIRssdlkskiellKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEAL-----NSSELKEKFEELEAE 727
|
330
....*....|....*...
gi 255918225 1205 LGEQIDNLQRVKQKLEKE 1222
Cdd:PLN03229 728 LAAARETAAESNGSLKND 745
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1130-1363 |
4.35e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1130 ARAKVEKLRSDLSRELEEISERLEEaggatsvqiEMNKKR--EAEFQKMRRDLEEATLQH---EATA-------AALRKK 1197
Cdd:pfam00038 69 ERARLQLELDNLRLAAEDFRQKYED---------ELNLRTsaENDLVGLRKDLDEATLARvdlEAKIeslkeelAFLKKN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1198 HADSVAELGEQIDNLQRVkqklekeksefkLELDDVTS-NMEQIIK-AKANLEKVSRTLEDQANE-YRVKLEEAQRSLND 1274
Cdd:pfam00038 140 HEEEVRELQAQVSDTQVN------------VEMDAARKlDLTSALAeIRAQYEEIAAKNREEAEEwYQSKLEELQQAAAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1275 FTTQRAKLQTENGELARQLEEKEALISQLTRgklsytqQMEDLKRQLEEegkAKNALAHALQSSRhdcDLLREQYEEEME 1354
Cdd:pfam00038 208 NGDALRSAKEEITELRRTIQSLEIELQSLKK-------QKASLERQLAE---TEERYELQLADYQ---ELISELEAELQE 274
|
....*....
gi 255918225 1355 AKAELQRVL 1363
Cdd:pfam00038 275 TRQEMARQL 283
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1736-1922 |
4.52e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.78 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1736 LTQLQTEVEEAVQECRNAEEK---AKKAITDAAMMAEELKKE-QDTSAHLERMKKNMEQTikdlQHRLDEAEQIA----- 1806
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKleeAEKRAEKAEAEVAALNRRiQLLEEELERTEERLAEA----LEKLEEAEKAAdeser 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1807 -LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTE--EDK--KNLMRLQDLVDKLQL---KVK 1878
Cdd:pfam00261 79 gRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraEERaeLAESKIVELEEELKVvgnNLK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 255918225 1879 AYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKL 1922
Cdd:pfam00261 159 SLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL 202
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1247-1448 |
4.85e-03 |
|
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: 41.76 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1247 LEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGK 1326
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1327 AKNALAHALQSSRHdcdllREQYEEEMEAKAELQRVLSKANSevaqwrtkyeTDAI-QRTEELEEAKKKLAQRLQDAEEA 1405
Cdd:pfam09726 480 ARASAEKQLAEEKK-----RKKEEEATAARAVALAAASRGEC----------TESLkQRKRELESEIKKLTHDIKLKEEQ 544
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255918225 1406 VEAVNAKCSSLEKTKHRlQNEIEDLMvdversNAAAAALDKKQ 1448
Cdd:pfam09726 545 IRELEIKVQELRKYKES-EKDTEVLM------SALSAMQDKNQ 580
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1684-1835 |
5.13e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.78 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1684 QAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAVQECRNAEEKAKKAITD 1763
Cdd:pfam00261 63 LEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESK 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1764 AAMMAEELKKEQDTSAHLE-------RMKKNMEQTIKDLQHRLDEAEQIALKGgKKQLQKLEARVRELENELEAEQKRN 1835
Cdd:pfam00261 143 IVELEEELKVVGNNLKSLEaseekasEREDKYEEQIRFLTEKLKEAETRAEFA-ERSVQKLEKEVDRLEDELEAEKEKY 220
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1774-1938 |
5.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1774 EQDTSAHLERMKKNMEQtikdlqhrLDEAEQIALKGgKKQLQKLEaRVRELENELEAEQKRNAESVKGMRK-----SERR 1848
Cdd:COG4913 220 EPDTFEAADALVEHFDD--------LERAHEALEDA-REQIELLE-PIRELAERYAAARERLAELEYLRAAlrlwfAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1849 IKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQANTN-LSKFRKVQHELDEAEERADIAESQVNKLRAKSR 1927
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170
....*....|.
