|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-773 |
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: 1323.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 340 DILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 420 VQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 579
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 580 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGaAAAAEAESggGGGKKGAKKKGSSFQTVSALFR 659
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG-AAAAEAEE--GGGKKGGKKKGSSFQTVSALFR 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14910 558 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 637
|
650 660 670
....*....|....*....|....*....|....
gi 82524274 740 GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14910 638 GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
100-773 |
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: 1314.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEatsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKES---GKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 340 DILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd01377 238 DILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 420 VQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd01377 318 KEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPakGKVEA 578
Cdd:cd01377 398 EQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKP--KKSEA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 579 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaaaaaEAESGGGGGKKGAKKKGSSFQTVSALF 658
Cdd:cd01377 476 HFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLF-------KDYEESGGGGGKKKKKGGSFRTVSQLH 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 659 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 738
Cdd:cd01377 549 KEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIP 628
|
650 660 670
....*....|....*....|....*....|....*
gi 82524274 739 EGQFiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd01377 629 KGFD-DGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-773 |
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: 1310.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 340 DILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 420 VQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 579
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 580 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAaaeAESGGGGGKKGAKKKGSSFQTVSALFR 659
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQT---AEAEGGGGKKGGKKKGSSFQTVSALFR 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14915 558 ENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 637
|
650 660 670
....*....|....*....|....*....|....
gi 82524274 740 GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14915 638 GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-773 |
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: 1306.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDS--KMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14913 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 340 DILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 420 VQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14913 319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 579
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 580 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaaAAAEAESGGGGGKKGAKKKGSSFQTVSALFR 659
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY----ATFATADADSGKKKVAKKKGSSFQTVSALFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14913 555 ENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPE 634
|
650 660 670
....*....|....*....|....*....|....
gi 82524274 740 GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14913 635 GQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
100-773 |
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: 1252.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEatSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEE--SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 340 DILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 420 VQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 579
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 580 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaaAAAEAESGGGGGKKGAKKKGSSFQTVSALFR 659
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF----STYASAEADSGAKKGAKKKGSSFQTVSALFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14918 555 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE 634
|
650 660 670
....*....|....*....|....*....|....
gi 82524274 740 GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14918 635 GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-773 |
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: 1229.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 340 DILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 420 VQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 579
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 580 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsGAAAAAEAESGGGGGKKGAKKKGSSFQTVSALFR 659
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLF-SGAQTAEGASAGGGAKKGGKKKGSSFQTVSALFR 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14912 560 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 639
|
650 660 670
....*....|....*....|....*....|....
gi 82524274 740 GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14912 640 GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-773 |
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: 1217.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEeATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKE-QQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 340 DILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14923 240 DILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 420 VQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 579
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 580 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgAAAAAEAESGGGGGKKGAKKKGSSFQTVSALFR 659
Cdd:cd14923 480 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLF--SNYAGAEAGDSGGSKKGGKKKGSSFQTVSAVFR 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14923 558 ENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPE 637
|
650 660 670
....*....|....*....|....*....|....
gi 82524274 740 GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14923 638 GQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
101-773 |
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: 1155.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVIQYFATIAVTGE--KKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDgpGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 338
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 339 IDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 419 TVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 499 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKVE 577
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPdKKRKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 578 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsGAAAAAEAESGGGGGKKGAKKKGSSFQTVSAL 657
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY-ENYVGSDSTEDPKSGVKEKRKKAASFQTVSQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 658 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAI 737
Cdd:cd14927 561 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAI 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 82524274 738 PEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14927 641 PDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-773 |
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: 1130.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14917 159 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 340 DILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 420 VQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 579
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 580 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaaAAAEAESGGGGGKKGAKKKGSSFQTVSALFR 659
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLF----ANYAGADAPIEKGKGKAKKGSSFQTVSALHR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14917 555 ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE 634
|
650 660 670
....*....|....*....|....*....|....
gi 82524274 740 GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14917 635 GQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-773 |
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: 1127.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIAVTGEK-KKEEATSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRsKKENPNANK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 338
Cdd:cd14916 159 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 339 IDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 419 TVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 499 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEA 578
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 579 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaAAAAEAESGGGGGKKGAKKKGSSFQTVSALF 658
Cdd:cd14916 479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLF---STYASADTGDSGKGKGGKKKGSSFQTVSALH 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 659 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 738
Cdd:cd14916 556 RENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 635
|
650 660 670
....*....|....*....|....*....|....*
gi 82524274 739 EGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14916 636 EGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
88-773 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1032.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 88 IEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFML 167
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 168 TDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEeatsgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV--------GRLEEQILQSNPILEAFGNAKTVRNNNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 248 GKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQ-GEITVPSI 326
Cdd:pfam00063 153 GKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQsGCYTIDGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 327 DDQEELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPR 406
Cdd:pfam00063 232 DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 407 VKVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:pfam00063 312 IKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 486 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSN 564
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 565 NFQKPKPakgKVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGGGGGKKGA 644
Cdd:pfam00063 470 HFQKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTPK 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 645 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 724
Cdd:pfam00063 547 RTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 82524274 725 FKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:pfam00063 627 FVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
100-773 |
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: 1028.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14929 154 MLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 340 DILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14929 233 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 420 VQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14929 313 IEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 579
Cdd:cd14929 393 EQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 580 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaaAAAEAESGGGGGKKGAKKKGSSFQTVSALFR 659
Cdd:cd14929 473 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF----ENYISTDSAIQFGEKKRKKGASFQTVASLHK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14929 549 ENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPK 628
|
650 660 670
....*....|....*....|....*....|....
gi 82524274 740 GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14929 629 SKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
101-773 |
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: 987.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVIQYFATIAVTGEkkkeEATSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTGK----QSSDGK--GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAID 340
Cdd:cd14934 156 LAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 341 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd14934 236 VLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 421 QQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14934 316 EQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 501 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGK-VEAH 579
Cdd:cd14934 396 QEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 580 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaaaaaeaESGGGGGKKGAKKKGSSFQTVSALFR 659
Cdd:cd14934 476 FELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLF---------KEEEAPAGSKKQKRGSSFMTVSNFYR 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14934 547 EQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQ 626
|
650 660 670
....*....|....*....|....*....|....
gi 82524274 740 GqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14934 627 G-FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
81-785 |
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: 985.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 81 NPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISD 160
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 161 NAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAvtgekkkeeaTSGKMQGTLEDQIISANPLLEAFGNAKTVR 240
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVS----------GSNTEVGSVEDQILESNPILEAFGNAKTLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 241 NDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQG- 319
Cdd:smart00242 151 NNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 320 EITVPSIDDQEELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQA-EPDGTEVADKAAYLQNLNSADL 398
Cdd:smart00242 230 CLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 399 LKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQ 478
Cdd:smart00242 310 EKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 479 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYe 557
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 558 QHLGKSNNFQKPKPakgKVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaaaaaeaesgg 637
Cdd:smart00242 468 QHHKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLF------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 638 gGGKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 717
Cdd:smart00242 532 -PSGVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFP 610
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82524274 718 SRILYADFKQRYKVLNASAIPEGQFiDSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGLLEEMRD 785
Cdd:smart00242 611 YRLPFDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-773 |
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: 967.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIAVTgeKKKEEATSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGAS--KKTDEAAKSK--GSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14909 157 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 340 DILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 420 VQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14909 317 VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAK-GKVEA 578
Cdd:cd14909 397 EQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 579 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaAAAAEAESGGGGGKKGAKKKGSSFQTVSALF 658
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIF---ADHAGQSGGGEQAKGGRGKKGGGFATVSSAY 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 659 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 738
Cdd:cd14909 554 KEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQ 633
|
650 660 670
....*....|....*....|....*....|....*
gi 82524274 739 EGQfiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14909 634 GEE--DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
100-773 |
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: 834.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQ-EAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 179 GESGAGKTVNTKRVIQYFATIAvtgekKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALS-----GSGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDY----AFVSQGEITVPSIDDQEELMA 334
Cdd:cd00124 156 GRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYylndYLNSSGCDRIDGVDDAEEFQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 335 TDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREE--QAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNE 412
Cdd:cd00124 236 LLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 413 YVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 490
Cdd:cd00124 316 TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 491 FFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKP 569
Cdd:cd00124 396 FFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 570 KPAKGkveaHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSmktlaylfsgaaaaaeaesgggggkkgakkkgs 649
Cdd:cd00124 475 RKAKL----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS--------------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 650 sfqtvsaLFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 729
Cdd:cd00124 518 -------QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRY 590
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 82524274 730 KVLNASAiPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd00124 591 RILAPGA-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
30-1119 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 825.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 30 KPFDAKSSVFVVDAKESFVKATVqsreggKVTAKTEGGTTVTVK--DDQVYPMNPPKYDKIEDMAMMTHLHEPAVLYNLK 107
Cdd:COG5022 14 IPDEEKGWIWAEIIKEAFNKGKV------TEEGKKEDGESVSVKkkVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 108 ERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTV 187
Cdd:COG5022 88 KRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 188 NTKRVIQYFATIavtgekkkeEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIE 267
Cdd:COG5022 168 NAKRIMQYLASV---------TSSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 268 TYLLEKSRVTFQLKAERSYHIFYQIMSNKkPDLIEMLLITTNPYDYAFVSQGE-ITVPSIDDQEELMATDSAIDILGFTS 346
Cdd:COG5022 239 TYLLEKSRVVHQNKNERNYHIFYQLLAGD-PEELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 347 DERVSIYKLTGAVMHYGNMKFKqKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNS 426
Cdd:COG5022 318 EEQDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 427 VGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKK 506
Cdd:COG5022 397 RDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 507 EGIEWEFIDFgMDLAACIELIEK--PMGIFSILEEECMFPKATDTSFKNKLYEQ-HLGKSNNFQKPKPAKGKveahFSLV 583
Cdd:COG5022 477 EGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 584 HYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaaaaaeaesggggGKKGAKKKGSSFQTVSALFRENLN 663
Cdd:COG5022 552 HYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLF---------------DDEENIESKGRFPTLGSRFKESLN 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 664 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI 743
Cdd:COG5022 617 SLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYT 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 744 ---DSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDDKLAQLITRTQAMCRGYLARVEYQKMVERRESIFC 820
Cdd:COG5022 697 wkeDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQV 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 821 IQYNVRAFMNVKHWPWMKLYFKIKPLLKSAETEKEMANMKEEFEKaKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQS 900
Cdd:COG5022 777 IQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIK-LQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSL 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 901 EADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINaELTAKKRKLEDECSELKKDID-----DLELTLAKVEKEK 975
Cdd:COG5022 856 KAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELESEIIELKKSLSsdlieNLEFKTELIARLK 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 976 HATEN-KVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQekkiRMD 1054
Cdd:COG5022 935 KLLNNiDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQ----YGA 1010
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 82524274 1055 LERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKKefEMSNLQSKIEDEQalgMQLQKKIKELQ 1119
Cdd:COG5022 1011 LQESTKQLKELPVEVAELQSASKIISSESTELSILK--PLQKLKGLLLLEN---NQLQARYKALK 1070
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
101-773 |
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: 783.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVIQYFATIAVTGEKK-----KEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASKPKGsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 256 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDDQEELMAT 335
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 336 DSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYV 414
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 415 TKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 494 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLgksnnfQKPKPAK 573
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 574 GKVE--AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGGGGGKKGAKKKGSSF 651
Cdd:cd14911 474 TDFRgvADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRKGMF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 652 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 731
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 82524274 732 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
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 ... |
101-773 |
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: 763.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEeatsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVASSHKGRKD----HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14920 158 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL--EGFNnYRFLSNGYIPIPGQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 340 DILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 419 TVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14920 315 TKEQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 497 FVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNFQKPKPAK 573
Cdd:cd14920 394 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 574 GKVEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAA----AAAEAESGGGGGKKGAKKKGS 649
Cdd:cd14920 473 DKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgLDQVTGMTETAFGSAYKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 650 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 729
Cdd:cd14920 551 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 82524274 730 KVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14920 631 EILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-773 |
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: 713.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAID 340
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAG-DKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 341 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 420 VQQVYNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14932 320 QEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 499 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNFQKPKpaKGK 575
Cdd:cd14932 400 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKV-VQEQGNNPKFQKPK--KLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 576 VEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAA---AAEAESGGGGGKKGAKKKGSSFQ 652
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRivgLDKVAGMGESLHGAFKTRKGMFR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 653 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 732
Cdd:cd14932 557 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 82524274 733 NASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14932 637 TPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
101-773 |
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: 692.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASSHKGKKDTSITGE----LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMATDSAID 340
Cdd:cd14921 158 IVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN-NYTFLSNGFVPIPAAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 341 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 420 VQQVYNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14921 316 KEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 499 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGK 575
Cdd:cd14921 396 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 576 VEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAA----AAEAESGGGGGKKGAKKKGSSF 651
Cdd:cd14921 475 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRivglDQMAKMTESSLPSASKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 652 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 731
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 82524274 732 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14921 633 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-773 |
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: 683.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 179 GESGAGKTVNTKRVIQYFATiaVTGEKKKEEATsgkmqgtlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFAT--VGGSSSGETQV--------EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 338
Cdd:cd01380 151 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 339 IDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 419 TVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd01380 311 TLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 497 FVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNN-FQKPKPAKGK 575
Cdd:cd01380 391 FKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFSNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 576 veahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKtlaylfsgaaaaaeaesgggggkkgakkkgssFQTVS 655
Cdd:cd01380 470 ----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR--------------------------------KKTVG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 656 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 735
Cdd:cd01380 514 SQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPS 593
|
650 660 670
....*....|....*....|....*....|....*...
gi 82524274 736 AipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd01380 594 K--EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-773 |
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: 670.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAID 340
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL-ENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 341 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 421 QQVYNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 500 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKpaKGKV 576
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPK--KLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 577 EAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAA--EAESGGGGGKKGAKKKGSSFQTV 654
Cdd:cd15896 478 EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVglDKVSGMSEMPGAFKTRKGMFRTV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 655 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 734
Cdd:cd15896 558 GQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 637
|
650 660 670
....*....|....*....|....*....|....*....
gi 82524274 735 SAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd15896 638 NAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-773 |
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: 665.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14919 155 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 340 DILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 420 VQQVYNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 499 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGK 575
Cdd:cd14919 393 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 576 veAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAA----AAEAESGGGGGKKGAKKKGSSF 651
Cdd:cd14919 472 --ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiiglDQVAGMSETALPGAFKTRKGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 652 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 731
Cdd:cd14919 550 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 82524274 732 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14919 630 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-773 |
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: 651.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE----LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATDSAID 340
Cdd:cd14930 158 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 341 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14930 236 VLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 420 VQQVYNSVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14930 315 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 498 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 574
Cdd:cd14930 394 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLRD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 575 kvEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGGGGGKKGA--KKKGSSFQ 652
Cdd:cd14930 473 --QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPggRPRRGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 653 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 732
Cdd:cd14930 551 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 82524274 733 NASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14930 631 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-773 |
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: 624.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRgkKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFAtiavtgekkkeeATSGKMQGtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd01383 79 ESGAGKTETAKIAMQYLA------------ALGGGSSG-IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSA 338
Cdd:cd01383 146 KICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNcLTIDGVDDAKKFHELKEA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 339 IDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd01383 225 LDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 419 TVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDT-KQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd01383 305 TLQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 498 VLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNFqkpkpaKGKV 576
Cdd:cd01383 385 KLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGER 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 577 EAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKtLAYLFSGAAAAAEAESGGGGGKKGAKKKGssfQTVSA 656
Cdd:cd01383 457 GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQ-LPQLFASKMLDASRKALPLTKASGSDSQK---QSVAT 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 657 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 736
Cdd:cd01383 533 KFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPED 612
|
650 660 670
....*....|....*....|....*....|....*..
gi 82524274 737 IPEGQFIDSkkASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd01383 613 VSASQDPLS--TSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
101-773 |
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: 624.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVIQYFATIavtgekkkeeatSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd01381 82 SGAGKTESTKLILQYLAAI------------SGQ-HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSAI 339
Cdd:cd01381 149 IEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD-ASDYYYLTQGNcLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 340 DILGFTSDERVSIYKLTGAVMHYGNMKFKQKQRE--EQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 417
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 418 QTVQQVYNSVGALAKAVYEKMFLWMVTRIN----QQLDTKQPRQYfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINsaiyKPRGTDSSRTS-IGVLDIFGFENFEVNSFEQLCINFANENLQQFFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 494 HHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPkpa 572
Cdd:cd01381 387 RHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 573 KGKVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGGGggkkgakkkgssfQ 652
Cdd:cd01381 462 KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKS-------------P 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 653 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 732
Cdd:cd01381 529 TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVL 608
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 82524274 733 nASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd01381 609 -VPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
101-773 |
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: 619.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVIQYFAtiavtgekkkeeATSGKMQGTLE---DQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 257
Cdd:cd01378 82 SGAGKTEASKRIMQYIA------------AVSGGSESEVErvkDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 258 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDS 337
Cdd:cd01378 150 KGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 338 AIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDgTEVADKAAYLQNLNSADLLKALCYPRVKVGNEY---V 414
Cdd:cd01378 230 AMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 415 TKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQ-YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd01378 309 EVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 494 HhmFVL--EQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNKLyEQHLGKSNNFQKP 569
Cdd:cd01378 389 E--LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 570 KPAKGKVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGGgggkkgakkkgs 649
Cdd:cd01378 465 SGHFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSKKRPP------------ 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 650 sfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 729
Cdd:cd01378 533 ---TAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERY 609
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 82524274 730 KVLNASAIPEGQFIDsKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd01378 610 KLLSPKTWPAWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
101-773 |
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: 606.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVIQYFAtiAVTGEkkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14883 82 SGAGKTETTKLILQYLC--AVTNN-----------HSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPDLIEMLLITTNPYDYAFVSQ-GEITVPSIDDQEELMATDSA 338
Cdd:cd14883 149 IKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGaKHSKELKEKLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 339 IDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 417
Cdd:cd14883 229 MNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 418 QTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14883 309 LKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 498 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQkpKPAKGKV 576
Cdd:cd14883 389 KLEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYE--KPDRRRW 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 577 EAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGGGGGKKGAKKKGSSFQ-TVS 655
Cdd:cd14883 465 KTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTSRGTSKGKpTVG 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 656 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 735
Cdd:cd14883 545 DTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPR 624
|
650 660 670
....*....|....*....|....*....|....*...
gi 82524274 736 AIPEGQFIDsKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14883 625 ARSADHKET-CGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
100-773 |
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: 578.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 179 GESGAGKTVNTKRVIQYFATIAvtgekkKEEATSGKmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG------GRAVTEGR---SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDS 337
Cdd:cd01384 152 GRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKD-PKQFHYLNQSKcFELDGVDDAEEYRATRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 338 AIDILGFTSDERVSIYKLTGAVMHYGNMKFKqkqreEQAEPDGTEVADKAA--YLQNlnSADLL--------KALCYPRV 407
Cdd:cd01384 231 AMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEKSefHLKA--AAELLmcdekaleDALCKRVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 408 KVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd01384 304 VTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 488 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKSNNF 566
Cdd:cd01384 384 LQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 567 QKPKPAKGKveahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaaaaaeaesggGGGKKGAKK 646
Cdd:cd01384 462 SKPKLSRTD----FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF-------------PPLPREGTS 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 647 KGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFK 726
Cdd:cd01384 525 SSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 82524274 727 QRYKVLnASAIPEGQFiDSKKASEKLLGSIDIDhtQYKFGHTKVFFK 773
Cdd:cd01384 605 DRFGLL-APEVLKGSD-DEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
103-773 |
2.61e-171 |
|
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: 536.83 E-value: 2.61e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 182 GAGKTVNTKRVIQYFAtiavtgekkkeeATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01382 84 GAGKTESTKYILRYLT------------ESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLittnpydyafvsqgeiTVPSIDDQEELMATDSAIDI 341
Cdd:cd01382 152 VGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 342 LGFTSDERVSIYKLTGAVMHYGNMKFkqkqrEEQAEPD--GTEVADK-------AAYLQNLNSADLLKALCYpRVKVGNE 412
Cdd:cd01382 216 IGLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSggGCNVKPKseqsleyAAELLGLDQDELRVSLTT-RVMQTTR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 413 YVTKGQ------TVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQpRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 486
Cdd:cd01382 290 GGAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 487 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLgksNN 565
Cdd:cd01382 369 KLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK---NH 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 566 FQKPKPAKGKVEAH--------FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaaaaaeAESGG 637
Cdd:cd01382 445 FRLSIPRKSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF--------ESSTN 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 638 GGGKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 717
Cdd:cd01382 517 NNKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFP 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 82524274 718 SRILYADFKQRYKVLNASAIPEgqfIDSK---KASEKLLGSIDIDhtqYKFGHTKVFFK 773
Cdd:cd01382 597 SRTSFHDLYNMYKKYLPPKLAR---LDPRlfcKALFKALGLNEND---FKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
101-773 |
5.95e-171 |
|
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: 536.28 E-value: 5.95e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRQEAPPHIFSISDNAY-QFM---LTDRENQSI 175
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtQLIqsgVLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 176 LITGESGAGKTVNTKRVIQYFATI----AVTGEKKKEEATSGKMQ--GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARItsgfAQGASGEGEAASEAIEQtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQGEITVPSIDDQ 329
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 330 EELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT-EVADKAAYLQNLNSADLLKALCYPRVK 408
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 409 VGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 489 QQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-----KPmGIFSILEEECMFPKA-TDTSFKNKLYEQHLGK 562
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgkvngKP-GIFITLDDCWRFKGEeANKKFVSQLHASFGRK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 563 SNNFQKPKPAKG-------KVEA--HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYqKSSMKTLAYLfsgaaaaaea 633
Cdd:cd14890 479 SGSGGTRRGSSQhphfvhpKFDAdkQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELI-KQSRRSIREV---------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 634 esgggggkkgakkkgssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICR 713
Cdd:cd14890 548 -------------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQ 608
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 82524274 714 KGFPSRILYADFKQRYKVLNASAipegqfiDSKKASEKLLGSI-DIDHTQYKFGHTKVFFK 773
Cdd:cd14890 609 QGFALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKMlGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
100-773 |
9.28e-166 |
|
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: 522.33 E-value: 9.28e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRgKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 179 GESGAGKTVNTKRVIQYFATIAVTGEKKKEeatsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF--- 255
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS---------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFskl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 256 ------GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMS-----------------------NKKPDLIEMLLI 306
Cdd:cd14888 151 kskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 307 TT-NPYDYAFVSqGEITVPSIDDQEELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTE 382
Cdd:cd14888 231 EPhLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 383 VADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIG 461
Cdd:cd14888 310 DLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 462 VLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELI-EKPMGIFSILEEE 540
Cdd:cd14888 390 VLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 541 CMFPKATDTSFKNKLYEQHLGkSNNFQKPKpakgKVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTL 620
Cdd:cd14888 469 CFVPGGKDQGLCNKLCQKHKG-HKRFDVVK----TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFI 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 621 AYLFsgaaaaaeaeSGGGGGKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQL 700
Cdd:cd14888 544 SNLF----------SAYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQL 613
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 82524274 701 RCNGVLEGIRICRKGFPSRILYADFKQRYKVLnasAIPEGQfidskkasekllgsidIDHTQYKFGHTKVFFK 773
Cdd:cd14888 614 KYGGVLQAVQVSRAGYPVRLSHAEFYNDYRIL---LNGEGK----------------KQLSIWAVGKTLCFFK 667
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
853-1930 |
7.51e-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: 534.37 E-value: 7.51e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 853 EKEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKIKEVTER 932
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 933 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQ 1012
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1013 TLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKKEF 1092
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1093 EMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNK 1172
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1173 KREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNL 1252
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1253 EKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKA 1332
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1333 KSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDAEEHVE 1412
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1413 AVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQ---KY--EETHAELEASQKESRSLSte 1487
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAisaRYaeERDRAEAEAREKETRALS-- 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1488 lfkIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILR 1567
Cdd:pfam01576 641 ---LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLR 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1568 IQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHSNRMAAEAL 1647
Cdd:pfam01576 718 LEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1648 RNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQN 1727
Cdd:pfam01576 798 KQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGK 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1728 TSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEA 1807
Cdd:pfam01576 878 SALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1808 EQLALKGGKKQIQKLEARVRELEGEVENEQKRNVEAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKR 1887
Cdd:pfam01576 958 EGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKR 1037
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|...