gi 255918225 1928 DIGAKKMHDEE 1938
Cdd:COG4913 370 ALGLPLPASAE 380
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1530-1647 |
5.57e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1530 KIRKQLEVEKLELQSALEEAEASLE-HEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRMVDSLQTSLDAETR 1608
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEaIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEK 107
|
90 100 110
....*....|....*....|....*....|....*....
gi 255918225 1609 SRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKN 1647
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1780-1901 |
5.98e-03 |
|
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: 41.64 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1780 HLERMKKNMEQTIKDLQHRLDEAEQIAlkggKKQLQKLEARVRELENELEaEQKRNAESVKGMRKSERrikeltyQTEED 1859
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELH----EKQKFYLRQSVIDLQTKLQ-EMQMERDAMADIRRRES-------QSQED 142
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 255918225 1860 KKNlmRLQDLVDKLQlkvkAYKRQAEEAEEQANTNLSKFRKV 1901
Cdd:pfam15921 143 LRN--QLQNTVHELE----AAKCLKEDMLEDSNTQIEQLRKM 178
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
832-991 |
6.44e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 832 MKLYFKIKPLL--KSAETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQ 909
Cdd:smart00787 139 MKLLEGLKEGLdeNLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 910 LIKNKIQleaKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKK-----------DIDDLELTLAKVEKEKHATENKVK 978
Cdd:smart00787 219 EIMIKVK---KLEELEEELQELESKIEDLTNKKSELNTEIAEAEKkleqcrgftfkEIEKLKEQLKLLQSLTGWKITKLS 295
|
170
....*....|...
gi 255918225 979 NLTEEMAGLDEII 991
Cdd:smart00787 296 GNTLSMTYDREIN 308
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
848-1082 |
6.47e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 41.38 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 848 EKEMANMKEEFGRvkdALEKSEARRKELEEKMVSLLQEKN------------DLQLQVQAEQDNLNDAEERCDQLIKNKI 915
Cdd:PLN03229 485 QERLENLREEFSK---ANSQDQLMHPVLMEKIEKLKDEFNkrlsrapnylslKYKLDMLNEFSRAKALSEKKSKAEKLKA 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 916 QLEAKVKEMTERLEDEEEMNAeltakkRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMaGLDEIIAKlt 995
Cdd:PLN03229 562 EINKKFKEVMDRPEIKEKMEA------LKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSM-GLEVIGVT-- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 996 keKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKkvrmdLERAKRKLEGDLKlTQESIMDLENdk 1075
Cdd:PLN03229 633 --KKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSKIELLK-----LEVAKASKTPDVT-EKEKIEALEQ-- 702
|
....*..
gi 255918225 1076 lQLEEKL 1082
Cdd:PLN03229 703 -QIKQKI 708
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1491-1630 |
6.50e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1491 EESLEHLeTFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQ---LEVEKLELQSALEEAEASLEHEEGKILRAQLEf 1567
Cdd:COG2433 379 EEALEEL-IEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQverLEAEVEELEAELEEKDERIERLERELSEARSE- 456
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1568 nqikaeiERKLAEKDEEMEQAKrnhlRMVDSLQTSLDaETRSRNEALRVKKKMEGDLNEMEIQ 1630
Cdd:COG2433 457 -------ERREIRKDREISRLD----REIERLERELE-EERERIEELKRKLERLKELWKLEHS 507
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1682-1838 |
6.94e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1682 LLQAELEELRAVVEQTERSRK----------LAEQELIETSERVQLLHSQNTSLINQKKKMESdLTQLQTEVEEAVQECR 1751
Cdd:PRK11281 60 LVQQDLEQTLALLDKIDRQKEeteqlkqqlaQAPAKLRQAQAELEALKDDNDEETRETLSTLS-LRQLESRLAQTLDQLQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1752 NAE-----------------EKAKKAITDAAMMAEE----LKKEQDTSAHL---ERMKKNMEQTIKDLQHRLdeaEQIAL 1807
Cdd:PRK11281 139 NAQndlaeynsqlvslqtqpERAQAALYANSQRLQQirnlLKGGKVGGKALrpsQRVLLQAEQALLNAQNDL---QRKSL 215
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255918225 1808 KG-------GKKQLQKLEARVRELENELEAEQ-----KRNAES 1838
Cdd:PRK11281 216 EGntqlqdlLQKQRDYLTARIQRLEHQLQLLQeainsKRLTLS 258
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1174-1349 |
7.03e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.99 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1174 QKMRRDLEEatlQHEATAAALRKKhadsvaelgeqIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLE---KV 1250
Cdd:pfam03148 232 EQTANDLRA---QADAVNFALRKR-----------IEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEaplKL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1251 SRT-LEDQAneYRVKLE----EAQRSLNDfttqraklqtengELARQLEEKEALISQLTRGKLSYtQQMEDLKRQLEEEG 1325
Cdd:pfam03148 298 AQTrLENRT--YRPNVElcrdEAQYGLVD-------------EVKELEETIEALKQKLAEAEASL-QALERTRLRLEEDI 361
|
170 180
....*....|....*....|....