gi 82524274 1888 QAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVK 1930
Cdd:pfam01576 1038 QLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
100-773 |
2.78e-163 |
|
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: 514.71 E-value: 2.78e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIAvtgekkkeEATSGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVA--------GSTNG-----VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSnkKPDLIEMLLITTNPyDYAFVSQGE-ITVPSIDDQEELMATDSA 338
Cdd:cd14872 148 RICGASTENYLLEKSRVVYQIKGERNFHIFYQLLA--SPDPASRGGWGSSA-AYGYLSLSGcIEVEGVDDVADFEEVVLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 339 IDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEP----DGTEVADKAAYLQnLNSADLLKALCYPRVKVgneyv 414
Cdd:cd14872 225 MEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGstvaNRDVLKEVATLLG-VDAATLEEALTSRLMEI----- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 415 tKGQ-------TVQQVYNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 486
Cdd:cd14872 299 -KGCdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 487 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSnn 565
Cdd:cd14872 378 KLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS-- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 566 FQKPKPAKGKvEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGggggkkgak 645
Cdd:cd14872 455 TFVYAEVRTS-RTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQKTSKV--------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 646 kkgssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 725
Cdd:cd14872 525 -------TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERF 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 82524274 726 KQRYKVLNaSAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14872 598 LKRYRFLV-KTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
100-773 |
5.22e-162 |
|
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: 512.01 E-value: 5.22e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 179 GESGAGKTVNTKRVIQYFATIAvtgekkkeeatSGKMQGTLEdQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA-----------GGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLiEMLLITTNPYDYAFvSQGEITVPSIDDQEELMATDSA 338
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEE-RLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 339 IDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE--PDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd14903 227 LSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 417 GQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14903 307 PLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 497 FVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgkv 576
Cdd:cd14903 387 FKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR--- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 577 eAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGGGGGKKGAKK-KGSSFQTVS 655
Cdd:cd14903 463 -TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRgGALTTTTVG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 656 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnas 735
Cdd:cd14903 542 TQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF--- 618
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 82524274 736 aIPEGQFIDSKKAS--EKLLGSIDIDH-TQYKFGHTKVFFK 773
Cdd:cd14903 619 -LPEGRNTDVPVAErcEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
103-773 |
3.69e-160 |
|
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: 508.07 E-value: 3.69e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESG 182
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 183 AGKTVNTKRVIQYFAtiavtgekkkeeATSGKMQGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01385 84 SGKTESTNFLLHHLT------------ALSQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSAID 340
Cdd:cd01385 152 RGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDcYTLEGEDEKYEFERLKQAME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 341 ILGFTSDERVSIYKLTGAVMHYGNMKFKQK--QREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd01385 231 MVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 419 TVQQVYNSVGALAKAVYEKMFLWMVTRINQQL----DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 494
Cdd:cd01385 311 KLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 495 HMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHlgKSNNF-QKPKpa 572
Cdd:cd01385 391 HIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAKFKQQH--KDNKYyEKPQ-- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 573 kgKVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTL-----------------------AYLFSGAAA 629
Cdd:cd01385 466 --VMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVreligidpvavfrwavlraffraMAAFREAGR 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 630 AAEAESGGGGGKKGAKKKGSSF--------QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLR 701
Cdd:cd01385 544 RRAQRTAGHSLTLHDRTTKSLLhlhkkkkpPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLR 623
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 82524274 702 CNGVLEGIRICRKGFPSRILYADFKQRYKVLnasaIPEGQfIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd01385 624 YTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
100-771 |
1.63e-159 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 505.09 E-value: 1.63e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY------RGKKRQEAPPHIFSISDNAYQFMLTDRE-- 171
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 172 --NQSILITGESGAGKTVNTKRVIQYFAtiAVTGEKKKEEATSGkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLA--SVSSATTHGQNATE--RENVRDRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNP-YDYAFVSQGEITVPSIDD 328
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEeYKYLNSSQCYDRRDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 329 QEELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAY-LQNLNSADLLKALCYPRV 407
Cdd:cd14901 237 SVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 408 KVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 486 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKSN 564
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 565 NFQKPKPAKGKveAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAylfsgaaaaaeaesgggggkkga 644
Cdd:cd14901 475 SFSVSKLQQGK--RQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS----------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 645 kkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 724
Cdd:cd14901 530 -------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDA 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 82524274 725 FKQRYKVLNAS------AIPEGQFIDSKKASEKLLGSIDIDHTQykFGHTKVF 771
Cdd:cd14901 603 FVHTYSCLAPDgasdtwKVNELAERLMSQLQHSELNIEHLPPFQ--VGKTKVF 653
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-773 |
4.63e-159 |
|
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: 502.96 E-value: 4.63e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIavtgekkkeeatsGKMQ-GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVL-------------GKANnRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI---MSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDD--QEELM 333
Cdd:cd01379 148 GAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIyagLAEDK-KLAKYKLPENKPPRYLQNDGLTVQDIVNNSgnREKFE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 334 ATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQ----AEPDGTEVADKAAYLQNLNSADLLKALCYPRVKV 409
Cdd:cd01379 227 EIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 410 GNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQP---RQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 486
Cdd:cd01379 307 RGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSasdEPLSIGILDIFGFENFQKNSFEQLCINIANE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 487 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFG-----MDLaacieLIEKPMGIFSILEEECMFPKATDTSFKNKLyEQHLg 561
Cdd:cd01379 387 QIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKF-HNNI- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 562 KSNNFQKPKpakgKVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAylfsgaaaaaeaesgggggk 641
Cdd:cd01379 460 KSKYYWRPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR-------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 642 kgakkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 721
Cdd:cd01379 516 ----------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRIL 585
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 82524274 722 YADFKQRYKVL--NASAIPEGqfidSKKASEKLLGSIDIDHtqYKFGHTKVFFK 773
Cdd:cd01379 586 FADFLKRYYFLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
101-773 |
1.37e-157 |
|
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: 499.66 E-value: 1.37e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEatsgkmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTGK 260
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVNQRRNNLVTE------------QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQI---MSNKKPDLIEMLlittNPYDYAFVSQG-EITVPSIDDQEELMATD 336
Cdd:cd01387 149 IVGAITSQYLLEKSRIVTQAKNERNYHVFYELlagLPAQLRQKYGLQ----EAEKYFYLNQGgNCEIAGKSDADDFRRLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 337 SAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEpdGTEVADKA-----AYLQNLNSADLLKALCYPRVKVGN 411
Cdd:cd01387 225 AAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQE--GVSVGSDAeiqwvAHLLQISPEGLQKALTFKVTETRR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 412 EYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 491
Cdd:cd01387 303 ERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 492 FNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 570
Cdd:cd01387 383 FNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 571 PAkgkvEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGGGGGKKGAKKKGSS 650
Cdd:cd01387 461 MP----LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKGRFVTMKPRT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 651 fQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 730
Cdd:cd01387 537 -PTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYR 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 82524274 731 VLNASAIPEGQFIDSKKA-SEKLLGSIDIDhtQYKFGHTKVFFK 773
Cdd:cd01387 616 CLVALKLPRPAPGDMCVSlLSRLCTVTPKD--MYRLGATKVFLR 657
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
106-773 |
2.10e-155 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 493.89 E-value: 2.10e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNaevVAAYRGKKRQEA-----PPHIFSISDNAYQFMLTDR----ENQSI 175
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYD---VPGFDSQRKEEAtasspPPHVFSIAERAYRAMKGVGkgqgTPQSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 176 LITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14892 84 VVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 256 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPyDYAFVSQGE-ITVPSIDDQEELMA 334
Cdd:cd14892 164 NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAE-SFLFLNQGNcVEVDGVDDATEFKQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 335 TDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAD--KAAYLQNLNSADLLKALCYpRVKVGne 412
Cdd:cd14892 243 LRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFKLVT-QTTST-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 413 yvTKGQ------TVQQVYNSVGALAKAVYEKMFLWMVTRIN----QQL------DTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:cd14892 320 --ARGSvleiklTAREAKNALDALCKYLYGELFDWLISRINachkQQTsgvtggAASPTFSPFIGILDIFGFEIMPTNSF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEK-PMGIFSILEEECMFP-KATDTSFKNK 554
Cdd:cd14892 398 EQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 555 LYEQHLGKSNNFQKPKPAKgkveAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMktlaylfsgaaaaaeae 634
Cdd:cd14892 477 YHQTHLDKHPHYAKPRFEC----DEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK----------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 635 sgggggkkgakkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRK 714
Cdd:cd14892 536 -----------------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRRE 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 715 GFPSRILYADFKQRYKVL-------NASAIPEGQFIDSKKASEKLLGSIDIDHTQykFGHTKVFFK 773
Cdd:cd14892 593 GFPIRRQFEEFYEKFWPLarnkagvAASPDACDATTARKKCEEIVARALERENFQ--LGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
101-773 |
1.69e-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: 491.23 E-value: 1.69e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIAvtgeKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVIS----QQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQ-GEITVPSIDDQEELMATDSA 338
Cdd:cd14873 158 NIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 339 IDILGFTSDERVSIYKLTGAVMHYGNMKFkqkqreeqAEPDGTEVADK-----AAYLQNLNSADLLKALCYPRVKVGNEY 413
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLRGEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 414 VTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQyFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14873 309 ILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 494 HHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgkSNNfqkPKPAK 573
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH---ANN---HFYVK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 574 GKVEAH-FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGGGGGKKGAkkkgssfQ 652
Cdd:cd14873 461 PRVAVNnFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRR-------P 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 653 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 732
Cdd:cd14873 534 TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVL 613
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 82524274 733 -NASAIPEgqfiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14873 614 mRNLALPE----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-773 |
5.10e-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: 472.64 E-value: 5.10e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKK-RQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVIQYFATIavtgekkkeeatSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKL------------SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEEL-----MAT 335
Cdd:cd14897 151 LLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELeyyrqMFH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 336 DSaIDIL---GFTSDERVSIYKLTGAVMHYGNMKFkqkqrEEQAEPDGTEVADK-----AAYLQNLNSADLLKALCYPRV 407
Cdd:cd14897 230 DL-TNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 408 KVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF-----IGVLDIAGFEIFDFNSLEQLCIN 482
Cdd:cd14897 304 TIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCIN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 483 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLyEQHLG 561
Cdd:cd14897 384 LSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 562 KSNNFQKPKpaKGKVEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaaaaaeaesgggggk 641
Cdd:cd14897 462 ESPRYVASP--GNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF----------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 642 kgakkkgssfqtvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 721
Cdd:cd14897 521 -------------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIK 587
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 82524274 722 YADFKQRYKVL-----NASAIPEGQFIDSKKasekllgsiDIDHTQYKFGHTKVFFK 773
Cdd:cd14897 588 YEDFVKRYKEIcdfsnKVRSDDLGKCQKILK---------TAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
102-732 |
5.46e-142 |
|
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: 455.92 E-value: 5.46e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAY-----------RGKKRQEAPPHIFSISDNAYQFM--- 166
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 167 -LTDRENQSILITGESGAGKTVNTKRVIQYFATIavtGEKKKEEATS-GKMQGTLEDQIISANPLLEAFGNAKTVRNDNS 244
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQA---GDNNLAASVSmGKSTSGIAAKVLQTNILLESFGNARTLRNDNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 245 SRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMllittnpydyafvsqgeitvp 324
Cdd:cd14900 160 SRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR--------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 325 siDDQEELMAtdsAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA-------DKAAYLQNLNSAD 397
Cdd:cd14900 219 --DMYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 398 LLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQL-----DTKQPRQYFIGVLDIAGFEIFD 472
Cdd:cd14900 294 LEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 473 FNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSF 551
Cdd:cd14900 374 KNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 552 KNKLYEQhLGKSNNFQKPKPAKGKveAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMktlaylfsgaaaaa 631
Cdd:cd14900 453 ASKLYRA-CGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYGLQ-------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 632 eaesgggggkkgakkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRI 711
Cdd:cd14900 516 --------------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRV 569
|
650 660
....*....|....*....|.
gi 82524274 712 CRKGFPSRILYADFKQRYKVL 732
Cdd:cd14900 570 ARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-773 |
3.22e-140 |
|
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: 452.18 E-value: 3.22e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRG--KKRQEA------PPHIFSISDNAYQFMLTDREN 172
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiIQNGEYfdikkePPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 173 QSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEAT-------SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTltssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 246 RFGKFIRIHFG-TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNP--YDYAFVSQGE-I 321
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLsgDRYDYLKKSNcY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 322 TVPSIDDQEELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQNLNSADLL 399
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 400 KALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQL--------DTKQPRQYFIGVLDIAGFEIF 471
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 472 DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF--IDFgMDLAACIELIEK-PMGIFSILEEECMFPKATD 548
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 549 TSFKNKLYEQHLGKSNNFQKPKPAKGKveahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAA 628
Cdd:cd14907 482 EKLLNKIKKQHKNNSKLIFPNKINKDT----FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGED 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 629 AAAEAESGGGGGKKGAKkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEG 708
Cdd:cd14907 558 GSQQQNQSKQKKSQKKD------KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLES 631
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 82524274 709 IRICRKGFPSRILYADFKQRYKVLNasaipegqfidskkasekllgsididhTQYKFGHTKVFFK 773
Cdd:cd14907 632 IRVRKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
100-773 |
8.08e-138 |
|
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: 445.16 E-value: 8.08e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 179 GESGAGKTVNTKRVIQYFATIAvtgekkkeeatsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA------------GGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDS 337
Cdd:cd14904 149 GKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 338 AIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAdKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 417
Cdd:cd14904 229 SLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLS-QVAKMLGLPTTRIEEALCNRSVVTRNESVTVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 418 QTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14904 308 LAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 497 FVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQH--LGKSNNFQKPKPAKg 574
Cdd:cd14904 388 FKTVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 575 kveAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGGGGGKKGAKkkgssfQTV 654
Cdd:cd14904 466 ---TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEGKSGKGTKAP------KSL 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 655 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 734
Cdd:cd14904 537 GSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFP 616
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 82524274 735 SAIPEGqfiDSKKASEKLLGSIDIDHT-QYKFGHTKVFFK 773
Cdd:cd14904 617 PSMHSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
19-832 |
1.64e-135 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 444.47 E-value: 1.64e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 19 KSEKERIEAQNKPFDAKSSVFVVDAKES----------------------FVKATVQ-SREGGKVTAK---TEGGTTVTV 72
Cdd:PTZ00014 2 ARTKEKAKTANKLFRRNSNVEAFDKSGNvlkgfyvwtdkapavkedpdlmFAKCLVLpGSTGEKLTLKqidPPTNSTFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 73 KDDQVY----PMNPPKYDkieDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYR-GKK 147
Cdd:PTZ00014 82 KPEHAFnansQIDPMTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRdAKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 148 RQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATiavtgekkkeeATSGKMQGTLEDQIISAN 227
Cdd:PTZ00014 159 SDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS-----------SKSGNMDLKIQNAIMAAN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 228 PLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLIt 307
Cdd:PTZ00014 228 PVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 308 TNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-----PDGTE 382
Cdd:PTZ00014 307 KSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDaaaisDESLE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 383 VADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGV 462
Cdd:PTZ00014 387 VFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGM 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 463 LDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECM 542
Cdd:PTZ00014 467 LDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 543 FPKATDTSFKNKLYEQhLGKSNNFqkpKPAKGKVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAY 622
Cdd:PTZ00014 547 APGGTDEKFVSSCNTN-LKNNPKY---KPAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRD 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 623 LFSGAAAAAEAESGGgggkkgakkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRC 702
Cdd:PTZ00014 623 LFEGVEVEKGKLAKG--------------QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHS 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 703 NGVLEGIRICRKGFPSRILYADFKQRYKVLNAsAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGLLEE 782
Cdd:PTZ00014 689 LSILEALQLRQLGFSYRRTFAEFLSQFKYLDL-AVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQ 767
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 82524274 783 MRDDKLAQ---LITRTQAMCRGYLARveyQKMVERRESIFCIQYNVRAFMNVK 832
Cdd:PTZ00014 768 IQREKLAAwepLVSVLEALILKIKKK---RKVRKNIKSLVRIQAHLRRHLVIA 817
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
102-773 |
6.59e-135 |
|
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: 437.03 E-value: 6.59e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFML----TDRENQSILI 177
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 178 TGESGAGKTVNTKRVIQYFAtiavtgekkkeEATSGKMQgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgT 257
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIM-----------ELCRGNSQ--LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-R 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 258 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEML-LITTNPYDYAFVSQGEITVPSI--DDQEELMa 334
Cdd:cd14889 149 NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYgLLDPGKYRYLNNGAGCKREVQYwkKKYDEVC- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 335 tdSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEY 413
Cdd:cd14889 228 --NAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 414 VTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLdtkQPRQYF------IGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd14889 306 IQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQACINLANEQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 488 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNFQ 567
Cdd:cd14889 383 LQYFFNHHIFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 568 KPKPAKGKveahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGGGGGKKGAKKK 647
Cdd:cd14889 462 KSRSKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSDN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 648 --GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 725
Cdd:cd14889 538 fnSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEF 617
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 82524274 726 KQRYKVLnasaIPEGQFIDSKKASEKLLGSIDIdhTQYKFGHTKVFFK 773
Cdd:cd14889 618 AERYKIL----LCEPALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
100-773 |
1.20e-132 |
|
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: 430.23 E-value: 1.20e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAA--WMIYTYSGLFCVTVNPYKWLPvyNAEVvAAYRGKKRQEAPPHIFSISDNAYQFMLTDRE---NQS 174
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 175 ILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQG------TLEDQIISANPLLEAFGNAKTVRNDNSSRFG 248
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 249 KFIRIHFGTTG-KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQ-GEITVPSI 326
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLL-LSPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 327 DDQEELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREE----QAEPDGTEVADKAAYLQNLNSADLLKAL 402
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 403 CYPRVKVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFD-FNSLEQLCI 481
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 482 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHl 560
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 561 GKSNNFQKPKPaKGKVEAhFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKssmktlaylfsgaaaaaeaesggggg 640
Cdd:cd14891 475 KRHPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLAS-------------------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 641 kkgakkkgssfqtvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRI 720
Cdd:cd14891 527 --------------SAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRV 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 82524274 721 LYADFKQRYKVLNASAI------PEGQFIdskkasEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14891 593 TYAELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
100-730 |
1.53e-129 |
|
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: 424.30 E-value: 1.53e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYR--------GKKRQEAPPHIFSISDNAYQFML-TD 169
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTledQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVEIGK---RILQTNPILESFGNAQTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEmLLITTNPYDYAFVSQGEIT-----VP 324
Cdd:cd14902 158 FIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD-LLGLQKGGKYELLNSYGPSfarkrAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 325 SIDDQEELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKqkqrEEQAEPDGTEVA-------DKAAYLQNLNSAD 397
Cdd:cd14902 237 ADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFT----AENGQEDATAVTaasrfhlAKCAELMGVDVDK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 398 LLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLD-------TKQPRQYF--IGVLDIAGF 468
Cdd:cd14902 313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsISDEDEELatIGILDIFGF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 469 EIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKAT 547
Cdd:cd14902 393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 548 DTSFKNKLYEQHLGksnnfqkpkpakgkvEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGA 627
Cdd:cd14902 472 NQALSTKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 628 AAAAEAESGGGGGKKGAKKKGSSfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLE 707
Cdd:cd14902 537 NRDSPGADNGAAGRRRYSMLRAP--SVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLE 614
|
650 660
....*....|....*....|...