gi 255918225 1326 KAKNalaHALQSSRHDCDLLREQY 1349
Cdd:pfam03148 362 AVKA---NSLFIDREKCMGLRKRL 382
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
951-1907 |
7.05e-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: 41.58 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 951 ELKKDIDdleltlakvekEKHATENKVKNLTEEMAGLDEII--------AKLTKEKKALQEAHQQALDDLQAE-EDKVNT 1021
Cdd:TIGR01612 480 DIKKDID-----------ENSKQDNTVKLILMRMKDFKDIIdfmelykpDEVPSKNIIGFDIDQNIKAKLYKEiEAGLKE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1022 LTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKkkefDISQQNSKIEDeqa 1101
Cdd:TIGR01612 549 SYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIK----NISDKNEYIKK--- 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1102 lALQLQKKLKENQARIEELEEELEAERTARAK-VEKLRSDLSRELEEISE-RLEEAGGATSVQIEMN------------- 1166
Cdd:TIGR01612 622 -AIDLKKIIENNNAYIDELAKISPYQVPEHLKnKDKIYSTIKSELSKIYEdDIDALYNELSSIVKENaidntedkakldd 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1167 --KKREAEFQKMRrDLEEATLQ-HEATAAALRKKHADSVAEL-----GEQIDNLQRVKQKLEKEKSEFKLELDDVTSNME 1238
Cdd:TIGR01612 701 lkSKIDKEYDKIQ-NMETATVElHLSNIENKKNELLDIIVEIkkhihGEINKDLNKILEDFKNKEKELSNKINDYAKEKD 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1239 QIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALISQLTRGKLSYTQQMEDLK 1318
Cdd:TIGR01612 780 ELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCK 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1319 RQLEEEGKAKNALAHALQSSRHDCDLlrEQYEEEM-EAKAELQRVLSKANSEVAQWRTKYETDA-IQRTEELEEAKKKLA 1396
Cdd:TIGR01612 860 EKIDSEHEQFAELTNKIKAEISDDKL--NDYEKKFnDSKSLINEINKSIEEEYQNINTLKKVDEyIKICENTKESIEKFH 937
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1397 QRLQDAEEAVEA---VNAKCSSLEKT-KHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKIlaewkqKYEESQSELESS 1472
Cdd:TIGR01612 938 NKQNILKEILNKnidTIKESNLIEKSyKDKFDNTLIDKINELDKAFKDASLNDYEAKNNELI------KYFNDLKANLGK 1011
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1473 QKEArslstelfKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNV-HELEK-IRKQLEVEKLELqsaLEEAE 1550
Cdd:TIGR01612 1012 NKEN--------MLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIiDEIEKeIGKNIELLNKEI---LEEAE 1080
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1551 ASLEHeegkilraqleFNQIKAEIERKLAE---KDEEMEQAKRNHlRMVDSLQTSLDAETRSRNEALRVKKKMEGDLNEM 1627
Cdd:TIGR01612 1081 INITN-----------FNEIKEKLKHYNFDdfgKEENIKYADEIN-KIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEI 1148
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1628 EIQLSQANRIAseaqkhlknsqahlkdtqlqldDAVHANDDLKEniaiVERRnnllqaeleelravveqtersrklaEQE 1707
Cdd:TIGR01612 1149 KAQINDLEDVA----------------------DKAISNDDPEE----IEKK-------------------------IEN 1177
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1708 LIETSERVQLLHSQNTSLINQKKKMESDLTQLqteveeavQECRNAEEKAKKAItdAAMMAEELKKEQDTSAHlerMKKN 1787
Cdd:TIGR01612 1178 IVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSL--------EEVKGINLSYGKNL--GKLFLEKIDEEKKKSEH---MIKA 1244
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1788 MEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAE----QKRNAESVKGMRKSERRI-------------- 1849
Cdd:TIGR01612 1245 MEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDhhiiSKKHDENISDIREKSLKIiedfseesdindik 1324
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1850 KEL-TYQTEEDKKN------LMRLQDLVDKLQL--------KVKAYKRQAEEAEEQANTNLSKFRKVQHELDE 1907
Cdd:TIGR01612 1325 KELqKNLLDAQKHNsdinlyLNEIANIYNILKLnkikkiidEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD 1397
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1035-1249 |
7.07e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 41.36 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1035 DLEGSLE--QEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQN--------------SKIED 1098