gi 82524274 708 GIRICRKGFPSRILYADFKQRYK 730
Cdd:cd14902 615 AVRIARHGYSVRLAHASFIELFS 637
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
100-739 |
6.70e-129 |
|
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: 421.24 E-value: 6.70e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYR--GKKRQ---EAP----PHIFSISDNAYQFMLTD- 169
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELG-KLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIM---SNKKPDLIEMLLITTN----PYDYAFVSQGEI- 321
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggDEEEHEKYEFHDGITGglqlPNEFHYTGQGGAp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 322 TVPSIDDQEELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQRE---EQAEPDGTEVADKAAYLQNLNSADL 398
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDgaaEIAEEGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 399 LKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNK 554
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 555 LYEQHLGKSN-----NFQKPKPAKGKVEAHFSLVHYAGTVDYNI-AGWLDKNKDPLNETVVGLYQKSSMktlaylfsgaa 628
Cdd:cd14908 479 LYETYLPEKNqthseNTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESGQQ----------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 629 aaaeaesgggggkkgakkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEG 708
Cdd:cd14908 548 -----------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEA 598
|
650 660 670
....*....|....*....|....*....|.
gi 82524274 709 IRICRKGFPSRILYADFKQRYKVLnASAIPE 739
Cdd:cd14908 599 VRVARSGYPVRLPHKDFFKRYRML-LPLIPE 628
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
100-773 |
9.28e-125 |
|
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: 408.22 E-value: 9.28e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRG-KKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 179 GESGAGKTVNTKRVIQYFATiavtgekkkeeATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS-----------AKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQGEITVPSIDDQEELMATDSA 338
Cdd:cd14876 150 GGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLG-LKEYKFLNPKCLDVPGIDDVADFEEVLES 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 339 IDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQ-----AEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEY 413
Cdd:cd14876 229 LKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 414 VTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14876 309 IEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 494 HHMFVLEQEEYKKEGIEWEFIDFgMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKSNnfqKPKPA 572
Cdd:cd14876 389 DIVFERESKLYKDEGIPTAELEY-TSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSNG---KFKPA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 573 KGKVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGGgggkkgakkkgssfQ 652
Cdd:cd14876 464 KVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKG--------------S 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 653 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 732
Cdd:cd14876 530 LIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL 609
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 82524274 733 NAsAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14876 610 DL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-773 |
6.14e-123 |
|
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: 405.11 E-value: 6.14e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNaevVAAYRGK--KRQEAPPHIFSISDNAYQFMLT-------D 169
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 170 RENQSILITGESGAGKTVNTKRVIQYFATIA----VTGEKKKEEATSGkmqgtleDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSkhttATSSSKRRRAISG-------SELLSANPILESFGNARTLRNDNSS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 246 RFGKFIRIHFG-----TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPD-LIEMLLITTNPYDYAFVSQG 319
Cdd:cd14895 151 RFGKFVRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 320 EITV--PSIDDQEELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA------------- 384
Cdd:cd14895 231 QCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspsslt 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 385 -----DKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQY- 458
Cdd:cd14895 311 vqqhlDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNp 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 459 ----------FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE 528
Cdd:cd14895 391 nkaankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 529 -KPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKpaKGKVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNET 607
Cdd:cd14895 470 qRPSGIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 608 VVGLYQKSSMKTLAYLFSGAAAAAEAESGGGGGKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKT 687
Cdd:cd14895 547 LFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESA 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 688 PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASaipegQFIDSKKASEkLLGSIDIDHTQykFGH 767
Cdd:cd14895 627 SDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAA-----KNASDATASA-LIETLKVDHAE--LGK 698
|
....*.
gi 82524274 768 TKVFFK 773
Cdd:cd14895 699 TRVFLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
100-773 |
3.25e-119 |
|
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: 392.22 E-value: 3.25e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIavtgEKKKEEATSGKMQGTLedqiisanPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 259
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----YQDQTEDRLRQPEDVL--------PILESFGHAKTILNANASRFGQVLRLHL-QHG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEI-TVPSIDDQEELMATDSA 338
Cdd:cd14896 148 VIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 339 IDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQ---AEPDGTEVADKAAYLQnlNSADLLKALCYPRVKVGN-EYV 414
Cdd:cd14896 227 LQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevaAVSSWAEIHTAARLLQ--VPPERLEGAVTHRVTETPyGRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 415 TKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF--IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 492
Cdd:cd14896 305 SRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 493 NHHMFVLEQEEYKKEGIEWEFIDfGMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK- 570
Cdd:cd14896 385 SQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQl 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 571 --PAkgkveahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGGGggkkgakkkg 648
Cdd:cd14896 463 plPV-------FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP---------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 649 ssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 728
Cdd:cd14896 526 ----TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLAR 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 82524274 729 YKVLNASAIPEgqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14896 602 FGALGSERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-732 |
2.43e-112 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 373.03 E-value: 2.43e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKR-QEAPPHIFSISDNAYQFMLTDRE--NQSILI 177
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 178 TGESGAGKTVNTKRVIQYFATIAVTgekkKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 257
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAAS----PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 258 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPyDYAFVSQGEITVpsidDQEELMATDS 337
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGA-AFSWLPNPERNL----EEDCFEVTRE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 338 AIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEyv 414
Cdd:cd14880 234 AMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQ-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 415 tkgqtvQQVYNSV----------GALAKAVYEKMFLWMVTRINQQLDTKQPR-QYFIGVLDIAGFEIFDFNSLEQLCINF 483
Cdd:cd14880 312 ------QQVFKKPcsraecdtrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 484 TNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGK 562
Cdd:cd14880 386 ANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 563 SNNFQKPKPAKgkvEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGGGGGKK 642
Cdd:cd14880 465 NPCLGHNKLSR---EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 643 GAKkkgssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILY 722
Cdd:cd14880 542 PVL-------TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSH 614
|
650
....*....|
gi 82524274 723 ADFKQRYKVL 732
Cdd:cd14880 615 QNFVERYKLL 624
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-735 |
4.66e-108 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 362.76 E-value: 4.66e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKR-QEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFatIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTT 258
Cdd:cd14906 83 ESGSGKTEASKTILQYL--INTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 259 GKLASADIETYLLEKSRVTFQL-KAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQ-------- 329
Cdd:cd14906 161 GKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFKSQssnknsnh 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 330 -------EELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQ---REEQAEPDGTEVADKAAYLQNLNSADLL 399
Cdd:cd14906 241 nnktesiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 400 KALCYPRVKVGNE--YVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRIN----QQLDTKQPRQY-------FIGVLDIA 466
Cdd:cd14906 321 QALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINrkfnQNTQSNDLAGGsnkknnlFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 467 GFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPK 545
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 546 ATDTSFKNKlYEQHLGKSNNFQKPKPAKGKveahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFS 625
Cdd:cd14906 480 GSEQSLLEK-YNKQYHNTNQYYQRTLAKGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 626 GAAAAAEAESGGGGGKKgakkkgssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGV 705
Cdd:cd14906 555 QQITSTTNTTKKQTQSN----------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGV 624
|
650 660 670
....*....|....*....|....*....|
gi 82524274 706 LEGIRICRKGFPSRILYADFKQRYKVLNAS 735
Cdd:cd14906 625 LNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
106-773 |
5.36e-108 |
|
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: 360.36 E-value: 5.36e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRQ-----EAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAtsgkmqgtledqIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTDVQSL------------ILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYdYAFVSQGEI-TVPSIDDQEELMATDSA 338
Cdd:cd14886 155 GLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASKCyDAPGIDDQKEFAPVRSQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 339 IDILgFTSDERVSIYKLTGAVMHYGNMKFKQKQR---EEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVT 415
Cdd:cd14886 234 LEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETII 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 416 KGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 495
Cdd:cd14886 313 SPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 496 MFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLyEQHLgKSNNFQkpkPAKG 574
Cdd:cd14886 393 VFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSFI---PGKG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 575 KVeAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGggggkkgakkkgssfQTV 654
Cdd:cd14886 467 SQ-CNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKG---------------KFL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 655 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL-- 732
Cdd:cd14886 531 GSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILis 610
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 82524274 733 -NASAIPEGQfiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14886 611 hNSSSQNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
101-730 |
6.43e-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: 356.71 E-value: 6.43e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAY----------RGKKRQEAPPHIFSISDNAYQFMLTD 169
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKM-----QGTLEDQIISANPLLEAFGNAKTVRNDNS 244
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPpaspsRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 245 SRFGKFIRIHF-GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNK----KPDLIEMLLITTNPYDYAFVSQG 319
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 320 EITV--PSIDDQEELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQ--KQREEQAEPDGTEVA----------D 385
Cdd:cd14899 242 LCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 386 KAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQL--------------- 450
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 451 DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlAACIELIE-K 529
Cdd:cd14899 402 DDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 530 PMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVV 609
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 610 GLYQKSSMKTLAYLFSGAAAAAEAESGGGGGKKGAKKKGSSFQT----VSALFRENLNKLMTNLRSTHPHFVRCIIPNET 685
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIaavsVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 82524274 686 KTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 730
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-773 |
4.94e-103 |
|
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: 346.41 E-value: 4.94e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 102 VLYNLKERYAAWMI-YTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEA-PPHIFSISDNAY-QFMLTDRENQSILIT 178
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 179 GESGAGKTVNTKRVIQYFAtiavtgeKKKEEATSGKMQGTLEDQIIS----ANPLLEAFGNAKTVRNDNSSRFGKFIRIH 254
Cdd:cd14875 83 GESGSGKTENAKMLIAYLG-------QLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 255 F-GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITV------PSID 327
Cdd:cd14875 156 FdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 328 DQEELMATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQnLNSADLLKalCYpRV 407
Cdd:cd14875 236 DAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFLTACRLLQ-LDPAKLRE--CF-LV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 408 KVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQ----QLDTKQPRqyFIGVLDIAGFEIFDFNSLEQLCINF 483
Cdd:cd14875 312 KSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNAsitpQGDCSGCK--YIGLLDIFGFENFTRNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 484 TNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGK 562
Cdd:cd14875 390 ANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 563 SNNFQKPKPAkgkVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAEsgggggkk 642
Cdd:cd14875 469 SPYFVLPKST---IPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRK-------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 643 gakkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILY 722
Cdd:cd14875 538 ---------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPI 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 723 ADF-KQRYKVLNASAIPEGQFIDSKKASEKLLGS----IDIDHTQYKFGHTKVFFK 773
Cdd:cd14875 609 EQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-773 |
8.89e-99 |
|
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: 335.05 E-value: 8.89e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 182 GAGKTVNTKRVIQYFATIAVTGEKKkeeATSGKMQgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAGSVGGV---LSVEKLN--------AALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFvsqgeITVPSIDDQE------ELMAT 335
Cdd:cd01386 152 ASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF-----GIVPLQKPEDkqkaaaAFSKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 336 DSAIDILGFTSDERVSIYKLTGAVMHYGN---MKFKQKQREEQAEPdgtEVADKAAYLQNLNSADLLKALCYPRVKVGNE 412
Cdd:cd01386 227 QAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 413 YVTKGQTVQQVYNS------------VGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------ 474
Cdd:cd01386 304 QSTTSSGQESPARSssggpkltgveaLEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrga 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 475 SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK---------------PMGIFSILEE 539
Cdd:cd01386 384 TFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLDE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 540 ECMFPKATDTSFKNKLYeQHLGKSNNFQKPKPA-KGKVEAHFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQKS 615
Cdd:cd01386 464 EALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLrRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQES 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 616 SMKTLAylfsgaaaaaeaesgggggkkgakkkgSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPN------ETKTPG 689
Cdd:cd01386 543 QKETAA---------------------------VKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTSS 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 690 AMEHELVLH------QLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL----NASAIPEGQFIDSKKASEKLLGSIDID 759
Cdd:cd01386 596 PAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLapplTKKLGLNSEVADERKAVEELLEELDLE 675
|
730
....*....|....
gi 82524274 760 HTQYKFGHTKVFFK 773
Cdd:cd01386 676 KSSYRIGLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
101-773 |
2.26e-92 |
|
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: 315.22 E-value: 2.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYR---GKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 177
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 178 TGESGAGKTVNTKRVIQYFAtiavtgekkkeeATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 257
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLT------------CRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 258 TGK-LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQGE----ITVPSIDDQEEL 332
Cdd:cd14878 150 RKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTMredvSTAERSLNREKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 333 MATDSAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNE 412
Cdd:cd14878 229 AVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 413 YVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRIN----QQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14878 309 MIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclqSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 489 QQFFNHHMFVLEQEEYKKEGIEWEFI-DFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSNN-- 565
Cdd:cd14878 389 HHYINEVLFLQEQTECVQEGVTMETAySPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKL--QSLLESSNtn 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 566 --FQKPKPAKGKVE-----AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaaaaaeaesggg 638
Cdd:cd14878 467 avYSPMKDGNGNVAlkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF-------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 639 ggkkgakkkGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPS 718
Cdd:cd14878 533 ---------QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPV 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 82524274 719 RILYADFKQRYKVLnASAIPEGQfidsKKASEKLLGSIDIDHTQ---YKFGHTKVFFK 773
Cdd:cd14878 604 RLSFSDFLSRYKPL-ADTLLGEK----KKQSAEERCRLVLQQCKlqgWQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
101-736 |
3.64e-90 |
|
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: 306.05 E-value: 3.64e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKwlPVYNAEVVAAYRgKKRQEAPPHIFSISDNAYQFMLTdRENQSILITGE 180
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVIQYFatiaVTGEKKKEeatsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgtTGK 260
Cdd:cd14898 78 SGSGKTENAKLVIKYL----VERTASTT---------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpdliemLLITTNPYDYAFVSQGEITVpsIDDQEELMATDSAID 340
Cdd:cd14898 143 ITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSAMK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 341 ILGFTSDErvSIYKLTGAVMHYGNMKFKQkqrEEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd14898 215 SLGIANFK--SIEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 421 QQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQyfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14898 290 KQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAK 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 501 QEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKAT--DTSFKNKLYEQHLGKSNNFQKPKpakgkvea 578
Cdd:cd14898 368 QGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNGFINTKARDKIK-------- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 579 hfsLVHYAGTVDYNIAGWLDKNKdplnetvvglyQKSSMKTLAYLFSGAAAAAeaesgggggkkgakkkgssfQTVSALF 658
Cdd:cd14898 439 ---VSHYAGDVEYDLRDFLDKNR-----------EKGQLLIFKNLLINDEGSK--------------------EDLVKYF 484
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82524274 659 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 736
Cdd:cd14898 485 KDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-773 |
3.82e-87 |
|
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: 299.24 E-value: 3.82e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEvvaaYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 182 GAGKTVNTKRVIQYFatiaVTGEKKKEEATSgkmqgTLEDqiisANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14937 79 GSGKTEASKLVIKYY----LSGVKEDNEISN-----TLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14937 146 VSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 342 LGFtSDERVSIYKLTGAVMHYGNMKFKQ-----KQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd14937 225 MNM-HDMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 417 GQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 497 FVLEQEEYKKEGIEWEFIDFGMDlAACIELIEKPMGIFSILEEECMFPKATDTSfknkLYEQHLGKSNNFQKPKPAKGKV 576
Cdd:cd14937 384 YEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKYASTKKDI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 577 EAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAESGggggkkgakkkgssfQTVSA 656
Cdd:cd14937 459 NKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK---------------NLITF 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 657 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRIcRKGFPSRILYADFKQRYKVLNASA 736
Cdd:cd14937 524 KYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYST 602
|
650 660 670
....*....|....*....|....*....|....*..
gi 82524274 737 IPEGQFIDSKKASEKLLGSIDIDhtQYKFGHTKVFFK 773
Cdd:cd14937 603 SKDSSLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
100-773 |
4.92e-86 |
|
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: 298.87 E-value: 4.92e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAA--------WMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRE 171
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 172 NQSILITGESGAGKTVNTKRVIQYFAtiAVTGEKKkeeatsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 251
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLA--AVSDRRH------GADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKML 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 252 RIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtnpYDYafvsqgeitvPSIDDQEE 331
Cdd:cd14887 153 LLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAG---EGD----------PESTDLRR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 332 LMATDSAIDILGftsDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADK---AAYLQNLNS----- 395
Cdd:cd14887 220 ITAAMKTVGIGG---GEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADrshSSEVKCLSSglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 396 -------ADLLKALCYPRVKVGNEYVTKGQTVQQV------YNSVGALA------KAVYEKMFLWMVTRINQQLDTKQPR 456
Cdd:cd14887 297 easrkhlKTVARLLGLPPGVEGEEMLRLALVSRSVretrsfFDLDGAAAardaacKNLYSRAFDAVVARINAGLQRSAKP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 457 QY--------------FIGVLDIAGFEIF---DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFI----D 515
Cdd:cd14887 377 SEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsafP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 516 FGMDLAAC--------IELIEKP--------------MGIFSILEEE-CMFPKATDTSFKNKLYEQHLGK----SNNFQK 568
Cdd:cd14887 457 FSFPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKN 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 569 PKPAKGKVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTlaylfsgaaaaaeaESGGGGGKKGAKKKG 648
Cdd:cd14887 537 ITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACSTYT--------------RLVGSKKNSGVRAIS 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 649 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 728
Cdd:cd14887 603 SRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRR 682
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 82524274 729 YKVLNASAIPEgqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14887 683 YETKLPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
106-772 |
6.58e-83 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 287.14 E-value: 6.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 106 LKERYAAWMIYTY---SGLfcVTVNPYKWLPVYNAEVVAAYR-------GKKRQEAPPHIFSISDNAYQFMLTDRENQSI 175
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 176 LITGESGAGKTVNTKRVIQYFATIAVTGEKkkeeatsgkmqGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 254
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSSHSKK-----------GTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 255 FGTTGKLASADIETYLLEKSRVTfQLKA-ERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFV--SQGEITV--PSIDDQ 329
Cdd:cd14879 157 FNERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGL-DDPSDYALLasYGCHPLPlgPGSDDA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 330 E---ELMAtdsAIDILGFTSDERVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQNLNSADLLKALCY 404
Cdd:cd14879 235 EgfqELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 405 PRVKVGNEYVTkgqtvqqVY-NSVGA------LAKAVYEKMFLWMVTRINQQL-DTKQPRQYFIGVLDIAGFEIFD---F 473
Cdd:cd14879 312 KTKLVRKELCT-------VFlDPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSstgG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 474 NSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEEC-MFPKATDTSF 551
Cdd:cd14879 385 NSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDEQM 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 552 KNKLYEQHLGKSNNFQKPKPAKGKVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSmktlaylfsgaaaaa 631
Cdd:cd14879 464 LEALRKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRGAT--------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 632 eaesgggggkkgakkkgssfQtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRI 711
Cdd:cd14879 529 --------------------Q-----LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAAR 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 82524274 712 CRKGFPSRILYADFKQRYKvlnasaiPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFF 772
Cdd:cd14879 584 LRVEYVVSLEHAEFCERYK-------STLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
100-721 |
1.03e-74 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 264.08 E-value: 1.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRQEA-------PPHIFSISDNAYQFMLTDRE 171
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 172 NQSILITGESGAGKTVNTKRVIQYFATIavtgekkkeeatSGKMQGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKF 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI------------QTDSQMTeRIDKLIYINNILESMSNATTIKNNNSSRCGRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 251 IRIHFGT---------TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGE- 320
Cdd:cd14884 149 NLLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEs 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 321 -----------ITVPSIDDQEELMATDSA-----IDILGFTS-DERV--SIYKLTGAVMHYGNMKFKQkqreeqaepdgt 381
Cdd:cd14884 229 hqkrsvkgtlrLGSDSLDPSEEEKAKDEKnfvalLHGLHYIKyDERQinEFFDIIAGILHLGNRAYKA------------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 382 evadkAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRIN---------QQLDT 452
Cdd:cd14884 297 -----AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekDESDN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 453 KQPRQY---FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDfgmdLAACIELIEK 529
Cdd:cd14884 372 EDIYSIneaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDV----APSYSDTLIF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 530 PMGIFSILEEECMFP----KATDTSFKNKLY----EQHLGKSNNFQKPKP-------AKGKVEAH-FSLVHYAGTVDYNI 593
Cdd:cd14884 448 IAKIFRRLDDITKLKnqgqKKTDDHFFRYLLnnerQQQLEGKVSYGFVLNhdadgtaKKQNIKKNiFFIRHYAGLVTYRI 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 594 AGWLDKNKDPLNETVVGLYQKSSMKTLaylfsgaaaaaeaesggggGKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTH 673
Cdd:cd14884 528 NNWIDKNSDKIETSIETLISCSSNRFL-------------------REANNGGNKGNFLSVSKKYIKELDNLFTQLQSTD 588
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 82524274 674 PHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 721
Cdd:cd14884 589 MYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
101-753 |
9.18e-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: 248.10 E-value: 9.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPvyNAEVVAAYRGKKRQeapPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 181 SGAGKTVNTKRVI-QYFAtiaVTGEKKKEEATSgkmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 259
Cdd:cd14881 77 SGSGKTYASMLLLrQLFD---VAGGGPETDAFK---------HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPD-LIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 338
Cdd:cd14881 144 ALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEeRVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 339 IDILG--FTSDERVsiyklTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLqNLNSADLLKALcYPRVKVgneyvTK 416
Cdd:cd14881 224 LGILGipFLDVVRV-----LAAVLLLGNVQFIDGGGLEVDVKGETELKSVAALL-GVSGAALFRGL-TTRTHN-----AR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 417 GQTVQQVyNSVG-------ALAKAVYEKMFLWMVTRINQQLD-----TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFT 484
Cdd:cd14881 292 GQLVKSV-CDANmsnmtrdALAKALYCRTVATIVRRANSLKRlgstlGTHATDGFIGILDMFGFEDPKPSQLEHLCINLC 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 485 NEKLQQFFNHHMFVLEQEEYKKEGIEWEF-IDFgMDLAACIELIEK-PMGIFSILEEECMfPKATDTSFKNKLYEQHlgK 562
Cdd:cd14881 371 AETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQH--R 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 563 SNN-FQKPKPAKGKVeahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMktlaylfsgaaaaaeaesgggggk 641
Cdd:cd14881 447 QNPrLFEAKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNC------------------------ 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 642 kgakkkGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 721
Cdd:cd14881 500 ------NFGFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMR 573
|
650 660 670
....*....|....*....|....*....|..
gi 82524274 722 YADFKQRYKVLnASAIPEGQFIDSKKASEKLL 753
Cdd:cd14881 574 FKAFNARYRLL-APFRLLRRVEEKALEDCALI 604
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
101-732 |
3.37e-64 |
|
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: 231.68 E-value: 3.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYrgkkrqeappHIFSISDNAYQFMLTDREN-QSILITG 179
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 180 ESGAGKTVNTKRVIQYfatiaVTGEKKKEEATSgkmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14874 72 ESGSGKSYNAFQVFKY-----LTSQPKSKVTTK---------HSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14874 138 LTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLEDAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 340 DILGFTSDERVSIYKLTGAVMHYGNMKFKQKqREEQAEPDGTEVADKA-----AYLQNLNSADLLKALCyPRVKVGNEYv 414
Cdd:cd14874 217 HVLGFSDDHCISIYKIISTILHIGNIYFRTK-RNPNVEQDVVEIGNMSevkwvAFLLEVDFDQLVNFLL-PKSEDGTTI- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 415 tkgqTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLdtKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14874 294 ----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHL--KCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 494 HHMFVLEQEEYKKEGIEwefIDFGM----DLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSnNFQK 568
Cdd:cd14874 368 KHSFHDQLVDYAKDGIS---VDYKVpnsiENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-SYGK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 569 pkpAKGKVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaaaaaeaesgggggKKGAKKKG 648
Cdd:cd14874 444 ---ARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLF----------------ESYSSNTS 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 649 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 728
Cdd:cd14874 505 DMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQ 584
|
....
gi 82524274 729 YKVL 732
Cdd:cd14874 585 YRCL 588
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
102-773 |
2.33e-63 |
|
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: 229.63 E-value: 2.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 182 GAGKTVNTKRVIQYFATIavtgekkkeeatsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14882 83 YSGKTTNARLLIKHLCYL-------------GDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMS--NKKPDLIEMLLITTNPYDYAFVSQG-------------EITVPSI 326
Cdd:cd14882 150 SGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 327 DDQEELMAtdsaidILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREeqAEPDGTEVADKAAYLQNLNSADLLKALCYPR 406
Cdd:cd14882 230 KEFEEILK------DLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 407 VKVGNEYVTKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTkqPR-----QYFIGVLDIAGFEIFDFNSLEQLCI 481
Cdd:cd14882 302 LIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 482 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEecmfpKATDTSFKNKLYEQHLG 561
Cdd:cd14882 380 NTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 562 KSNNFQKPkpakgkVEAH-FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaaaaaeaesggggg 640
Cdd:cd14882 455 KHSQFVKK------HSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMF---------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 641 kkgAKKKGSSFQTVSALFR----ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGF 716
Cdd:cd14882 513 ---TNSQVRNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGF 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 82524274 717 PSRILYADFKQRYKVLnasAIPEGQFIDSKKASEKLLgSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14882 590 SYRIPFQEFLRRYQFL---AFDFDETVEMTKDNCRLL-LIRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
106-716 |
2.56e-63 |
|
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: 230.36 E-value: 2.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 184
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 185 KTVNTKRVIQYFATIAVTGEKkkeeatsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASA 264
Cdd:cd14905 85 KSENTKIIIQYLLTTDLSRSK------------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 265 DIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPDLIEMLLITTNPYDYaFVSQGEITVPSIDDQEELMATDSAIDILG 343
Cdd:cd14905 153 KLYSYFLDENRVTYQNKGERNFHIFYQFLKGiTDEEKAAYQLGDINSYHY-LNQGGSISVESIDDNRVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 344 FTSDERVSIYKLTGAVMHYGNMKFKQKQREeqaepdgTEVADKAAYlqnlnsADLLKALCYPRVKVGNEYVT-KGQTVQQ 422
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRTLI------ESLSHNITFDSTKLENILISdRSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 423 VYNSVGALAKAVYEKMFLWMVTRINQQLdtkQPRQY--FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14905 299 AVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 501 QEEYKKEGIEWEFIDFGMDLAACIELIEKpmgIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNFQKpKPAKgkveahF 580
Cdd:cd14905 376 QREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL-QNFLSRHHLFGK-KPNK------F 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 581 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKtlaYLFSGA---AAAAEAESGGGGGKKGAKKKGSSFQTVSAL 657
Cdd:cd14905 445 GIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITK---YLFSRDgvfNINATVAELNQMFDAKNTAKKSPLSIVKVL 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 658 FR------ENLNK-----------------------LMTNLRSTHP---------HFVRCIIPNETKTPGAMEHELVLHQ 699
Cdd:cd14905 522 LScgsnnpNNVNNpnnnsgggggggnsgggsgsggsTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQ 601
|
650
....*....|....*..
gi 82524274 700 LRCNGVLEGIRICRKGF 716
Cdd:cd14905 602 IKSLCLLETTRIQRFGY 618
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
103-730 |
2.31e-62 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 229.09 E-value: 2.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRQ----------EAPPHIFSISDNAYQFMLTDREN 172
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 173 QSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIR 252
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 253 IHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKK--PDLIEMLLITTNPYDYAFVSQG--EITVPSID- 327
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFALDa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 328 -DQEELMATDSAIDIlgfTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDG--TEVADKAAYL-----QNLNSADLL 399
Cdd:cd14893 244 rDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGAnsTTVSDAQSCAlkdpaQILLAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 400 KAlcYPRV------------KVGNEYVT--KGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQL----DTKQPRQYFIG 461
Cdd:cd14893 321 EV--EPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVIN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 462 -----VLDIAGFEIFD--FNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWE-------FIDFGMDLAACIELI 527
Cdd:cd14893 399 sqgvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVEnrltvnsNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 528 E-KPMGIFSILEEECMFPKATDTSFKNKLY----------EQHLGKSNNFQKPKPAKgKVEAHFSLVHYAGTVDYNIAGW 596
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFsgneavgglsRPNMGADTTNEYLAPSK-DWRLLFIVQHHCGKVTYNGKGL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 597 LDKNKDPLNETVVGLYQkSSMKTLAYLFSGAAAAAEAESGGGGGKKGAKKKGSSFQTVSALFRENLN------------- 663
Cdd:cd14893 558 SSKNMLSISSTCAAIMQ-SSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqa 636
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82524274 664 -KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 730
Cdd:cd14893 637 dALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
122-253 |
6.95e-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: 6.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 122 FCVTVNPYKWLPVYNAEVV-AAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIA 200
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 201 VTGEKKKEEATS---GKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 253
Cdd:cd01363 81 FNGINKGETEGWvylTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-771 |
1.01e-44 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 175.02 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYR-GKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 179 GESGAGKTVNTKRVIQYFA-----------TIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAyqvkgsrrlptNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 248 GKFIRIHFGTTgKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSID 327
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK-NIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 328 DQEELMATDSAIDILGFTSDERVSIYKLTGAVMHYGN-------------MKFKQKQRE----------EQAEPDGTEVA 384
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 385 DKAAYL-QNLNSADLLKALCYPRVK-VGNEYV-TKGQTVQQVYNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF-- 459
Cdd:cd14938 319 VKNLLLaCKLLSFDIETFVKYFTTNyIFNDSIlIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININtn 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 460 -IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM--GIFSI 536
Cdd:cd14938 399 yINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFSL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 537 LEEECMfPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGkVEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSS 616
Cdd:cd14938 479 LENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITG-NKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 617 MKTLAYLFSGAAAAAEAESGGGGGKKGAKKKGSSF--------QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTP 688
Cdd:cd14938 557 NEYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFkrrydtknQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKRE 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 689 -GAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAsaipegqfiDSKKASEKLLGSIDIDHTQYKFGH 767
Cdd:cd14938 637 lCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMIGN 707
|
....
gi 82524274 768 TKVF 771
Cdd:cd14938 708 NMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1180-1938 |
8.65e-31 |
|
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: 132.87 E-value: 8.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1180 KMRRdlEEATLQHEATAATLrKKHADSVAELGEQIDNLQRVKQKLEKEKsEMKMEIDDLAsnMEVISKSKGNLEKMCRTL 1259
Cdd:TIGR02168 171 KERR--KETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERYK-ELKAELRELE--LALLVLRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1260 EDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEeikaksalaha 1339
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN----------- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1340 lqssrhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKK------LAQRLQDAEEHVEA 1413
Cdd:TIGR02168 314 ----------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaeleeLESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1414 VNAKCASLEKTKQRLQNEVEDLMIDVERtnaacaaLDKKQRNFDKILAEWKQKYEEthAELEASQKESRSLSTELFKIKN 1493
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLER-------LEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1494 AYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEA----------SLEHEEG 1563
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlseLISVDEG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1564 KILRIQLEL------------NQVKSEID----------RKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRL 1621
Cdd:TIGR02168 535 YEAAIEAALggrlqavvvenlNAAKKAIAflkqnelgrvTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1622 KKKMEGDLNEMEI--QLNHSNRMAAEALRNYRNtqgILKDTQLHLDDALRGQEDLKEQLAMVERRAnllqaEIEELRATL 1699
Cdd:TIGR02168 615 RKALSYLLGGVLVvdDLDNALELAKKLRPGYRI---VTLDGDLVRPGGVITGGSAKTNSSILERRR-----EIEELEEKI 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1700 EQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKE 1779
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1780 QDTSAHLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELEGEVENEQKRNVEAIKGLRKHERRVKELTY 1859
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 82524274 1860 QTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKI 1938
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
864-1749 |
8.78e-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: 123.24 E-value: 8.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 864 EKAKENLAKAEAKRKELEEKMvalmqekNDLQLQVqseadsladaeERCDQLIKTKIQLEAKIKEV-TERAEDEEEINAE 942
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQL-------KSLERQA-----------EKAERYKELKAELRELELALlVLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 943 LTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEED 1022
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1023 KVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKKEFEMSNLQSKIE 1102
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1103 DEQALGMQLQKKIKELQarieeleeeIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMR 1182
Cdd:TIGR02168 404 RLEARLERLEDRRERLQ---------QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1183 RDLEEATLQHEATAATLrkkhaDSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQ 1262
Cdd:TIGR02168 475 QALDAAERELAQLQARL-----DSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQA 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1263 VseLKTKEEEQQRLINELTAQRGRLQT---ESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHA 1339
Cdd:TIGR02168 550 V--VVENLNAAKKAIAFLKQNELGRVTflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLV 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1340 LQSSRHDCDLLREQYEEEQEAKAELQRAmsKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQrlqdAEEHVEAVNAKCA 1419
Cdd:TIGR02168 628 VDDLDNALELAKKLRPGYRIVTLDGDLV--RPGGVITGGSAKTNSSILERRREIEELEEKIEE----LEEKIAELEKALA 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1420 SLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESL 1499
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1500 DHLETLKRENKNLQQEISDLTEQIAEG-------GKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLEL 1572
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELraeltllNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1573 NQVKSEIDrKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRN 1652
Cdd:TIGR02168 862 EELEELIE-ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1653 TQGIL-KDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEEL-RATLEqtersrkiAEQELLDASERVQLLHTQNTSL 1730
Cdd:TIGR02168 941 LQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgPVNLA--------AIEEYEELKERYDFLTAQKEDL 1012
|
890
....*....|....*....
gi 82524274 1731 INTKKKLETDISQIQGEME 1749
Cdd:TIGR02168 1013 TEAKETLEEAIEEIDREAR 1031
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
850-1595 |
1.40e-26 |
|
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: 119.02 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 850 AETEKEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLqlqvqseadsladaeERCDQLIKTKIQLEAKI--K 927
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA---------------ERYQALLKEKREYEGYEllK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 928 EVTERAEDEEEINAELTAKKRKLEDecseLKKDIDDLELTLAKVEKEKHATENKVKNLTE-EMAGLDETIAKLTKEKKAL 1006
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEK----LTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1007 Q---EAHQQTLDDLQAEEDKvntlTKAKI-KLEQQVDDLEGSLEQEKKIRmdlerakRKLEGDLKLAQESTMDVENDKQQ 1082
Cdd:TIGR02169 307 ErsiAEKERELEDAEERLAK----LEAEIdKLLAEIEELEREIEEERKRR-------DKLTEEYAELKEELEDLRAELEE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1083 LDEKLKKKEFEMSNLQSKIEDeqalgmqLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGG 1162
Cdd:TIGR02169 376 VDKEFAETRDELKDYREKLEK-------LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1163 ATSAQiemnkkrEAEFQKMRRDLEEATLQHEATAATLRKkhadsvaeLGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNM 1242
Cdd:TIGR02169 449 EIKKQ-------EWKLEQLAADLSKYEQELYDLKEEYDR--------VEKELSKLQRELAEAEAQARASEERVRGGRAVE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1243 EVISKSKGNlekmcrtLEDQVSELKTKEEEQQRLINelTAQRGRLQ----------TESGEYSRQ-------------LD 1299
Cdd:TIGR02169 514 EVLKASIQG-------VHGTVAQLGSVGERYATAIE--VAAGNRLNnvvveddavaKEAIELLKRrkagratflplnkMR 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1300 EKDSLVSQLSRG--------------------KQAF-----TQQIEELKRQ--------LEEEIKAKS--------ALAH 1338
Cdd:TIGR02169 585 DERRDLSILSEDgvigfavdlvefdpkyepafKYVFgdtlvVEDIEAARRLmgkyrmvtLEGELFEKSgamtggsrAPRG 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1339 ALQSSRHDCDLLREQYEEEQEAKAELQRAMSKAN---SEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQDAEEHVEAVN 1415
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRrieNRLDELSQELS-DASRKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1416 AKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEwkQKYEETHAELEASQKESRSLSTELFKIKNAY 1495
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1496 EESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQV 1575
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
810 820
....*....|....*....|
gi 82524274 1576 KSEIDRKIAEKDEEIDQLKR 1595
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSE 921
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
847-1596 |
2.31e-26 |
|
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: 118.63 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 847 LKSAETEKEMANMKEEFEKAKENLA----KAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQL 922
Cdd:TIGR02169 191 LIIDEKRQQLERLRREREKAERYQAllkeKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 923 EAKIKEVTERAED--EEEINA------ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDE 994
Cdd:TIGR02169 271 EQLLEELNKKIKDlgEEEQLRvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 995 TIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTM 1074
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1075 DVENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLS------- 1147
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEervrggr 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1148 -----------------RELEEISER----LEEAGGA------------TSAQIEMNKKREA------EFQKMRRDLEEA 1188
Cdd:TIGR02169 511 aveevlkasiqgvhgtvAQLGSVGERyataIEVAAGNrlnnvvveddavAKEAIELLKRRKAgratflPLNKMRDERRDL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1189 TLQHEATAAtlrkKHADSVAELGEQIDNLQR-------VKQKLEKEKSEM---KM-----EIDDLASNMEVISKSKGNLE 1253
Cdd:TIGR02169 591 SILSEDGVI----GFAVDLVEFDPKYEPAFKyvfgdtlVVEDIEAARRLMgkyRMvtlegELFEKSGAMTGGSRAPRGGI 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1254 KMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAK 1333
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1334 SALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQDAEEHVEA 1413
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL---SKLEEEVSRIEARLREIEQKLNR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1414 VNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKN 1493
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1494 AYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIK------KQIEQEKSELQAALEEAE-----ASLEHEE 1562
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEpvnmlAIQEYEE 983
|
810 820 830
....*....|....*....|....*....|....*
gi 82524274 1563 GKILRIQLELNQVKSEIDRK-IAEKDEEIDQLKRN 1596
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEEERKaILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1152-1878 |
2.65e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 118.24 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1152 EISERLEEAGGATSAqIEMNKKREaEFQKMRRDLEEATLQHEATAATLRKKHADsVAELGEQIDNLQRVKQKLEKEKSEM 1231
Cdd:TIGR02168 217 ELKAELRELELALLV-LRLEELRE-ELEELQEELKEAEEELEELTAELQELEEK-LEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1232 KMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRG 1311
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1312 KQAFTQQIEE--------------LKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQeaKAELQRAMSKANSEVAQ 1377
Cdd:TIGR02168 374 LEELEEQLETlrskvaqlelqiasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1378 WRTKYEtDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVED----------------------- 1434
Cdd:TIGR02168 452 LQEELE-RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkallknqsglsgilgvlselis 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1435 --------------------LMIDVERTNAACAALDKKQRNFDKILAE---WKQKYEETHAELEASQKESRSLSTELFKI 1491
Cdd:TIGR02168 531 vdegyeaaieaalggrlqavVVENLNAAKKAIAFLKQNELGRVTFLPLdsiKGTEIQGNDREILKNIEGFLGVAKDLVKF 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1492 KNAYE-------------ESLDHLETLKRENK-------------------------------NLQQEISDLTEQIAEGG 1527
Cdd:TIGR02168 611 DPKLRkalsyllggvlvvDDLDNALELAKKLRpgyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1528 KRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRkiaeKDEEIDQLKRNHIRVVESMQST 1607
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEAEIEEL 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1608 LDAEIRSRNDAIRLKKKM---EGDLNEMEIQLNHSNRMAAEAlrnyrntQGILKDTQLHLDDALRGQEDLKEQLAMVERR 1684
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIeelEAQIEQLKEELKALREALDEL-------RAELTLLNEEAANLRERLESLERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1685 ANLLQAEIEELRATLEQtersrkiAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKK 1764
Cdd:TIGR02168 840 LEDLEEQIEELSEDIES-------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1765 AITDAAMMAEELKKEQdtsAHLERMKKNLEQTVKDL--QHRLDEAEQLALK-GGKKQIQKLEARVRELEGEVENEQKRNV 1841
Cdd:TIGR02168 913 LRRELEELREKLAQLE---LRLEGLEVRIDNLQERLseEYSLTLEEAEALEnKIEDDEEEARRRLKRLENKIKELGPVNL 989
|
810 820 830
....*....|....*....|....*....|....*..
gi 82524274 1842 EAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKL 1878
Cdd:TIGR02168 990 AAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1615 |
1.36e-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: 115.92 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 847 LKSAETEKEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKI 926
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 927 KEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKAL 1006
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1007 QEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLEraKRKLEGDLKLAQESTMDVENDKQQLDEK 1086
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1087 LKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAER---ASRAKAEKQRSDLSRELEEISER------- 1156
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsEGVKALLKNQSGLSGILGVLSELisvdegy 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1157 ---LEEAGGATSAQIEMNKKREAefqkmrRDLEEATLQHEATAATL----RKKHADSVAELGEQIDNLQRVKQKL-EKEK 1228
Cdd:TIGR02168 536 eaaIEAALGGRLQAVVVENLNAA------KKAIAFLKQNELGRVTFlpldSIKGTEIQGNDREILKNIEGFLGVAkDLVK 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1229 SEMKME------------IDDLASNMEVISK-------------------------SKGNLEKMCRTLEdqVSELKTKEE 1271
Cdd:TIGR02168 610 FDPKLRkalsyllggvlvVDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsAKTNSSILERRRE--IEELEEKIE 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1272 EQQRLINELTAQRGRLQTEsgeysrqLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLR 1351
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKE-------LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1352 EQYEEEQEAKAELQRAMSKANSEVAQWRtkyetdaiQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNE 1431
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELE--------AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1432 VEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKN 1511
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1512 LQQEISDLTEQIAEGGKRIHELE-KIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDR--------- 1581
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEvRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaai 992
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 82524274 1582 ----KIAEKDEEIDQLKRNHIRVVESMQST---LDAEIRSR 1615
Cdd:TIGR02168 993 eeyeELKERYDFLTAQKEDLTEAKETLEEAieeIDREARER 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1317-1918 |
3.55e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 114.26 E-value: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1317 QQIEELKRQ---------LEEEIKAKSALAHALQSsrhdcDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYEtdai 1387
Cdd:COG1196 200 RQLEPLERQaekaeryreLKEELKELEAELLLLKL-----RELEAELEELEAELEELEAELEELEAELAELEAELE---- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1388 qrteELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKY 1467
Cdd:COG1196 271 ----ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1468 EETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSEL 1547
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1548 QAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRsRNDAIRLKKKMEG 1627
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-LLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1628 DLNEMEIQLNHSN------------------RMAAEALRNYRNTQGILKDTQlhldDALRGQEDLKEQLAmveRRANLLQ 1689
Cdd:COG1196 506 FLEGVKAALLLAGlrglagavavligveaayEAALEAALAAALQNIVVEDDE----VAAAAIEYLKAAKA---GRATFLP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1690 AEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTkkkLETDISQIQGEMEDIVQEARNAEEKAKKA---- 1765
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL---LGRTLVAARLEAALRRAVTLAGRLREVTLegeg 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1766 ITDAAMMAEELKKEQDTSahLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNVEAIK 1845
Cdd:COG1196 656 GSAGGSLTGGSRRELLAA--LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 82524274 1846 GLRKHERRVKELTYQTEEDRKNVLRLQDLvDKLQSKVKAYKRQAEEAEeqsNVNLAkfrKIQhELEEAEERAD 1918
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDL-EELERELERLEREIEALG---PVNLL---AIE-EYEELEERYD 798
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1126-1916 |
4.89e-25 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 114.01 E-value: 4.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1126 EeeieaerasrAKAEKQRsdlsRELEEISERLEEaggatsAQIEMNKKREaEFQKMRRDLEEAtlqhEATAATLRKKHAD 1205
Cdd:TIGR02169 169 D----------RKKEKAL----EELEEVEENIER------LDLIIDEKRQ-QLERLRREREKA----ERYQALLKEKREY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1206 SVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQ-QRLINELTAQR 1284
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1285 GRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAEL 1364
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1365 QRamskansEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVErtna 1444
Cdd:TIGR02169 384 RD-------ELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK---- 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1445 acaALDKKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTElfkiknayeesLDHLETLKRENKNLQQEISDLTEQIA 1524
Cdd:TIGR02169 452 ---KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE-----------LAEAEAQARASEERVRGGRAVEEVLK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1525 EGGKRIHELekiKKQIEQEKSELQAALEEAEAS------LEHEEGKILRIQ------------LELNQVKSE--IDRKIA 1584
Cdd:TIGR02169 518 ASIQGVHGT---VAQLGSVGERYATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrrkagratfLPLNKMRDErrDLSILS 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1585 EKDE--------EIDQLKRNHIR-------VVESMQS-----------TLDAEI-----------RSRNDAIRLKKKMEG 1627
Cdd:TIGR02169 595 EDGVigfavdlvEFDPKYEPAFKyvfgdtlVVEDIEAarrlmgkyrmvTLEGELfeksgamtggsRAPRGGILFSRSEPA 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1628 DLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRK 1707
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1708 IAEQELLDASERVQLLHTQNTSLINTKKKLETDIS-----QIQGEMEDIVQEARNAEEKAKKaiTDAAMMAEELKKEQdt 1782
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLRE--IEQKLNRLTLEKEY-- 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1783 sahLERMKKNLEQTVKDLQHRLDE--AEQLALKGGKK----QIQKLEARVRELEGEVENEQKRNVEAIKGLRKHERRVKE 1856
Cdd:TIGR02169 831 ---LEKEIQELQEQRIDLKEQIKSieKEIENLNGKKEeleeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1857 LTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNvNLAKFRKIQHELEEAEER 1916
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLEDVQAELQRVEEE 966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
842-1595 |
6.69e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 113.61 E-value: 6.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 842 KIKPLLKSAETEKEMANMKEEFEKAKENLAKAEAKrkELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLiktkiq 921
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRELELALLVLRLE--ELREELEELQEELKEAEEELEELTAELQELEEKLEEL------ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 922 lEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTK 1001
Cdd:TIGR02168 273 -RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1002 EKKALQEAHQQTLDDLQAEEDKVNTLTKAkikLEQQVDDLEGSLEQEKKIRMDLERAKRKLEgDLKLAQEstmdvENDKQ 1081
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQ---LETLRSKVAQLELQIASLNNEIERLEARLE-RLEDRRE-----RLQQE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1082 QLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAG 1161
Cdd:TIGR02168 423 IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1162 GATS--AQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAelgeqIDNLQRVKQKLE--KEKSEMK---ME 1234
Cdd:TIGR02168 503 GFSEgvKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVV-----VENLNAAKKAIAflKQNELGRvtfLP 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1235 IDDL------ASNMEVISKSKG------NLEKMCRTLEDQVSEL------KTKEEEQQRLINELTAQ------------- 1283
Cdd:TIGR02168 578 LDSIkgteiqGNDREILKNIEGflgvakDLVKFDPKLRKALSYLlggvlvVDDLDNALELAKKLRPGyrivtldgdlvrp 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1284 -----RGRLQTESG--EYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQY-- 1354
Cdd:TIGR02168 658 ggvitGGSAKTNSSilERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLar 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1355 -EEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqdaEEHVEAVNAKCASLEKTKQRLQNEVE 1433
Cdd:TIGR02168 738 lEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL----EAQIEQLKEELKALREALDELRAELT 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1434 DLmidvertNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQ 1513
Cdd:TIGR02168 814 LL-------NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1514 QEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELN-----------QVKSEIDRK 1582
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeeysltleeaeALENKIEDD 966
|
810
....*....|...