Cdd:pfam15066 299 DTEQSFEslQPLEEDMALNEVLQKLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKQQvfvdiinklkenveELIED 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1099 EQALALQ----------LQKKLKENQARIEELEEELEaerTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNK- 1167
Cdd:pfam15066 379 KYNVILEkndinktlqnLQEILANTQKHLQESRKEKE---TLQLELKKIKVNYVHLQERYITEMQQKNKSVSQCLEMDKt 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1168 --KREAE---FQKMRRDLEEATlqheATAAALRKKHADSvaeLGEQIDNLQRVKQKLEKEksefklelddvtsNMEQIIK 1242
Cdd:pfam15066 456 lsKKEEEverLQQLKGELEKAT----TSALDLLKREKET---REQEFLSLQEEFQKHEKE-------------NLEERQK 515
|
....*..
gi 255918225 1243 AKANLEK 1249
Cdd:pfam15066 516 LKSRLEK 522
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1751-1916 |
7.08e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1751 RNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQTIKDLQHRLdeaeqialkggkkqLQKLEARVRELENELEA 1830
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKE------AEAIKKEALLEAKEEIHKL--------------RNEFEKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1831 EQKRNAESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQAnTNLSKFRKVQHELDEAEE 1910
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI-SGLTAEEAKEILLEKVEE 165
|
....*...
gi 255918225 1911 --RADIAE 1916
Cdd:PRK12704 166 eaRHEAAV 173
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
849-1045 |
7.10e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.40 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 849 KEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEM---- 924
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESergr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 925 ----TERLEDEEEMN---AELTAKKRKLED---ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKL 994
Cdd:pfam00261 81 kvleNRALKDEEKMEileAQLKEAKEIAEEadrKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255918225 995 -TKEKKALQ------EAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKK 1045
Cdd:pfam00261 161 eASEEKASEredkyeEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1676-1921 |
7.25e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1676 VERRNNL------LQAELEELRAVVEQTERSRKLAEQEL--IETSERVQLLHSQNTSLINQKKKMESDLTQLQTEVEEAV 1747
Cdd:pfam17380 312 VERRRKLeeaekaRQAEMDRQAAIYAEQERMAMERERELerIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1748 QECRNAEEKAKKAitdaaMMAEElkkeqdtsahlERMKKNMEQTIKDLQHRLDEAEqialkGGKKQLQKLEA-RVRELEN 1826
Cdd:pfam17380 392 ERVRQELEAARKV-----KILEE-----------ERQRKIQQQKVEMEQIRAEQEE-----ARQREVRRLEEeRAREMER 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1827 ELEAEQKRNaESVKGMRKSERRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELD 1906
Cdd:pfam17380 451 VRLEEQERQ-QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAI 529
|
250
....*....|....*
gi 255918225 1907 EAEERADIAESQVNK 1921
Cdd:pfam17380 530 YEEERRREAEEERRK 544
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
972-1937 |
7.30e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 972 ATENKVKNLTEEMAGLdeiIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQvddlEGSLEQEKKVRMDLE 1051
Cdd:NF041483 302 ANEQRTRTAKEEIARL---VGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAA----EDTAAQLAKAARTAE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1052 RAKRKLEGDLKLTQESIMDlENDKLQLE-----EKLKKKEFDISQQnskiedeqaLALQLQKKLKENQARieeLEEELEA 1126
Cdd:NF041483 375 EVLTKASEDAKATTRAAAE-EAERIRREaeaeaDRLRGEAADQAEQ---------LKGAAKDDTKEYRAK---TVELQEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1127 ERTARAKVEKLRSDLSRELEEIseRLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELG 1206
Cdd:NF041483 442 ARRLRGEAEQLRAEAVAEGERI--RGEARREAVQQIEEAARTAEELLTKAKADADELRSTATAESERVRTEAIERATTLR 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1207 EQIDN-LQRVKQKLEKEKSEFKLELDDVTSNMEQiiKAKANLEKVSRTLEDQA-----------NEYRVKLEEAQRSLND 1274