gi 82524274 1583 IAEKDEEIDQLKR 1595
Cdd:TIGR02168 967 EEEARRRLKRLEN 979
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
924-1810 |
1.01e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 113.24 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 924 AKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKdIDDLELTLAKVE-----KEKHATENKVKNLTEEMAGLDETIAK 998
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 999 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAK-IKLEQQVDDLEGSLEQekkirmdlerakrkLEGDLKLAQESTMDVE 1077
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAEIAS--------------LERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1078 NDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERL 1157
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1158 EEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKhADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDD 1237
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1238 lasnmeviskskgnlekmcrtLEDQVSELktkeeeqQRLINELTAQRGRLQTESGEYSRQLDEKDS-------LVSQLSR 1310
Cdd:TIGR02169 481 ---------------------VEKELSKL-------QRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1311 GKQAFTQQIEelkrqleeeikakSALAHALQSSRHDCDLLRE---QYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAI 1387
Cdd:TIGR02169 533 VGERYATAIE-------------VAAGNRLNNVVVEDDAVAKeaiELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1388 QRTEELEEAKKKLAQRLQDAEEHVEAVNakcaSLEkTKQRLQNEVEDLMID---VERTNAACAALDKKQRNFDKILAEwK 1464
Cdd:TIGR02169 600 GFAVDLVEFDPKYEPAFKYVFGDTLVVE----DIE-AARRLMGKYRMVTLEgelFEKSGAMTGGSRAPRGGILFSRSE-P 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1465 QKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEK 1544
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1545 SELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDR-KIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKK 1623
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1624 KMEGDLNEM-EIQLNHSNRMAAEALRN--YRNTQGILKDTQLHLddalrgqEDLKEQLAMVERRANLLQAEIEELRATLE 1700
Cdd:TIGR02169 834 EIQELQEQRiDLKEQIKSIEKEIENLNgkKEELEEELEELEAAL-------RDLESRLGDLKKERDELEAQLRELERKIE 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1701 QTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQgeMEDIVQEARNAEEKAKKAITDAAMMA-EELKKE 1779
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL--SLEDVQAELQRVEEEIRALEPVNMLAiQEYEEV 984
|
890 900 910
....*....|....*....|....*....|.
gi 82524274 1780 QDTSAHLERMKKNLEQTVKDLQHRLDEAEQL 1810
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1148-1938 |
1.12e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 109.77 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1148 RELEEISERLEEAggatsaQIEMNKKREaEFQKMRRDLEEAtlqhEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKE 1227
Cdd:TIGR02169 177 EELEEVEENIERL------DLIIDEKRQ-QLERLRREREKA----ERYQALLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1228 KSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQ-QRLINELTAQRGRLQTESGEYSRQLDEKDSLVS 1306
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1307 QLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRamskansEVAQWRTKYEtDA 1386
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-------ELKDYREKLE-KL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1387 IQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVErtnaacaALDKKQRNFDKILAEWKQK 1466
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK-------KQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1467 YEETHAELEASQKESRSLSTELfkiknayeeslDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELekiKKQIEQEKSE 1546
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQREL-----------AEAEAQARASEERVRGGRAVEEVLKASIQGVHGT---VAQLGSVGER 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1547 LQAALEEAEAS------LEHEEGKILRIQ------------LELNQVKSE--IDRKIAEKDE--------EIDQLKRNHI 1598
Cdd:TIGR02169 537 YATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrrkagratfLPLNKMRDErrDLSILSEDGVigfavdlvEFDPKYEPAF 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1599 R-------VVESMQSTldaeiRSRNDAIRLKKkMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQ 1671
Cdd:TIGR02169 617 KyvfgdtlVVEDIEAA-----RRLMGKYRMVT-LEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1672 EDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVqllhtqntslintkKKLETDISQIQGEMEdi 1751
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL--------------EELEEDLSSLEQEIE-- 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1752 vqearNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMkknleqtvkDLQHRLDEAEQLALKGgKKQIQKLEARVRELEG 1831
Cdd:TIGR02169 755 -----NVKSELKELEARIEELEEDLHKLEEALNDLEAR---------LSHSRIPEIQAELSKL-EEEVSRIEARLREIEQ 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1832 EVENEQKRNVEAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNVNLAKFRKIQHELE 1911
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
810 820
....*....|....*....|....*..
gi 82524274 1912 EAEERADIAESQVNKLRVKSREVHTKI 1938
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
840-1436 |
5.84e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.33 E-value: 5.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 840 YFKIKPLLKSAETE---KEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLI 916
Cdd:COG1196 215 YRELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 917 KTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETI 996
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 997 AKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDV 1076
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1077 ENDKQQLDEKLKKKEFEMSNLQSKIEDEQALgmQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEIS-- 1154
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEE--LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgv 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1155 -ERLEEAGGATSAQIEMNKKREAEFQ-KMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMK 1232
Cdd:COG1196 533 eAAYEAALEAALAAALQNIVVEDDEVaAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1233 MEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGk 1312
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE- 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1313 qafTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAqwrtKYETDAIQRTEE 1392
Cdd:COG1196 692 ---ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPEPPDLEE 764
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 82524274 1393 LEEAKKKLAQRLQD-------AEEHVEAVNAKCASLEKTKQRLQNEVEDLM 1436
Cdd:COG1196 765 LERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLE 815
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
861-1603 |
3.96e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.84 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 861 EEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEIN 940
Cdd:PTZ00121 1191 EELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 941 AELTAKKRKLED-ECSELKKDIDDLEltlaKVEKEKHATENKVKnlTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQA 1019
Cdd:PTZ00121 1271 AIKAEEARKADElKKAEEKKKADEAK----KAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1020 EEdkvntltKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKKEFEMSNLQS 1099
Cdd:PTZ00121 1345 AE-------AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1100 KIEDEQALGMQLQKKIKELQARIEELEeeieaerasRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEfq 1179
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEEAK---------KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-- 1486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1180 KMRRDLEEATLQ-HEATAATLRKKHADSVAELGEQidnlqrvKQKLEKEKSEMKMEIDDLASNMEvisksKGNLEKMCRT 1258
Cdd:PTZ00121 1487 EAKKKAEEAKKKaDEAKKAAEAKKKADEAKKAEEA-------KKADEAKKAEEAKKADEAKKAEE-----KKKADELKKA 1554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1259 LEDQVSELKTKEEEQQRlinelTAQRGRLQTESGEYSRQLDEKdSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSalAH 1338
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKK-----AEEDKNMALRKAEEAKKAEEA-RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE--LK 1626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1339 ALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAiQRTEEL---EEAKKKLAQRLQDAEEH---VE 1412
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaEEDEKKAAEALKKEAEEakkAE 1705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1413 AVNAKCASLEKTKQRLQNEVEDLMIDVERTnaacaaldKKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIK 1492
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1493 NAY-EESLDHLETLKR-ENKNLQQEISDLTEQIAEGGKRIHELEKIKKqiEQEKSELQAALEEAEASLEhEEGKILRIQL 1570
Cdd:PTZ00121 1778 EAViEEELDEEDEKRRmEVDKKIKDIFDNFANIIEGGKEGNLVINDSK--EMEDSAIKEVADSKNMQLE-EADAFEKHKF 1854
|
730 740 750
....*....|....*....|....*....|...
gi 82524274 1571 ELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVES 1603
Cdd:PTZ00121 1855 NKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1142-1755 |
3.99e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.63 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1142 QRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRkkhadsvaELGEQIDNLQRVK 1221
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY--------ELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1222 QKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEK 1301
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1302 DSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSsrhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTK 1381
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE-------LEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1382 YETDAIQRTEELEEAKKKLAQRLQDAEEHVEAvnakcASLEKTKQRLQNEVEDLMIDVERtnaacAALDKKQRNFDKILA 1461
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEA-----AARLLLLLEAEADYEGFLEGVKA-----ALLLAGLRGLAGAVA 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1462 EWKQKYEETHAELEAS-----------QKESRSLSTELFKIKNAYEESLDHLETLKR----ENKNLQQEISDLTEQIAEG 1526
Cdd:COG1196 528 VLIGVEAAYEAALEAAlaaalqnivveDDEVAAAAIEYLKAAKAGRATFLPLDKIRAraalAAALARGAIGAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1527 GKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLE---LNQVKSEIDRKIAEKDEEIDQLKRNHIRVVES 1603
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEgegGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1604 MQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVER 1683
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 82524274 1684 RANLLQAEIEEL-----RAtleqtersrkiaEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEA 1755
Cdd:COG1196 768 ELERLEREIEALgpvnlLA------------IEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLET 832
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
223-718 |
9.66e-22 |
|
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: 102.90 E-value: 9.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 223 IISANPLLEAFGNAKTVRNDNSSRFGKF--IRIHFGTTG---KLASADIETYLLEKSRVTFQL------KAERSYHIFYQ 291
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 292 IMS--NKKP--------------DLIEMLLITTNPYDYA-FVSQGEITVPSIDDQEELMatdSAIDILGFTSDERVSIYK 354
Cdd:cd14894 329 MVAgvNAFPfmrllakelhldgiDCSALTYLGRSDHKLAgFVSKEDTWKKDVERWQQVI---DGLDELNVSPDEQKTIFK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 355 LTGAVMHYGNMKFKQKQREEQAEPDGT---EVADKAAYLQNLNSADLL-KALCYPRVKVGNEYVTKGQTVQ--QVYNSVG 428
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLeRMLMTKSVSLQSTSETFEVTLEkgQVNHVRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 429 ALAKAVYEKMFLWMVTRINQ--------------QLDTKQPRQYFIGVL---DIAGFEIFDFNSLEQLCINFTNEKLQQF 491
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEatkmsalstdgnkhQMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINYLSEKLYAR 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 492 FNHHMFVLEQEEYKKEGIEWEfidfgmdlAACIELIEKPMGIFSILEEECMFPKATDTSF-----KNKLYEQHLGKSNNF 566
Cdd:cd14894 566 EEQVIAVAYSSRPHLTARDSE--------KDVLFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIYDRNSS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 567 QKPKPAKGKVEAH-----------FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAAAAAEAES 635
Cdd:cd14894 638 RLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQLGWSPN 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 636 GGGGGKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKG 715
Cdd:cd14894 718 TNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNS 797
|
...
gi 82524274 716 FPS 718
Cdd:cd14894 798 SSS 800
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
851-1539 |
1.30e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.71 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 851 ETEKEManmkeefEKAKENLAKAEAKRKELEEKMValmqekndlQLQVQSE----ADSLADAEERCD-QLIKTKIQ-LEA 924
Cdd:COG1196 176 EAERKL-------EATEENLERLEDILGELERQLE---------PLERQAEkaerYRELKEELKELEaELLLLKLReLEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 925 KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKK 1004
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1005 ALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLD 1084
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1085 EKLKKKEFEMSNLQSKIEDEQAlgmQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGAT 1164
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEE---ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1165 SAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEksemkMEIDDLASNMEV 1244
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-----LEAALAAALQNI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1245 ISKSKgnlekmcRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKR 1324
Cdd:COG1196 552 VVEDD-------EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1325 QLEEEIKAKSALAhalqssrhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRL 1404
Cdd:COG1196 625 RTLVAARLEAALR------------RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1405 QDAEEHVEAvnakcasLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKESRSL 1484
Cdd:COG1196 693 LELEEALLA-------EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 82524274 1485 STELFKIKNAYEE-------SLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQ 1539
Cdd:COG1196 766 ERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRE 827
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1207-1835 |
1.09e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.63 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1207 VAELGEQIDNLQR----------VKQKL-EKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQR 1275
Cdd:COG1196 195 LGELERQLEPLERqaekaeryreLKEELkELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1276 LINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYE 1355
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1356 EEQEAKAELQRAMSKANSEVAQWRtkyetdaiqrtEELEEAKKKLAQRLQDAEEhveavnakcasLEKTKQRLQNEVEDL 1435
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAE-----------EELEELAEELLEALRAAAE-----------LAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1436 MIDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTElfkiknayeesldhLETLKRENKNLQQE 1515
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL--------------LAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1516 ISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRiqlelnqvkseIDRKIAEKDEEIDQLKR 1595
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI-----------GVEAAYEAALEAALAAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1596 NHIRVVESMQSTLDAeirsrndAIRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLK 1675
Cdd:COG1196 548 LQNIVVEDDEVAAAA-------IEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1676 EQLAMVERRANLLQAeiEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEA 1755
Cdd:COG1196 621 TLLGRTLVAARLEAA--LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1756 RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVEN 1835
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1008-1808 |
8.44e-20 |
|
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: 97.11 E-value: 8.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1008 EAHQQTLDDLQAEEDKVNTL-TKAKIKLEQQVDDLEGSLEQ---EKKIRMDLERAKRKLEGDLKlaqestMDVENDKQQL 1083
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLR------NQLQNTVHEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1084 DEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQA-----RIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLE 1158
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSilvdfEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEIS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1159 EAGGAT--------SAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSE 1230
Cdd:pfam15921 235 YLKGRIfpvedqleALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1231 MKMEIDDLASNmevISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEkdsLVSQLSR 1310
Cdd:pfam15921 315 YMRQLSDLEST---VSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK---LLADLHK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1311 GKQAFTQQIEELKRQLEEEIKAKSALAHalqssrhdcdllreqyeeeqeakaeLQRAMSKANSEVaqwrtkyetdaiQRT 1390
Cdd:pfam15921 389 REKELSLEKEQNKRLWDRDTGNSITIDH-------------------------LRRELDDRNMEV------------QRL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1391 EELEEAKKKLAQ--------RLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLmidvertNAACAALDKKQRNFDKILAE 1462
Cdd:pfam15921 432 EALLKAMKSECQgqmerqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTVSDLTAS 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1463 WKQK---YEETHAELEASQKESRSLSTELFKIKNAyEESLDHLET------LKRENKN-----LQQEISDLTEQIAEGGK 1528
Cdd:pfam15921 505 LQEKeraIEATNAEITKLRSRVDLKLQELQHLKNE-GDHLRNVQTecealkLQMAEKDkvieiLRQQIENMTQLVGQHGR 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1529 RIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQ-----LELNQVK-----SEIDRKIAEKDEEIDQLkRNHI 1598
Cdd:pfam15921 584 TAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEarvsdLELEKVKlvnagSERLRAVKDIKQERDQL-LNEV 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1599 RVVESMQSTL--DAEIRSRNdaIRLK-KKMEGDLNEMEIQLnhsnRMAAEALRNYRNTQGILKDTQLHlddALRGQEDLK 1675
Cdd:pfam15921 663 KTSRNELNSLseDYEVLKRN--FRNKsEEMETTTNKLKMQL----KSAQSELEQTRNTLKSMEGSDGH---AMKVAMGMQ 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1676 EQLAMVERRANLLQAEIEELratleqtersrkiaEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEA 1755
Cdd:pfam15921 734 KQITAKRGQIDALQSKIQFL--------------EEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQE 799
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 82524274 1756 RNAEEKakkaitdAAMMAEELKKEQDTSAHLERMKKNLEQ-TVK-DLQHRLDEAE 1808
Cdd:pfam15921 800 RRLKEK-------VANMEVALDKASLQFAECQDIIQRQEQeSVRlKLQHTLDVKE 847
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
837-1518 |
6.37e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.44 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 837 MKLYFKIKPLLKSAETEKEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAeercdqlI 916
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA-------A 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 917 KTKIQLEAKIKEVTERAEDEEEINAELTAKKRKL-EDECSELKKDIDDLEltlAKVEKEKHATENKVKnlTEEMAGLDET 995
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEAKKKADAAK---KKAEEKKKADEAKKK--AEEDKKKADE 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 996 IAKLTKEKKALQEAHQqtlddlQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIrmdlERAKRKLEgDLKLAQESTMD 1075
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKK------KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA----EEAKKKAE-EAKKADEAKKK 1478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1076 VENDKQQldEKLKKKEFEmsnlQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQR-SDLSRELEEIS 1154
Cdd:PTZ00121 1479 AEEAKKA--DEAKKKAEE----AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkAEEKKKADELK 1552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1155 ERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLE--KEKSEMK 1232
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelKKAEEEK 1632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1233 MEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKdslvsqlsrgk 1312
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA----------- 1701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1313 qaftQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQyEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEE 1392
Cdd:PTZ00121 1702 ----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1393 L-----EEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKilAEWKQKY 1467
Cdd:PTZ00121 1777 KeavieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEAD--AFEKHKF 1854
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 82524274 1468 EETHAELEASQKESRSlSTELFKIKNAYEESLDHLETLKRENKNLQQEISD 1518
Cdd:PTZ00121 1855 NKNNENGEDGNKEADF-NKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1077-1807 |
1.79e-18 |
|
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: 92.01 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1077 ENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISER 1156
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1157 LEeaggatsAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADsVAELGEQIDNLQRVKQKLEKEKSEMKMEID 1236
Cdd:TIGR04523 112 IK-------NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1237 DLASNMEVISKSKGNLEKMcrtledqVSELKTKEEEQqrliNELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFT 1316
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELL-------LSNLKKKIQKN----KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1317 QQIEELKrqlEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEvaqWRTKYETDAIQRTEELEEA 1396
Cdd:TIGR04523 253 TQLNQLK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD---WNKELKSELKNQEKKLEEI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1397 KKKLAQrlqdAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEA 1476
Cdd:TIGR04523 327 QNQISQ----NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1477 SQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEA 1556
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1557 SLEHEEGKILRIQ---LELNQVKSEIDRKIAEKDEEIDQLKRNhIRVVESMQSTLDAEIRSRNDAIrLKKKMEGDLNEME 1633
Cdd:TIGR04523 483 NLEQKQKELKSKEkelKKLNEEKKELEEKVKDLTKKISSLKEK-IEKLESEKKEKESKISDLEDEL-NKDDFELKKENLE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1634 IQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQEL 1713
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1714 LDASERVQLLHTQNTSLINTK-------KKLETDISQIQGEMEDIVQEARNAEEKA---KKAITDAAMMAEELKKEQDTS 1783
Cdd:TIGR04523 641 NKLKQEVKQIKETIKEIRNKWpeiikkiKESKTKIDDIIELMKDWLKELSLHYKKYitrMIRIKDLPKLEEKYKEIEKEL 720
|
730 740
....*....|....*....|....
gi 82524274 1784 AHLERMKKNLEQTVKDLQHRLDEA 1807
Cdd:TIGR04523 721 KKLDEFSKELENIIKNFNKKFDDA 744
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
850-1462 |
4.06e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 91.67 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 850 AETEKEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKIKEV 929
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 930 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN-------LTEEMAGLDETIAKLTKE 1002
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGgraveevLKASIQGVHGTVAQLGSV 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1003 K----KALQEAHQQTLDDLQAEED--------------------------KVNTLTKAKIKLEQQVDDLEGSLEQEKKIR 1052
Cdd:TIGR02169 534 GeryaTAIEVAAGNRLNNVVVEDDavakeaiellkrrkagratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPKYE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1053 -------------MDLERAKR--------KLEGDL--------------KLAQESTMDVENDKQQLDEKLKKKEFEMSNL 1097
Cdd:TIGR02169 614 pafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGELfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1098 QSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqIEMNKKREAE 1177
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV-------KSELKELEAR 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1178 FQKMRRDLEEATLQHEATAATLRkkhadsvaelGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCR 1257
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLS----------HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1258 TLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEeikaksala 1337
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE--------- 907
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1338 halqssrhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQ-----WRTKYETDAIQRTEELEEAKKKLAQRLQD------ 1406
Cdd:TIGR02169 908 ------------LEAQIEKKRKRLSELKAKLEALEEELSEiedpkGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnm 975
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 82524274 1407 -AEEHVEAVNAKCASLEKTKQRLQNEVEDL-----MIDVERTNAACAALDKKQRNFDKILAE 1462
Cdd:TIGR02169 976 lAIQEYEEVLKRLDELKEKRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1629-1930 |
9.31e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.00 E-value: 9.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1629 LNEMEIQLNHSNRMAAEALRnYRNTQGILKDTQLHLddALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKI 1708
Cdd:COG1196 195 LGELERQLEPLERQAEKAER-YRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1709 AEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1788
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1789 MKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEgEVENEQKRNVEAIKGLRKHERRVKELTYQTEEDRKNV 1868
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 82524274 1869 LRLQDLVDKLQSKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVK 1930
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1174-1918 |
1.12e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.20 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1174 REAEFQKMRRDLEEATLQHEATAATLRKKHADSVAElgeqidnlQRVKQKLEKEKSEMKMEIDDLASNMEViskskGNLE 1253
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAE--------EARKAEEAKKKAEDARKAEEARKAEDA-----RKAE 1143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1254 KMCRTLEDQVSELKTKEEEQQRLINELTAQRGRlqteSGEYSRQLDEkdslVSQLSRGKQAFTQQIEELKRQLEEEIKAK 1333
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDARKAEEARKAEDAK----KAEAARKAEE----VRKAEELRKAEDARKAEAARKAEEERKAE 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1334 SALAHALQSSRHDCDLLREQYEEEQEAK-AELQRAmskaNSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVE 1412
Cdd:PTZ00121 1216 EARKAEDAKKAEAVKKAEEAKKDAEEAKkAEEERN----NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKK 1291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1413 AVNAKCASLEKTKQRLQNEVEDLMIDVErtnaacaaLDKKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELfkik 1492
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADE--------AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA---- 1359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1493 NAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKilriqlel 1572
Cdd:PTZ00121 1360 EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-------- 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1573 nqvKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRN 1652
Cdd:PTZ00121 1432 ---KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1653 TQgilKDTQLHLDDALRGQEDLKEqlAMVERRANLLQAEIEELRA-TLEQTERSRKIAEQELLDASERVQllHTQNTSLI 1731
Cdd:PTZ00121 1509 KK---KADEAKKAEEAKKADEAKK--AEEAKKADEAKKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAE--EDKNMALR 1581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1732 NTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAiTDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQH-RLDEAEQL 1810
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElKKAEEENK 1660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1811 ALKGGKKQIQKLEARVRELEGEVENEQKRNVEAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAE 1890
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
730 740 750
....*....|....*....|....*....|.
gi 82524274 1891 EAE---EQSNVNLAKFRKIQHELEEAEERAD 1918
Cdd:PTZ00121 1741 EDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
946-1639 |
1.33e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 89.31 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 946 KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVN 1025
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1026 TLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKKEFEMSNLQSKIEDEQ 1105
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1106 ALGMQLQKKIKELQarieeleeeieaerasrakaekqrsdlsreleeiserleeaggatsAQIEMNKKREAEFQkmrrDL 1185
Cdd:TIGR04523 194 NKLLKLELLLSNLK----------------------------------------------KKIQKNKSLESQIS----EL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1186 EEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISkskgNLEKMCRTLEDQVSE 1265
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK----ELEKQLNQLKSEISD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1266 LKtkEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLsrgkqafTQQIEELKRQLEEeikaksalahalqsSRH 1345
Cdd:TIGR04523 300 LN--NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL-------NEQISQLKKELTN--------------SES 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1346 DCDLLREQYEEEQEAKAELQRAMSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTK 1425
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEI---------------KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1426 QRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETL 1505
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1506 KRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHE--EGKILRIQLELNQVKSEID--- 1580
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKslk 581
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 82524274 1581 RKIAEKDEEIDQLKRNhIRVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHS 1639
Cdd:TIGR04523 582 KKQEEKQELIDQKEKE-KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
899-1541 |
2.04e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 88.97 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 899 QSEADSLADAEERCDQLIKTKIQLEAkikevTERAEDE-EEINAELTAKKRKLEDECSElKKDIDDLeltLAKVEKEKHA 977
Cdd:PRK03918 134 QGEIDAILESDESREKVVRQILGLDD-----YENAYKNlGEVIKEIKRRIERLEKFIKR-TENIEEL---IKEKEKELEE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 978 TENKVKNLTEEMAGLDETIAKLTKEKKALqEAHQQTLDDLQAEEDKVNtltKAKIKLEQQVDDLEGSLEQEKKIRMDLER 1057
Cdd:PRK03918 205 VLREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLE---GSKRKLEEKIRELEERIEELKKEIEELEE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1058 AKRKLEgDLKLAQESTMDVENDKQQLDEKLKKKEFEMSNLQSKIEDeqalgmqLQKKIKELqarieeleeeieaerasra 1137
Cdd:PRK03918 281 KVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING-------IEERIKEL------------------- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1138 kaekqrSDLSRELEEISERLEEAggatsaqiemnKKREAEFQKMRRDLEEAtLQHEATAATLRKKHAD-SVAELGEQIDN 1216
Cdd:PRK03918 334 ------EEKEERLEELKKKLKEL-----------EKRLEELEERHELYEEA-KAKKEELERLKKRLTGlTPEKLEKELEE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1217 LQRVKQKLEKE-------KSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEdqvselktkEEEQQRLINELTAQRGRLQT 1289
Cdd:PRK03918 396 LEKAKEEIEEEiskitarIGELKKEIKELKKAIEELKKAKGKCPVCGRELT---------EEHRKELLEEYTAELKRIEK 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1290 ESGEYSRQLD----EKDSLVSQLSRGKQAFTQ-----QIEELKRQLE----EEIKAKSALAHALQSS----RHDCDLLRE 1352
Cdd:PRK03918 467 ELKEIEEKERklrkELRELEKVLKKESELIKLkelaeQLKELEEKLKkynlEELEKKAEEYEKLKEKliklKGEIKSLKK 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1353 QYEEEQE---AKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLqdaEEHVEAVNAkcaslEKTKQRLQ 1429
Cdd:PRK03918 547 ELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFY---NEYLELKDA-----EKELEREE 618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1430 NEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKY-EETHAELEasqKESRSLSTELFKIKNAYEESLDHLETLKRE 1508
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELR---EEYLELSRELAGLRAELEELEKRREEIKKT 695
|
650 660 670
....*....|....*....|....*....|...
gi 82524274 1509 nknlqqeISDLTEQIAEGGKRIHELEKIKKQIE 1541
Cdd:PRK03918 696 -------LEKLKEELEEREKAKKELEKLEKALE 721
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
846-1584 |
5.21e-17 |
|
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: 87.72 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 846 LLKSAETEKEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAK 925
Cdd:TIGR00618 169 LMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 926 IKEVTERAEDEEEInAELTAKKRKLEDECSELKKDIDDLELT--LAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEK 1003
Cdd:TIGR00618 249 REAQEEQLKKQQLL-KQLRARIEELRAQEAVLEETQERINRArkAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1004 KALQEAHQQTLdDLQAEEDKVNTLTKAKIKLEQQVddlegslEQEKKIRMDLERAKRKLEGDLKLAQestmDVENDKQQL 1083
Cdd:TIGR00618 328 MKRAAHVKQQS-SIEEQRRLLQTLHSQEIHIRDAH-------EVATSIREISCQQHTLTQHIHTLQQ----QKTTLTQKL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1084 dEKLKKKEFEMSNLQSKIEDEQALGMQLQ------KKIKELQARIEELEEEIEAERASRAKAE-----------KQRSDL 1146
Cdd:TIGR00618 396 -QSLCKELDILQREQATIDTRTSAFRDLQgqlahaKKQQELQQRYAELCAAAITCTAQCEKLEkihlqesaqslKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1147 SRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHA--DSVAELGEQIDN----LQRV 1220
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgeQTYAQLETSEEDvyhqLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1221 KQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDE 1300
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1301 kdslvsqlsrgkqaftQQIEElKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRT 1380
Cdd:TIGR00618 635 ----------------QQCSQ-ELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1381 KYEtDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDlmidvERTNAACAALDKKQRNFDKIL 1460
Cdd:TIGR00618 698 MLA-QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH-----QARTVLKARTEAHFNNNEEVT 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1461 AEWK--QKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKR-ENKNLQQEISDLTEQIAEGGKRIHELEKIK 1537
Cdd:TIGR00618 772 AALQtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 82524274 1538 KQIEQEKSELQAALEEaEASLEHEEGKILRIQLELNQVKSEIDRKIA 1584
Cdd:TIGR00618 852 LKYEECSKQLAQLTQE-QAKIIQLSDKLNGINQIKIQFDGDALIKFL 897
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1090-1845 |
7.60e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.50 E-value: 7.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1090 KEFEMSNLQSKIEDEQAlgMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIE 1169
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEAT--EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1170 MNKKREAEFQKMR--RDLEEATLQHEA-TAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEmKMEIDDLASNMEVIS 1246
Cdd:PTZ00121 1155 EIARKAEDARKAEeaRKAEDAKKAEAArKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1247 KSKGNLEKMCRTLEDQVSELKTKEEEQQrlINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQL 1326
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEAR--MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1327 EEEIKAKSALAHAlQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELE--EAKKKLAQRL 1404
Cdd:PTZ00121 1312 EEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKkaDAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1405 QDAEEHVEAV--NAKCASLEKTKQRLQNEVEDLMIDVERTNAACAAldKKQRNFDKILAEWKQKYEETHAELEASQKESR 1482
Cdd:PTZ00121 1391 KKADEAKKKAeeDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1483 SLSTELFKIKNAYEESLDHLETLKRENKNLQQEIsdltEQIAEGGKRIHEL---EKIKKQIEQEKSELQAALEEAEASLE 1559
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA----KKAAEAKKKADEAkkaEEAKKADEAKKAEEAKKADEAKKAEE 1544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1560 HEEGKILRIQLELNqvKSEIDRKIAEKDEEiDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKMEGDlnemEIQLNHS 1639
Cdd:PTZ00121 1545 KKKADELKKAEELK--KAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE----EAKKAEE 1617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1640 NRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQT----ERSRKIAEQELLD 1715
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaeEDEKKAAEALKKE 1697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1716 ASErvqllhtqntslintKKKLEtdisqiqgEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQ 1795
Cdd:PTZ00121 1698 AEE---------------AKKAE--------ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 82524274 1796 TVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNVEAIK 1845
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
970-1870 |
1.67e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 86.18 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 970 KVEKEKHATENKVKNLTEEMAGLDETIakltKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEK 1049
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKR----KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1050 KIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKkefEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEI 1129
Cdd:pfam02463 219 LELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ---EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1130 EAERASRAKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAE 1209
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKA----EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1210 LGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQT 1289
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1290 ESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMS 1369
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1370 KANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEhVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAAL 1449
Cdd:pfam02463 532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT-ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1450 DKKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDH-----LETLKRENKNLQQEISDLTEQIA 1524
Cdd:pfam02463 611 ATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSevkasLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1525 EGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNhirvvesm 1604
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEK-------- 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1605 qstLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERR 1684
Cdd:pfam02463 763 ---EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1685 ANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETdisqIQGEMEDIVQEARNAEEKAKK 1764
Cdd:pfam02463 840 LELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEK----EKEEKKELEEESQKLNLLEEK 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1765 AITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNVEAI 1844
Cdd:pfam02463 916 ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDEL 995
|
890 900
....*....|....*....|....*.
gi 82524274 1845 KGLRKHERRVKELTYQTEEDRKNVLR 1870
Cdd:pfam02463 996 EKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1140-1890 |
5.44e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.81 E-value: 5.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1140 EKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMR--RDLEEATLQHEA-TAATLRKKHADSVAELGEQIDN 1216
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEdaRKAEEARKAEDArKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1217 LQRVKqklEKEKSEMKMEIDDLASNMEVIskskgnlekmcRTLEDQVSELKTKEEEQQRLINELTAQRGRlQTESGEYSR 1296
Cdd:PTZ00121 1163 ARKAE---EARKAEDAKKAEAARKAEEVR-----------KAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAE 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1297 QLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVA 1376
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA 1307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1377 QWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAAcaaldKKQRNF 1456
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-----KKKADA 1382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1457 DKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKI 1536
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEA 1462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1537 KKQIEqEKSELQAALEEAEASLEHEEgkiLRIQLELNQVKSEIDRKIAEKDEEIDQLKR-NHIRVVESMQSTLDAEIRSR 1615
Cdd:PTZ00121 1463 KKKAE-EAKKADEAKKKAEEAKKADE---AKKKAEEAKKKADEAKKAAEAKKKADEAKKaEEAKKADEAKKAEEAKKADE 1538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1616 NDAIRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTqgilkdtqlhlDDALRGQEDLKEQLAMVERRANLLQAEIEEL 1695
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK-----------NMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1696 RATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLEtDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEE 1775
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE-ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1776 LKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLalkggKKQIQKLEARVRELEGEVEnEQKRNVEAIKGLRKHERRVK 1855
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL-----KKAEEENKIKAEEAKKEAE-EDKKKAEEAKKDEEEKKKIA 1760
|
730 740 750
....*....|....*....|....*....|....*
gi 82524274 1856 ELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAE 1890
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
911-1593 |
1.25e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 83.09 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 911 RCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAT----ENKVKNLT 986
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERkqvlEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 987 EEMAGLDETIAKLTKEKKALQEAH--QQTLDDLQAEEDKVNTLTKA------KIKLEQQVDDLEGSLEQEKKIRMDLERA 1058
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAVleetqeRINRARKAAPLAAHIKAVTQIEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1059 KRKLEGDLKLAQESTMDVENDKQQLDEKLKKKEFEMSNLQSKIEDEQAlgMQLQKKIKELQARIEELEEEIEAERASRAK 1138
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA--HEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1139 AEKQRSDLSRELEEISERLEEAGGATSAQIEMNK-----KREAEFQKMRRDLEEATLQHEATAATLRKKHADSVA----E 1209
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGqlahaKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAqslkE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1210 LGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSK----------GNLEKMCRTLEDQVSELKTKEEEQQRLINE 1279
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCihpnparqdiDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1280 LTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQA---FTQQIEELKRQLEEEIKAKSALAhalqssrhdcDLLREQYEE 1356
Cdd:TIGR00618 551 LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDipnLQNITVRLQDLTEKLSEAEDMLA----------CEQHALLRK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1357 EQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLm 1436
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML- 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1437 idvERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEA-------SQKESRSLS-TELFKIKNAYEESLDHLETLKRE 1508
Cdd:TIGR00618 700 ---AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAredalnqSLKELMHQArTVLKARTEAHFNNNEEVTAALQT 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1509 NKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDE 1588
Cdd:TIGR00618 777 GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEE 856
|
....*
gi 82524274 1589 EIDQL 1593
Cdd:TIGR00618 857 CSKQL 861
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
847-1732 |
2.41e-15 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 82.53 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 847 LKSAETEKEmanmkeefekakenlakaeakRKELEEKMvalmqekNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKI 926
Cdd:pfam01576 419 ARLSESERQ---------------------RAELAEKL-------SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 927 KEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKAL 1006
Cdd:pfam01576 471 QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1007 QEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLegDLKLAQEstmdvendkqqldek 1086
Cdd:pfam01576 551 QRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKF--DQMLAEE--------------- 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1087 lkkkefemSNLQSKIEDEQalgmqlqkkikelqarieeleeeieaeraSRAKAEkqrsdlSREleeiserleeaggatsa 1166
Cdd:pfam01576 614 --------KAISARYAEER-----------------------------DRAEAE------ARE----------------- 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1167 qiemnkkREAEFQKMRRDLEEAtlqheataatlrkkhadsvaelgeqidnlQRVKQKLEKEKSEMKMEIDDLASNMEVIS 1246
Cdd:pfam01576 634 -------KETRALSLARALEEA-----------------------------LEAKEELERTNKQLRAEMEDLVSSKDDVG 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1247 KSKGNLEKMCRTLEDQVSELKTKEEEqqrLINELTAqrgrlqTESGEYSRQLDEKdSLVSQLSRGKQAFTQQIEELKRQL 1326
Cdd:pfam01576 678 KNVHELERSKRALEQQVEEMKTQLEE---LEDELQA------TEDAKLRLEVNMQ-ALKAQFERDLQARDEQGEEKRRQL 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1327 EEEIKAKSAlahalqssrhdcdllreqyEEEQEAKaelQRAMSKAnsevaqwrtkyetdaiqrteeleeAKKKLAQRLQD 1406
Cdd:pfam01576 748 VKQVRELEA-------------------ELEDERK---QRAQAVA------------------------AKKKLELDLKE 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1407 AEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAAcaaldkkqrnFDKILAEWKQkyeethaeleaSQKESRSLST 1486
Cdd:pfam01576 782 LEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARAS----------RDEILAQSKE-----------SEKKLKNLEA 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1487 ELFKIKnayeeslDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKIL 1566
Cdd:pfam01576 841 ELLQLQ-------EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLR 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1567 RIQLELNQVKSEI--DRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAirLKKKMEGDLNEMEIQLNHSNRMAA 1644
Cdd:pfam01576 914 KSTLQVEQLTTELaaERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKS--SIAALEAKIAQLEEQLEQESRERQ 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1645 EALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLH 1724
Cdd:pfam01576 992 AANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMN 1071
|
....*...