Cdd:NF041483 520 RQAEEtLERTRAEAERLRAEAEEQAEEVRAAAER--AARELREETERAIAARQaeaaeeltrlhTEAEERLTAAEEALAD 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1275 FTTQRAKLQTENGelarqlEEKEALISQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHAlQSSRHDCDLLREQYEEEME 1354
Cdd:NF041483 598 ARAEAERIRREAA------EETERLRTEAAERIRTLQAQAEQEAERLRTEAAADASAARA-EGENVAVRLRSEAAAEAER 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1355 AKAELQRVLSKANSEVAQWRTKYETDAiqrTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSlEKTKHRLQNEiedlmvdv 1434
Cdd:NF041483 671 LKSEAQESADRVRAEAAAAAERVGTEA---AEALAAAQEEAARRRREAEETLGSARAEADQ-ERERAREQSE-------- 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1435 ersnaaaaaldkkqrnfdKILAEWKQKYEESQSELESSQKEARSLSTELfkLKNAYEESLEHLETFKRENKNLQEEISDL 1514
Cdd:NF041483 739 ------------------ELLASARKRVEEAQAEAQRLVEEADRRATEL--VSAAEQTAQQVRDSVAGLQEQAEEEIAGL 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1515 TEQLGeggknvHELEKIRKQLEVEKLELQS-ALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEE--------M 1585
Cdd:NF041483 799 RSAAE------HAAERTRTEAQEEADRVRSdAYAERERASEDANRLRREAQEETEAAKALAERTVSEAIAEaerlrsdaS 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1586 EQAKRNHLRMVDSLQTSLDAETRSRNEALRVKKKMEGDlnemeiQLSQANRIASEAQKHLKNSQAHLKDTQLQLDDAVHA 1665
Cdd:NF041483 873 EYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSD------AAAQADRLIGEATSEAERLTAEARAEAERLRDEARA 946
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1666 NDDLK--ENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTqLQTEV 1743
Cdd:NF041483 947 EAERVraDAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRT-LDEAR 1025
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1744 EEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAhLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEaRVRE 1823
Cdd:NF041483 1026 KDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEA-LRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVE-KART 1103
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1824 LENELEAEQKRNAESVKGmRKSERR------IKELTYQTEEDKKNLMRLQ-DLVDKLqlkVKAYKRQAEEAEEQ------ 1890
Cdd:NF041483 1104 DADELLVGARRDATAIRE-RAEELRdritgeIEELHERARRESAEQMKSAgERCDAL---VKAAEEQLAEAEAKakelvs 1179
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1891 -ANTNLSKFR-----KVQHELDEAEERADIAESQVNKLRAKSrDIGAKKMHDE 1937
Cdd:NF041483 1180 dANSEASKVRiaavkKAEGLLKEAEQKKAELVREAEKIKAEA-EAEAKRTVEE 1231
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1773-1925 |
7.32e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1773 KEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGK------KQLQKLEARVRELENELEAEQKRNAESVKGMRKSE 1846
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRqldresDRNQELQKRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 1847 RRIKELTYQTEEDKKNLMRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1925
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQ 161
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
909-1114 |
7.60e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 909 QLIKNKIQLeakVKEMterledeeemnAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKhatenkvKNLTEEMAGLD 988
Cdd:smart00787 113 LLMDKQFQL---VKTF-----------ARLEAKKMWYEWRMKLLEGLKEGLDENLEGLKEDY-------KLLMKELELLN 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 989 EIIAKLTKEKKALQEAHQQalddlqaeedkvntltkskvkLEQQVDDLEgsleqeKKVRMDLERAKRKLegdlKLTQESI 1068
Cdd:smart00787 172 SIKPKLRDRKDALEEELRQ---------------------LKQLEDELE------DCDPTELDRAKEKL----KKLLQEI 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255918225 1069 MDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQ 1114
Cdd:smart00787 221 MIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCR 266