gi 82524274 1725 TQNTSLIN 1732
Cdd:pfam01576 1072 REVSTLKS 1079
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
923-1792 |
2.56e-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: 82.33 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 923 EAKIKEVTERAEDEEEINAEL-TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHatenkvknlteemagLDETIAKLTK 1001
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL---------------NEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1002 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDKQ 1081
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1082 QLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEag 1161
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE-- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1162 gatsaqiemnKKREAEFQKMRRDLEEATLQHEATAATLRKKhadsvaELGEQIDNLQRvkqKLEKEKSEMKMEIDDLASN 1241
Cdd:pfam02463 403 ----------EEKEAQLLLELARQLEDLLKEEKKEELEILE------EEEESIELKQG---KLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1242 MEVISKSKGNLEkmcrtledqvSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEE 1321
Cdd:pfam02463 464 ELELKKSEDLLK----------ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1322 LKRQLEEEIKAKSALAHALQSSRHD-CDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKL 1400
Cdd:pfam02463 534 LGVAVENYKVAISTAVIVEVSATADeVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATL 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1401 AQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERT--NAACAALDKKQRNFDKILAEWKQKYEETHAELEASQ 1478
Cdd:pfam02463 614 EADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEegLAEKSEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1479 KESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASL 1558
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1559 EHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNH--IRVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQL 1636
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEeaELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1637 NHSNRMAAEAlrnyRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANllQAEIEELRATLEQTERSRKIAEQELLDA 1716
Cdd:pfam02463 854 EELERLEEEI----TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK--KELEEESQKLNLLEEKENEIEERIKEEA 927
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 1717 SERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKN 1792
Cdd:pfam02463 928 EILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1388-1928 |
6.30e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.88 E-value: 6.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1388 QRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKqrlqNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKY 1467
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1468 EETHaELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKqieqEKSEL 1547
Cdd:PRK03918 276 EELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK----KLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1548 QAALEEAEASLEHEEgKILRIQLELNQVKSEI-DRKIAEKDEEIDQLKR------NHIRVVESMQSTLDAEIRSRNDAIR 1620
Cdd:PRK03918 351 EKRLEELEERHELYE-EAKAKKEELERLKKRLtGLTPEKLEKELEELEKakeeieEEISKITARIGELKKEIKELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1621 LKKKMEGDLNEMEIQLNHSNRmaAEALRNYRntqgilkdtqlhlddalRGQEDLKEQLAMVERRANLLQAEIEELRATLE 1700
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHR--KELLEEYT-----------------AELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1701 qtERSRKIAEQELLDaservqllhtqntSLINTKKKLEtdiSQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQ 1780
Cdd:PRK03918 491 --KESELIKLKELAE-------------QLKELEEKLK---KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1781 DtsahLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEgEVENEQKRNVEAIKGLRKHERRVKELTYQ 1860
Cdd:PRK03918 553 E----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKELEREEKELKKLEEE 627
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 82524274 1861 TEEDRKNVLRLQDLVDKLQSKVKAYKRQ--AEEAEEQSNVNLAKFRKI---QHELEEAEERADIAESQVNKLR 1928
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKysEEEYEELREEYLELSRELaglRAELEELEKRREEIKKTLEKLK 700
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
922-1435 |
7.27e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.47 E-value: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 922 LEAKIKEVTERAE--DEEEINAELT--------AKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAG 991
Cdd:PRK02224 211 LESELAELDEEIEryEEQREQARETrdeadevlEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 992 LDETIAKLTKEKkALQEAHQQTLDDLQAEedkvntltkakikLEQQVDDLEGSLEQEkkiRMDLERAKRKLEGdlklAQE 1071
Cdd:PRK02224 291 LEEERDDLLAEA-GLDDADAEAVEARREE-------------LEDRDEELRDRLEEC---RVAAQAHNEEAES----LRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1072 STMDVENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELqarieeleeeieaerasrakaEKQRSDLSRELE 1151
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL---------------------RERFGDAPVDLG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1152 EISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEA-TLQHEATAATLRKK-----HADSVAELGEQIDNLQRVKQKLE 1225
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLRTARERVEEAeALLEAGKCPECGQPvegspHVETIEEDRERVEELEAELEDLE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1226 KEKSEMKMEIDDLASNMEVISKSKGNLEKMcRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLV 1305
Cdd:PRK02224 489 EEVEEVEERLERAEDLVEAEDRIERLEERR-EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1306 SQLSRGKQAFTQQIEELKRQLEEEIKAKSALAhALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETD 1385
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEA 646
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 82524274 1386 AIqrtEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDL 1435
Cdd:PRK02224 647 RI---EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL 693
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
850-1590 |
2.21e-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: 79.25 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 850 AETEKEMANMKEEfekakenLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKIKEV 929
Cdd:pfam02463 275 KEEEKEKKLQEEE-------LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 930 TERAEDEEEINAELTAKKRKLEdecsELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEA 1009
Cdd:pfam02463 348 EIKREAEEEEEEELEKLQEKLE----QLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1010 HQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKlegdlklaqeSTMDVENDKQQLDEKLKK 1089
Cdd:pfam02463 424 EKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK----------ETQLVKLQEQLELLLSRQ 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1090 KEFEMSNLQSKIEDEQA---LGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSA 1166
Cdd:pfam02463 494 KLEERSQKESKARSGLKvllALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTEL 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1167 QIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVIS 1246
Cdd:pfam02463 574 PLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVS 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1247 KSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQ-----RGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEE 1321
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAkeeilRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1322 LKRQLEEEIKAKSALAHALQSSRHDCDLLREQY--EEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKK 1399
Cdd:pfam02463 734 INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKseLSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEE 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1400 LAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTN----AACAALDKKQRNFDKILAEWKQKYEETHAELE 1475
Cdd:pfam02463 814 AELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELErleeEITKEELLQELLLKEEELEEQKLKDELESKEE 893
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1476 ASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAE 1555
Cdd:pfam02463 894 KEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG 973
|
730 740 750
....*....|....*....|....*....|....*
gi 82524274 1556 ASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEI 1590
Cdd:pfam02463 974 KVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1389-1925 |
2.50e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.19 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1389 RTEELEEakKKLAQRLQDAEEHVEAVNAKCASLEKTKQRlqneVEDLmidvERTNAACAALDKKQRNFDKilaewkQKYE 1468
Cdd:COG4913 214 REYMLEE--PDTFEAADALVEHFDDLERAHEALEDAREQ----IELL----EPIRELAERYAAARERLAE------LEYL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1469 ETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAE-GGKR-------IHELEKIKKQI 1540
Cdd:COG4913 278 RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRleqlereIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1541 EQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNH-------------IRVVESMQST 1607
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALrdlrrelreleaeIASLERRKSN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1608 LDAEIRSRNDAIR--LKKKME-----GDLneMEIQLNHSN-RMAAE-ALRNYRNTqgILKDTQlHLDDALR--GQEDLKE 1676
Cdd:COG4913 438 IPARLLALRDALAeaLGLDEAelpfvGEL--IEVRPEEERwRGAIErVLGGFALT--LLVPPE-HYAAALRwvNRLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1677 QLamverranllqaeieelratleQTERSRKIAEQELLDASERVQLLHtqntslintkkKLETDISQIQGEMEDIVQE-- 1754
Cdd:COG4913 513 RL----------------------VYERVRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLEAELGRrf 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1755 ----ARNAEE--KAKKAITDAAMMaeelkkeqdtsahlermKKNLEQTVKDLQHRLDE--------AEQLALKggKKQIQ 1820
Cdd:COG4913 560 dyvcVDSPEElrRHPRAITRAGQV-----------------KGNGTRHEKDDRRRIRSryvlgfdnRAKLAAL--EAELA 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1821 KLEARVRELEGEVE---------NEQKRNVEAIKGLRKHERRVKELTY---QTEEDRKNVLRLQDLVDKLQSKVKAYKRQ 1888
Cdd:COG4913 621 ELEEELAEAEERLEaleaeldalQERREALQRLAEYSWDEIDVASAEReiaELEAELERLDASSDDLAALEEQLEELEAE 700
|
570 580 590
....*....|....*....|....*....|....*..
gi 82524274 1889 AEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVN 1925
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1024-1632 |
2.64e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.93 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1024 VNTLTKAKIKLEQQVDDlegSLEQEKKIRMDLERAkrkleGDLKLAQEstmDVENDKQQLdeklkkkefeMSNLQSKIED 1103
Cdd:PRK02224 140 VNKLINATPSDRQDMID---DLLQLGKLEEYRERA-----SDARLGVE---RVLSDQRGS----------LDQLKAQIEE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1104 EQALGmqLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAgGATSAQIEMNKKREAEFQKMRR 1183
Cdd:PRK02224 199 KEEKD--LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL-ETLEAEIEDLRETIAETERERE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1184 DLEEATLQHEATAATLRKKHADSVAELG---EQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLE 1260
Cdd:PRK02224 276 ELAEEVRDLRERLEELEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1261 DQVSELKTKEEEqqrlineltaqrgrLQTESGEYSRQLDEKDSlvsqlsrgkqaftqQIEELKRQLEEEIKAKSALAHAL 1340
Cdd:PRK02224 356 ERAEELREEAAE--------------LESELEEAREAVEDRRE--------------EIEELEEEIEELRERFGDAPVDL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1341 QSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYE-------------TDAIQRTEELEEAKKKLAQRLQDA 1407
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgqpvegSPHVETIEEDRERVEELEAELEDL 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1408 EEHVEAVNAKCASLEKTK------QRLQNEVEDL--MID-----VERTNAACAALDKKQRNFDKILAEWKQKYEETHAEL 1474
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVeaedriERLEERREDLeeLIAerretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1475 EASQKESRSLSTELFKIKNAYeESLDHLETLKRENKNLQQEISDLTEQIAEggkrIHELEKIKKQIEQEKSELQAALEEA 1554
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREA----LAELNDERRERLAEKRERKRELEAE 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1555 --EASLEHEEGKILRIQLELNQVKSEIDRKIAEKDE----------EIDQLKR-------------------NHIRVVES 1603
Cdd:PRK02224 643 fdEARIEEAREDKERAEEYLEQVEEKLDELREERDDlqaeigavenELEELEElrerrealenrvealealyDEAEELES 722
|
650 660
....*....|....*....|....*....
gi 82524274 1604 MQSTLDAEIRSRNDAirlkkKMEGDLNEM 1632
Cdd:PRK02224 723 MYGDLRAELRQRNVE-----TLERMLNET 746
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1207-1810 |
5.26e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.77 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1207 VAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKmcrtLEDQVSELKTKEEEQQRLINELTAQRGR 1286
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED----LRETIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1287 LQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQR 1366
Cdd:PRK02224 291 LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1367 AMSKANSEVAQWRTkyetdaiqRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVErtnaac 1446
Cdd:PRK02224 371 ELEEAREAVEDRRE--------EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR------ 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1447 aALDKKQRNFDKILAEWK-----QKYEET-HAE-LEASQKESRSLSTELFKIK---NAYEESLDHLETLK---RENKNLQ 1513
Cdd:PRK02224 437 -TARERVEEAEALLEAGKcpecgQPVEGSpHVEtIEEDRERVEELEAELEDLEeevEEVEERLERAEDLVeaeDRIERLE 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1514 QEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELnqvkSEIDRKIAEKDEEIDQL 1593
Cdd:PRK02224 516 ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV----AELNSKLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1594 KRnhirvVESMQSTLdAEIRSRNDAIRLKKKmegDLNEMEiqlnhsnrmaaealrnyrntqgilkdtqlhlddalrgqED 1673
Cdd:PRK02224 592 ER-----IRTLLAAI-ADAEDEIERLREKRE---ALAELN--------------------------------------DE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1674 LKEQLAMVERRANLLQAEIEELRATLEQTERSRkiAEQELLDASERVQLLHTQntslintKKKLETDISQIQGEMEDIvq 1753
Cdd:PRK02224 625 RRERLAEKRERKRELEAEFDEARIEEAREDKER--AEEYLEQVEEKLDELREE-------RDDLQAEIGAVENELEEL-- 693
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 82524274 1754 earnaeekakkaitdaammaEELKKEQDTsahlermkknLEQTVKDLQHRLDEAEQL 1810
Cdd:PRK02224 694 --------------------EELRERREA----------LENRVEALEALYDEAEEL 720
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
33-77 |
8.18e-14 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 67.07 E-value: 8.18e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 82524274 33 DAKSSVFVVDAKESFVKATVQSREGGKVTAKTEGGTTVTVKDDQV 77
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1302-1912 |
1.48e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.49 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1302 DSLVSQLSRGKQAFtQQIEELKRQLE--EEIKAKSALAHALQSSRHDCDLLRE--QYEEEQEAKAELQRAMSKANSEVAQ 1377
Cdd:COG4913 228 DALVEHFDDLERAH-EALEDAREQIEllEPIRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1378 WRTKYEtDAIQRTEELEEAKKKLAQRLQDAE-EHVEAVNAKCASLEKTKQRLQNEVEDLmidvertNAACAALDkkqRNF 1456
Cdd:COG4913 307 LEAELE-RLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL-------EALLAALG---LPL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1457 DKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEqiaeggkrihELEKI 1536
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA----------RLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1537 KKQIEQE----KSELQAALEEAEASLEHE--EGKILRIqleLNQVKSEI---DRKIAEKDEEIDQLKRNHIRVVESMQST 1607
Cdd:COG4913 446 RDALAEAlgldEAELPFVGELIEVRPEEErwRGAIERV---LGGFALTLlvpPEHYAAALRWVNRLHLRGRLVYERVRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1608 LDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHS--NRMA------AEALRNYRntQGILKDTQLH-------LDDALRGQE 1672
Cdd:COG4913 523 LPDPERPRLDPDSLAGKLDFKPHPFRAWLEAElgRRFDyvcvdsPEELRRHP--RAITRAGQVKgngtrheKDDRRRIRS 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1673 DL------KEQLAMVERRANLLQAEIEELRATLEQTERSRKiAEQELLDASERVQllhTQNTSLINTkKKLETDISQIQG 1746
Cdd:COG4913 601 RYvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLA---EYSWDEIDV-ASAEREIAELEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1747 EMEDIvqearnaeEKAKKAITDAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLEARV 1826
Cdd:COG4913 676 ELERL--------DASSDDLAALEEQLEELEAELEE---LEEELDELKGEIGRLEKELEQAEE--------ELDELQDRL 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1827 RELEGEVENEQKRNVEAIKGLRKHERRVKELTYQTEEDR-KNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNVNLA---K 1902
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIdALRARLNRAEEELERAMRAFNREWPAETADLDADLEslpE 816
|
650
....*....|
gi 82524274 1903 FRKIQHELEE 1912
Cdd:COG4913 817 YLALLDRLEE 826
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
841-1273 |
1.49e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.26 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 841 FKIKPLLKSAETEKEMANMKEEFEKAKENLAKAEAKR---KELEEKMVALMQEKNDLQLQVQSEADSLADAEE----RCD 913
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 914 QLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLE-----LTLAKVEKEKHATENKVKNLTEE 988
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkCPVCGRELTEEHRKELLEEYTAE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 989 MAGLDETIAKLTKEKKALqEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEG----SLEQEKKIRMDLERAKRKLEG 1064
Cdd:PRK03918 461 LKRIEKELKEIEEKERKL-RKELRELEKVLKKESELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1065 DLKLAQ---ESTMDVENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGM-QLQKKIKELQARIEELEEEIEAERASRAKaE 1140
Cdd:PRK03918 540 EIKSLKkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELEPFYNEYLELKDAEKELERE-E 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1141 KQRSDLSRELEEISERLEEaggaTSAQIEMNKKREAEFQKMRRDLEEATLQHEATaaTLRKKHADSVAELGEQIDNLQRV 1220
Cdd:PRK03918 619 KELKKLEEELDKAFEELAE----TEKRLEELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRAELEELEKRREEI 692
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 82524274 1221 KQKLEKEKSEMKmEIDDLASNMEVISKSKGNLEKmcrtLEDQVSELKTKEEEQ 1273
Cdd:PRK03918 693 KKTLEKLKEELE-EREKAKKELEKLEKALERVEE----LREKVKKYKALLKER 740
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1044-1937 |
2.04e-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: 76.24 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1044 SLEQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKKEFEMSNLQSKiEDEQALGMQLQKKIKELqariE 1123
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY-ENELDPLKNRLKEIEHN----L 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1124 ELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREA-EFQKMRRDLEEATLQHEATAATLRKK 1202
Cdd:TIGR00606 262 SKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1203 HADSVAELGE-----QIDNLQRVKQKLEKEKSEMKMEIDDLASNMEV-------ISKSKGNLEKMCRTLEDQVSELKTKE 1270
Cdd:TIGR00606 342 KTELLVEQGRlqlqaDRHQEHIRARDSLIQSLATRLELDGFERGPFSerqiknfHTLVIERQEDEAKTAAQLCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1271 EEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLL 1350
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1351 REQYEeeQEAKAELQRAMSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQDAE-EHVEAVNAKCA------SLEK 1423
Cdd:TIGR00606 502 EVKSL--QNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQIRKIKsRHSDELTSLLGyfpnkkQLED 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1424 TKQRLQNEVEDLMIDVERTNAACAALDKKQ---RNFDKILAEWKQKYEETHAELEASQKESrslsTELFKIKNAYEESLD 1500
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELASLEQNKnhiNNELESKEEQLSSYEDKLFDVCGSQDEE----SDLERLKEEIEKSSK 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1501 HLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQV----- 1575
Cdd:TIGR00606 654 QRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglap 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1576 --KSEIDRKIAEKDEEIDQLK---------RNHIRVVESMQSTLDAEIRSRND-----AIRLKKKMEGDLNEMEIQLNHS 1639
Cdd:TIGR00606 734 grQSIIDLKEKEIPELRNKLQkvnrdiqrlKNDIEEQETLLGTIMPEEESAKVcltdvTIMERFQMELKDVERKIAQQAA 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1640 NRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEEL---RATLEQTERSRKIAEQELLDA 1716
Cdd:TIGR00606 814 KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELkseKLQIGTNLQRRQQFEEQLVEL 893
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1717 SERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEArnaEEKAKKAITDAAMMAEELKkeqdtsahlermkkNLEQT 1796
Cdd:TIGR00606 894 STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK---ETSNKKAQDKVNDIKEKVK--------------NIHGY 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1797 VKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVE----------------NEQKRNVEAIKGLRKHERRVKEL--- 1857
Cdd:TIGR00606 957 MKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEkinedmrlmrqdidtqKIQERWLQDNLTLRKRENELKEVeee 1036
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1858 --TYQTEEDRKNVLRLQDLVDKLQSKVKAYKR-------QAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLR 1928
Cdd:TIGR00606 1037 lkQHLKEMGQMQVLQMKQEHQKLEENIDLIKRnhvlalgRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELV 1116
|
....*....
gi 82524274 1929 VKSREVHTK 1937
Cdd:TIGR00606 1117 NKDLDIYYK 1125
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1076-1928 |
2.07e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 76.16 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1076 VENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEeieaeRASRAKAEKQRSDLSRELEEISE 1155
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEEL-----KLQELKLKEQAKKALEYYQLKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1156 RLEEAGGATSAQIEmnkKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEI 1235
Cdd:pfam02463 219 LELEEEYLLYLDYL---KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1236 DDLASNM-------EVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQL 1308
Cdd:pfam02463 296 EELKSELlklerrkVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1309 SRGKQAFTQQIEELKRQLEEEikaksaLAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQ 1388
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEE------LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1389 RTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTkqrlQNEVEDLMIDVERTNAACAALD--KKQRNFDKILAEWKQK 1466
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ----LELLLSRQKLEERSQKESKARSglKVLLALIKDGVGGRII 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1467 YEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSE 1546
Cdd:pfam02463 526 SAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1547 LQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKME 1626
Cdd:pfam02463 606 AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1627 GDLNEMEIQLNHSNRMAAEALRNyrntqgILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSR 1706
Cdd:pfam02463 686 ESELAKEEILRRQLEIKKKEQRE------KEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKK 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1707 KIAEQELLDASErvQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARnaEEKAKKAITDAAMMAEELKKEQDTSAHL 1786
Cdd:pfam02463 760 EEKEEEKSELSL--KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALE--EELKEEAELLEEEQLLIEQEEKIKEEEL 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1787 ERMKKNLEQTVKDLQHRLDEAEQLalkggKKQIQKLEARVRELEGEVENEQKRNVEAIKGLRKHERRVKELTyQTEEDRK 1866
Cdd:pfam02463 836 EELALELKEEQKLEKLAEEELERL-----EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKEL-EEESQKL 909
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82524274 1867 NVLRLQDLVDKLQSKVKAYKRQAEEA--EEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLR 1928
Cdd:pfam02463 910 NLLEEKENEIEERIKEEAEILLKYEEepEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG 973
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1033-1614 |
2.36e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.72 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1033 KLEQQVDDLEGSLEQEKKIRMDLERAKRKLE--GDLKLAQESTMDVENDKQQLDEklkkkefemsnLQSKIEDEQAlgmq 1110
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEY-----------LRAALRLWFA---- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1111 lQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIE-----MNKKRE------AEFQ 1179
Cdd:COG4913 287 -QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEreierLERELEererrrARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1180 KMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNL------- 1252
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparllal 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1253 -EKMCRTLEDQVSEL---------KTKEEEQQRLIN-ELTAQRGRLQTESGEYSRQLdekdSLVSQLSRGKQAFTQQIEE 1321
Cdd:COG4913 446 rDALAEALGLDEAELpfvgelievRPEEERWRGAIErVLGGFALTLLVPPEHYAAAL----RWVNRLHLRGRLVYERVRT 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1322 LKRQLEEEIKAKSALAHALQSSRHDC-DLLREQYEEEQ-----EAKAELQRA--------MSKANSEVAQ------WRTK 1381
Cdd:COG4913 522 GLPDPERPRLDPDSLAGKLDFKPHPFrAWLEAELGRRFdyvcvDSPEELRRHpraitragQVKGNGTRHEkddrrrIRSR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1382 YET--DAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQN--EVEDLMIDVERTNAACAALDKKQRNFD 1457
Cdd:COG4913 602 YVLgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1458 K---ILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISdlTEQIAEGGKRIHELe 1534
Cdd:COG4913 682 AssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERFAAA- 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1535 KIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQV----KSEIDRKIAE-------------------KDEEID 1591
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwpaeTADLDADLESlpeylalldrleedglpeyEERFKE 838
|
650 660
....*....|....*....|...
gi 82524274 1592 QLKRNHIRVVESMQSTLDAEIRS 1614
Cdd:COG4913 839 LLNENSIEFVADLLSKLRRAIRE 861
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1262-1928 |
3.99e-13 |
|
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: 75.21 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1262 QVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQ-----------------LSRGKQAFTQQIEELKR 1324
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQlqaetelcaeaeemrarLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1325 QLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTeELEEAKKKLAQRL 1404
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNS-KLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1405 QDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKESRSL 1484
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1485 STELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGK 1564
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1565 ILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHSNRMAA 1644
Cdd:pfam01576 322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1645 EALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMverranlLQAEIEELRATLEQTE----RSRK---IAEQELLDAS 1717
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK-------LQSELESVSSLLNEAEgkniKLSKdvsSLESQLQDTQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1718 ERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTV 1797
Cdd:pfam01576 475 ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1798 KDLQHRLDEAEQlalkggkkQIQKLEARVRELEGEVEN---EQKRNVEAIKGLRKHERRVKELtyqTEEDRKNVLRLQDL 1874
Cdd:pfam01576 555 EALTQQLEEKAA--------AYDKLEKTKNRLQQELDDllvDLDHQRQLVSNLEKKQKKFDQM---LAEEKAISARYAEE 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 82524274 1875 VDKlqskvkaykrqaeeAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLR 1928
Cdd:pfam01576 624 RDR--------------AEAEAREKETRALSLARALEEALEAKEELERTNKQLR 663
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
851-1453 |
7.49e-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: 74.38 E-value: 7.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 851 ETEKEMANMKEEFEKAKENLakaEAKRKELEEKMVALMQEKNDLQLQVQSEAD----------SLADAEERCDQLIKTKI 920
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQL---EALKSESQNKIELLLQQHQDRIEQLISEHEveitgltekaSSARSQANSIQSQLEII 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 921 QLEAK------IKEVTERAEDEEEINAELTAKKRKLEDECSELKKD--IDDLELTLAKVEKEKHATENkvKNLTEEMAGL 992
Cdd:pfam15921 305 QEQARnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 993 DETIAKLTKEKKALQEAHQQTLDdlqaeEDKVNTLTkakikleqqVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQES 1072
Cdd:pfam15921 383 LADLHKREKELSLEKEQNKRLWD-----RDTGNSIT---------IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMER 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1073 TMDVENDKQQLDEKLkkkefemSNLQSKIEDEQALgmqLQKKIKELqarieeleeeiEAERASRAKAEKQRSDLSRELEE 1152
Cdd:pfam15921 449 QMAAIQGKNESLEKV-------SSLTAQLESTKEM---LRKVVEEL-----------TAKKMTLESSERTVSDLTASLQE 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1153 ISERLEeaggATSAQIEMNKKRE----AEFQKMRRDLEE-ATLQHEATAATLRKKHADSVAE-LGEQIDNLQ-------R 1219
Cdd:pfam15921 508 KERAIE----ATNAEITKLRSRVdlklQELQHLKNEGDHlRNVQTECEALKLQMAEKDKVIEiLRQQIENMTqlvgqhgR 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1220 VKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKE-------EEQQRLINELTAQRGRLQTESG 1292
Cdd:pfam15921 584 TAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvklvnagSERLRAVKDIKQERDQLLNEVK 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1293 EYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSAlahALQSSRHDCDLLREQYEEEQEAKAELQRAMSKAN 1372
Cdd:pfam15921 664 TSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQS---ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKR 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1373 SEVAQWRTKYE------TDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTN--- 1443
Cdd:pfam15921 741 GQIDALQSKIQfleeamTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASlqf 820
|
650
....*....|
gi 82524274 1444 AACAALDKKQ 1453
Cdd:pfam15921 821 AECQDIIQRQ 830
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1296-1942 |
8.78e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.95 E-value: 8.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1296 RQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEE---EIKAKSALAHALQSSRHDC----DLLREQYEEEQEAKAELQRAM 1368
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAeryqALLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1369 SKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCaslEKTKQRLQNEVEDLMIDVERTNAACAA 1448
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG---EEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1449 LDKKQRNFDKILAEWKQKYEETHAELEAS-------QKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTE 1521
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELereieeeRKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1522 QIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILriqlELNQVKSEIDRKIAEKDEEIDQLKrnhirvv 1601
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN----ELEEEKEDKALEIKKQEWKLEQLA------- 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1602 eSMQSTLDAEIRSRNDAIRlkkKMEGDLNEMEIQLNhsnrmAAEA-LRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAM 1680
Cdd:TIGR02169 462 -ADLSKYEQELYDLKEEYD---RVEKELSKLQRELA-----EAEAqARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1681 VERR---------ANLLQA---EIEELRATLEQTERSRKIAEQELL------DASERVQLLHTQNT-----SLINTKKKL 1737
Cdd:TIGR02169 533 VGERyataievaaGNRLNNvvvEDDAVAKEAIELLKRRKAGRATFLplnkmrDERRDLSILSEDGVigfavDLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1738 ETDISQIQGE---MEDIvQEARN-----------------------AEEKAKKAITDAAMMAEELKKEQDTSAHLERMKK 1791
Cdd:TIGR02169 613 EPAFKYVFGDtlvVEDI-EAARRlmgkyrmvtlegelfeksgamtgGSRAPRGGILFSRSEPAELQRLRERLEGLKRELS 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1792 NLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELEGEVENEQKRNVEAIKGLRKHERRV-----------KELTYQ 1860
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQ-ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIenvkselkeleARIEEL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1861 TEEDRKNVLRLQDLVDKL-QSKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKII 1939
Cdd:TIGR02169 771 EEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
...