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1698-1912 |
7.70e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.09 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1698 ERSRKLAEQELIETSERVQllhSQNTSLINQKKKMEsdltqlQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT 1777
Cdd:pfam15709 314 ERSEEDPSKALLEKREQEK---ASRDRLRAERAEMR------RLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1778 SAHLERMKKnmeQTIKDLQHRLDEAEqialKGGKKQLQKLEARVRELENE-----LEAEQKRNAESVKGMRKSERRIKEL 1852
Cdd:pfam15709 385 RFEEIRLRK---QRLEEERQRQEEEE----RKQRLQLQAAQERARQQQEEfrrklQELQRKKQQEEAERAEAEKQRQKEL 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255918225 1853 TYQTEEDKKNLMRL--QDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHE-LDEAEERA 1912
Cdd:pfam15709 458 EMQLAEEQKRLMEMaeEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEaMKQAQEQA 520
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
918-1066 |
7.70e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 918 EAKvKEMTERLEDEEEMNAELTAKKRKLEDEcselkkdiddleltLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLtke 997
Cdd:PRK00409 506 EAK-KLIGEDKEKLNELIASLEELERELEQK--------------AEEAEALLKEAEKLKEELEEKKEKLQEEEDKL--- 567
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255918225 998 KKALQEAHQQALDDLQAEEDKVntltkskVKLEQQVDDLEGSLEQEKkvrmDLERAKRKLEGDLKLTQE 1066
Cdd:PRK00409 568 LEEAEKEAQQAIKEAKKEADEI-------IKELRQLQKGGYASVKAH----ELIEARKRLNKANEKKEK 625
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
1764-1928 |
8.35e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 40.74 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1764 AAMMAEELKKEQDTSAHLERMKKNMEQTikdlQHRLDEAEQI--ALKGGKKQLQKLEARVRELENELEAEQKRNAESVKG 1841
Cdd:PRK10361 28 AQQKAEQLAEREEMVAELSAAKQQITQS----EHWRAECELLnnEVRSLQSINTSLEADLREVTTRMEAAQQHADDKIRQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1842 MRKSERRIKE----LTYQTEE------DKKNLMRLQDLVDKLQLKVKAYKRQAEEA---EEQANTNLSkfrkvqHELDEA 1908
Cdd:PRK10361 104 MINSEQRLSEqfenLANRIFEhsnrrvDEQNRQSLNSLLSPLREQLDGFRRQVQDSfgkEAQERHTLA------HEIRNL 177
|
170 180
....*....|....*....|.
gi 255918225 1909 EE-RADIAESQVNKLRAKSRD 1928
Cdd:PRK10361 178 QQlNAQMAQEAINLTRALKGD 198
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
846-1154 |
8.41e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 846 ETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMT 925
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 926 ERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLE-----LTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 1000
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEqelqaLSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1001 LQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEE 1080
Cdd:COG4372 216 LAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALEL 295
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255918225 1081 KLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEE 1154
Cdd:COG4372 296 KLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1524-1708 |
8.48e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1524 NVHELEKIRKQ---LEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKdeemeqakrnhlRMVDSLQ 1600
Cdd:pfam00529 35 LVKEGDRVKAGdvlFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISR------------QDYDGAT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255918225 1601 TSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIAS---EAQKHLKNSQAHLKDTQLQLdDAVHANDDLKENIAIVE 1677
Cdd:pfam00529 103 AQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISREslvTAGALVAQAQANLLATVAQL-DQIYVQITQSAAENQAE 181
|
170 180 190
....*....|....*....|....*....|.
gi 255918225 1678 RRNNLLQAELEelravVEQTERSRKLAEQEL 1708
Cdd:pfam00529 182 VRSELSGAQLQ-----IAEAEAELKLAKLDL 207
|
|
| |