gi 82524274 1940 SEE 1942
Cdd:TIGR02169 851 SIE 853
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1317-1930 |
1.16e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.41 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1317 QQIEELKRQLEEEIKAKSALAHALQssrhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQwrTKYETdAIQRTEELEEA 1396
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRE--------LAERYAAARERLAELEYLRAALRLWFAQ--RRLEL-LEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1397 KKKLAQRLQDAEEHVEAVNAKCASLEKtkQRLQN---EVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAE 1473
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEA--QIRGNggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1474 LEASQKESRslstelfkiknayeeslDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKS----ELQA 1549
Cdd:COG4913 382 FAALRAEAA-----------------ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1550 ALEEAEASLEHEEGKiLRIQLELNQVKSEiDRK-----------------IAEKDEE-----IDQLKRNHIRVVESMQST 1607
Cdd:COG4913 445 LRDALAEALGLDEAE-LPFVGELIEVRPE-EERwrgaiervlggfaltllVPPEHYAaalrwVNRLHLRGRLVYERVRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1608 LDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHS--NRMA------AEALRNYRntQGILKDTQLH-------LDDALRGQE 1672
Cdd:COG4913 523 LPDPERPRLDPDSLAGKLDFKPHPFRAWLEAElgRRFDyvcvdsPEELRRHP--RAITRAGQVKgngtrheKDDRRRIRS 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1673 DL------KEQLAMVERRANLLQAEIEELRATLEQTERSRKiAEQELLDASERVQllhTQNTSLINTKKkLETDISQIQG 1746
Cdd:COG4913 601 RYvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLA---EYSWDEIDVAS-AEREIAELEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1747 EMEDI------VQEARNAEEKAKKAITDAAmmaEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKG------ 1814
Cdd:COG4913 676 ELERLdassddLAALEEQLEELEAELEELE---EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElralle 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1815 -----------GKKQIQKLEARVRELEGEVENEQKRNVEAIK---------------------------------GLRKH 1850
Cdd:COG4913 753 erfaaalgdavERELRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldadleslpeylalldrleedGLPEY 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1851 ERRVKE-LTYQTEEDrknvlrLQDLVDKLQSKVKAYKRQAE-------------------EAEEQSNVNLAKFRKIQHEL 1910
Cdd:COG4913 833 EERFKElLNENSIEF------VADLLSKLRRAIREIKERIDplndslkripfgpgrylrlEARPRPDPEVREFRQELRAV 906
|
730 740
....*....|....*....|
gi 82524274 1911 EEAEERADIAESQVNKLRVK 1930
Cdd:COG4913 907 TSGASLFDEELSEARFAALK 926
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
847-1278 |
1.94e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 847 LKSAETEKEMANMKEEFEKAK-ENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAK 925
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKaDELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 926 IKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHatENKVKnlTEEMAGLDETIAKLTKEKKA 1005
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIK--AAEEAKKAEEDKKKAEEAKK 1682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1006 LQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDvENDKQQLDE 1085
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAH 1761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1086 klKKKEFEMSNLQSKIEDEQALGMQLQKKikelqarieeleeeieaERASRAKAEKQRSDLSRELEEISERLEEAGGATS 1165
Cdd:PTZ00121 1762 --LKKEEEKKAEEIRKEKEAVIEEELDEE-----------------DEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIN 1822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1166 AQIEM---NKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNM 1242
Cdd:PTZ00121 1823 DSKEMedsAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
410 420 430
....*....|....*....|....*....|....*.
gi 82524274 1243 EVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLIN 1278
Cdd:PTZ00121 1903 PNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
917-1633 |
2.04e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 72.45 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 917 KTKIQLEAKIKEVTERAEDEEEINAELTAkkRKLEDECSELKKDIddleltlakveKEKHATENKVKNLTEEMAGLDETI 996
Cdd:pfam05483 105 ENKLQENRKIIEAQRKAIQELQFENEKVS--LKLEEEIQENKDLI-----------KENNATRHLCNLLKETCARSAEKT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 997 AKLTKEKkalqEAHQQTLDDLQAEEDKVNTLTKakiklEQQVDDLEGSLEQEKKIRMDLERAKRklegdlkLAQESTMDV 1076
Cdd:pfam05483 172 KKYEYER----EETRQVYMDLNNNIEKMILAFE-----ELRVQAENARLEMHFKLKEDHEKIQH-------LEEEYKKEI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1077 ENDKQQLDEKL---KKKEFEMSNLQSKIEDEQALGMQLQKKIKelqarieeleeeieAERASRAKAEKQRSDLSRELEEI 1153
Cdd:pfam05483 236 NDKEKQVSLLLiqiTEKENKMKDLTFLLEESRDKANQLEEKTK--------------LQDENLKELIEKKDHLTKELEDI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1154 SERLEEAggatsaqIEMNKKREAEFQKMRRDLEEATLQHEATAATLRK---KHADSVAELGEQIDNLQRV----KQKLEK 1226
Cdd:pfam05483 302 KMSLQRS-------MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKakaAHSFVVTEFEATTCSLEELlrteQQRLEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1227 EKSEMK---MEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKT---KEEEQQRLINELTAQRGRLQTESGEYSRQLDE 1300
Cdd:pfam05483 375 NEDQLKiitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHD 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1301 KDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAhalqssrHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRt 1380
Cdd:pfam05483 455 LEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELT-------AHCDKLLLENKELTQEASDMTLELKKHQEDIINCK- 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1381 KYETDAIQRTEELEEAKKKLAQRLQDAEEHV----EAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNF 1456
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENK 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1457 DKILaewkqkyEETHAELEASQKESRSLSTELfkikNAYEESLDHLETLKRENKNLQQEISDLTEQIAEgGKRIHElEKI 1536
Cdd:pfam05483 607 NKNI-------EELHQENKALKKKGSAENKQL----NAYEIKVNKLELELASAKQKFEEIIDNYQKEIE-DKKISE-EKL 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1537 KKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDqLKRNHIRVVESMQSTLDAEIRS-R 1615
Cdd:pfam05483 674 LEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG-LYKNKEQEQSSAKAALEIELSNiK 752
|
730
....*....|....*...
gi 82524274 1616 NDAIRLKKKMEGDLNEME 1633
Cdd:pfam05483 753 AELLSLKKQLEIEKEEKE 770
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1218-1918 |
2.83e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.98 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1218 QRVKQKLEKEKSEMK---MEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEY 1294
Cdd:TIGR04523 36 KQLEKKLKTIKNELKnkeKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1295 SRQLDEKDSLVSQLSRGKQaftqQIEELKRQLEEEIKAKSALahaLQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSE 1374
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKK----ENKKNIDKFLTEIKKKEKE---LEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1375 VAQWRTKYetdaiQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQR 1454
Cdd:TIGR04523 189 IDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1455 NFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDhlETLKRENKNLQQEISDLTEQIAEGGKRIHELE 1534
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1535 KIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLE----------LNQVKSEIDRKIaEKDEEIDQLKRNHIRVVESM 1604
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEnqsykqeiknLESQINDLESKI-QNQEKLNQQKDEQIKKLQQE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1605 QSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNhsnrMAAEALRNYRntqgilkdtqlhlddalrgqEDLKEQLAMVERR 1684
Cdd:TIGR04523 421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKE----LIIKNLDNTR--------------------ESLETQLKVLSRS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1685 ANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIvqearnaEEKAKK 1764
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL-------EDELNK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1765 aitdaamMAEELKKEQdtsahLERMKKNLEQTVKDLQHrldeaeqlalkggkkQIQKLEARVRELEGEVENEQKRNVEAI 1844
Cdd:TIGR04523 550 -------DDFELKKEN-----LEKEIDEKNKEIEELKQ---------------TQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82524274 1845 KGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERAD 1918
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1208-1713 |
3.04e-12 |
|
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: 71.70 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1208 AELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINElTAQRGRL 1287
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALRE-QAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1288 QTESGE-YSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQR 1366
Cdd:pfam05557 81 KKKYLEaLNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1367 AMSKAnsevaqwrtkyeTDAIQRTEELEeakKKLAQRLQDAEEhVEAVNAKCAS---LEKTKQRLQNEVEDLmidveRTN 1443
Cdd:pfam05557 161 QQSSL------------AEAEQRIKELE---FEIQSQEQDSEI-VKNSKSELARipeLEKELERLREHNKHL-----NEN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1444 AACAALDKKQRNFDKILAEwkqKYEETHAELEASQKESRSLSTEL---FKIKNAYEESLDHLETLKRENKNLQQEISDLT 1520
Cdd:pfam05557 220 IENKLLLKEEVEDLKRKLE---REEKYREEAATLELEKEKLEQELqswVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1521 EQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQlelnqvkseidRKIAEKDEEIDQLKRNhirv 1600
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-----------RRVLLLTKERDGYRAI---- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1601 VESMQSTLDAEIRSRNDAIRLK------KKMEGDLNEMEIQLNHSNRmaaealrnyrnTQGILKDTQLHLD---DALRGQ 1671
Cdd:pfam05557 362 LESYDKELTMSNYSPQLLERIEeaedmtQKMQAHNEEMEAQLSVAEE-----------ELGGYKQQAQTLErelQALRQQ 430
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 82524274 1672 EDLKEQLAMVERRANLLQaEIEELRATLEQTERSRKIAEQEL 1713
Cdd:pfam05557 431 ESLADPSYSKEEVDSLRR-KLETLELERQRLREQKNELEMEL 471
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
848-1431 |
3.60e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.99 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 848 KSAETEKEMANMKEEFEKAKENLAKAEAKRKELEEKmvalMQEKNDLqlqvqsEADsLADAEERCDQLIKTKIQLEAKIK 927
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEER----REELETL------EAE-IEDLRETIAETEREREELAEEVR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 928 EVTERAEDEEEINAELTAK-------KRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 1000
Cdd:PRK02224 283 DLRERLEELEEERDDLLAEaglddadAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1001 KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEgsleqekkirMDLERAKRKLEgdlklaqestmDVENDK 1080
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP----------VDLGNAEDFLE-----------ELREER 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1081 QQLDEKLKKKEFEMSNLQSKIEDEQALgmQLQKKIKEL--QARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLE 1158
Cdd:PRK02224 422 DELREREAELEATLRTARERVEEAEAL--LEAGKCPECgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1159 EAGGATSAQIEMNKKREAefqkmRRDLEEATLQHEATAATLRKKHA---DSVAELGEQIDNLQRVKQKLEKEKSEMKMEI 1235
Cdd:PRK02224 500 RAEDLVEAEDRIERLEER-----REDLEELIAERRETIEEKRERAEelrERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1236 DDLASNMEVISKSKGNLEKmcrtLEDQVSELKTKEEEQQRLiNELTAQRGRLQTESGEYsrqLDEKdslvsqlsrgkqaf 1315
Cdd:PRK02224 575 AELNSKLAELKERIESLER----IRTLLAAIADAEDEIERL-REKREALAELNDERRER---LAEK-------------- 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1316 tqqiEELKRQLEEEIKAksALAHALQSSRHDCDLLREQYEEE----QEAKAELQRAMSKANSEvaqwrtkyetdaIQRTE 1391
Cdd:PRK02224 633 ----RERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKldelREERDDLQAEIGAVENE------------LEELE 694
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 82524274 1392 ELEEAKKKLAQRLQDaeehVEAVNAKCASLEKTKQRLQNE 1431
Cdd:PRK02224 695 ELRERREALENRVEA----LEALYDEAEELESMYGDLRAE 730
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1205-1704 |
3.71e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.87 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1205 DSVAELGEQIDNLQRVKQKLEKEKSEMKM--EIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTK--EEEQQRLINEL 1280
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQRRLEllEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1281 TAQRGRLQTESGEYSRQLDEKDSLVSQLSrgkQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEA 1360
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIR---GNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1361 KAELQRamskansEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTK--------------- 1425
Cdd:COG4913 382 FAALRA-------EAAALLEALE----EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniparllalrdala 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1426 QRLQNEVEDL-----MIDVER-----TNAACAALdkkqRNF-------DKILAEWKQKYEETH--------------AEL 1474
Cdd:COG4913 451 EALGLDEAELpfvgeLIEVRPeeerwRGAIERVL----GGFaltllvpPEHYAAALRWVNRLHlrgrlvyervrtglPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1475 EASQKESRSLSTELFKIKNAYEESLDHL-------------ETLKRENKNLQQeisdlTEQIAEGGKR------------ 1529
Cdd:COG4913 527 ERPRLDPDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRAITR-----AGQVKGNGTRhekddrrrirsr 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1530 ----------IHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEID-----RKIAEKDEEIDQLK 1594
Cdd:COG4913 602 yvlgfdnrakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaeREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1595 RNHIrVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDL 1674
Cdd:COG4913 682 ASSD-DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
570 580 590
....*....|....*....|....*....|
gi 82524274 1675 KEQLAMVERRanlLQAEIEELRATLEQTER 1704
Cdd:COG4913 761 DAVERELREN---LEERIDALRARLNRAEE 787
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
854-1777 |
3.94e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 72.00 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 854 KEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKnDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKIKEVTERA 933
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 934 EDEEEINAELTAKKRKLEDECSELKKDIDdleltlakvekekHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAH--- 1010
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKtel 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1011 --QQTLDDLQAEEDKVNTLTKAKIKLEQQ----VDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLD 1084
Cdd:TIGR00606 346 lvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1085 EKLKKKEFEMSNLQSKIEDEQAL----GMQLQKKIKELQARIEELEEEIEAERASR------AKAEKQRSDLSRELEEIS 1154
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEIlekkQEELKFVIKELQQLEGSSDRILELDQELRkaerelSKAEKNSLTETLKKEVKS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1155 ERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATA-ATLRKKHADSVAELGEQIDNLQRVKQ------KLEKE 1227
Cdd:TIGR00606 506 LQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKdEQIRKIKSRHSDELTSLLGYFPNKKQledwlhSKSKE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1228 KSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTK----------EEEQQRLINELTAQRGRLQTESG----- 1292
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgsqdeESDLERLKEEIEKSSKQRAMLAGatavy 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1293 -EYSRQLDEKDS------------------LVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQ 1353
Cdd:TIGR00606 666 sQFITQLTDENQsccpvcqrvfqteaelqeFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1354 YEEEQEAKAELQRAMSKANSEVAQWRTKYET-DAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCAS------LEKTKQ 1426
Cdd:TIGR00606 746 IPELRNKLQKVNRDIQRLKNDIEEQETLLGTiMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAklqgsdLDRTVQ 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1427 RLQNEVEDlmidvertnaacaaldkKQRNFDKILaewkQKYEETHAELEASQKESRSLSTELFKIKN---AYEESLDHLE 1503
Cdd:TIGR00606 826 QVNQEKQE-----------------KQHELDTVV----SKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQ 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1504 TLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELqaaleeaeASLEHEEGKIlrIQLELNQVKSEIDRKI 1583
Cdd:TIGR00606 885 QFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEEL--------ISSKETSNKK--AQDKVNDIKEKVKNIH 954
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1584 AEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHSnrmaaealrnyRNTQGILKDtQLH 1663
Cdd:TIGR00606 955 GYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQ-----------KIQERWLQD-NLT 1022
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1664 LddaLRGQEDLKEqlamVERRANLLQAEIEELRATLEQTERSRkiaeqelldASERVQLLHTQNTSLINTKKKLETDISQ 1743
Cdd:TIGR00606 1023 L---RKRENELKE----VEEELKQHLKEMGQMQVLQMKQEHQK---------LEENIDLIKRNHVLALGRQKGYEKEIKH 1086
|
970 980 990
....*....|....*....|....*....|....
gi 82524274 1744 IQGEMEDivQEARNAEEKAKKAITDAAMMAEELK 1777
Cdd:TIGR00606 1087 FKKELRE--PQFRDAEEKYREMMIVMRTTELVNK 1118
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1187-1764 |
4.39e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 71.29 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1187 EATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEiddLASNMEVISKSKGNLEKMCRTLEDQVSEL 1266
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFK---LKEDHEKIQHLEEEYKKEINDKEKQVSLL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1267 KTKEEEQQRLINELTAqrgrLQTESGEYSRQLDEKDSLVS----QLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQ- 1341
Cdd:pfam05483 246 LIQITEKENKMKDLTF----LLEESRDKANQLEEKTKLQDenlkELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQi 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1342 SSRHDCDLLRE---QYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQ----DAEEHVEAV 1414
Cdd:pfam05483 322 ATKTICQLTEEkeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QRLEKNEDQLKIITMELQkkssELEEMTKFK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1415 NAKCASLEKTKQRLqNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQ-------KESRSLSTE 1487
Cdd:pfam05483 401 NNKEVELEELKKIL-AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKtseehylKEVEDLKTE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1488 LFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRI----HELEKIKKQIE---QEKSELQAALEEAEASL-- 1558
Cdd:pfam05483 480 LEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIinckKQEERMLKQIEnleEKEMNLRDELESVREEFiq 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1559 EHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKMEG--------DLN 1630
Cdd:pfam05483 560 KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENkqlnayeiKVN 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1631 EMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANL-LQAEIEELRATLEQTERS-RKI 1708
Cdd:pfam05483 640 KLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKrCQHKIAEMVALMEKHKHQyDKI 719
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 1709 AEQElldaSERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKK 1764
Cdd:pfam05483 720 IEER----DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEK 771
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1451-1942 |
5.93e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.25 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1451 KKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDH---LETLKRENKNLQQEISDLTEQIAEGG 1527
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1528 KRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKIlriqlELNQVKSEIDRKIAEKDEEIDQLKRnHIRVVESMQST 1607
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE-----EYLDELREIEKRLSRLEEEINGIEE-RIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1608 LDaeirsrndaiRLKKKMEGDLNEMEIqLNHSNRMAAEALRNYRNTQGILKDTqlhlddALRGQEDLKEQLAMVERRANL 1687
Cdd:PRK03918 340 LE----------ELKKKLKELEKRLEE-LEERHELYEEAKAKKEELERLKKRL------TGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1688 LQAEIEEL---RATLEQTERSRKIAEQELLDASERVQLLHTQNTSliNTKKKLetdISQIQGEMEDIVQEARNAEEKAKK 1764
Cdd:PRK03918 403 IEEEISKItarIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE--EHRKEL---LEEYTAELKRIEKELKEIEEKERK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1765 AITDAAMMAEELKKEQDtsahLERMKKNLEQtVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENeQKRNVEAI 1844
Cdd:PRK03918 478 LRKELRELEKVLKKESE----LIKLKELAEQ-LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS-LKKELEKL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1845 KGLRKHERRVKELTYQTEEDRKNVLR---------LQDLVDKLQSKVKAYKR--QAEEAEEQSNVNLAKFRKIQHELEEA 1913
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKeleelgfesVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKA 631
|
490 500
....*....|....*....|....*....
gi 82524274 1914 EERADIAESQVNKLRVKSREVHTKIISEE 1942
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKYSEEE 660
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1391-1942 |
8.54e-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: 70.92 E-value: 8.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1391 EELEEAKKKLAQRLQDAEE-HveavnakcaslEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEE 1469
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNElH-----------EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1470 THAELEASqkesRSLSTELFKIKNAyeeSLDHLETLKRENKNLQQEISDLTEQIAEG-GKRIHELEKIKK-QIEQEKSEL 1547
Cdd:pfam15921 150 TVHELEAA----KCLKEDMLEDSNT---QIEQLRKMMLSHEGVLQEIRSILVDFEEAsGKKIYEHDSMSTmHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1548 QAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIaekdeeiDQLKRNHirvvesmqstldaeirsrndairlKKKMEG 1627
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALKSESQNKI-------ELLLQQH------------------------QDRIEQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1628 DLNEMEIQLNHSNRMAAEALRNYRNTQgilkdTQLHLDdalrgQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRK 1707
Cdd:pfam15921 272 LISEHEVEITGLTEKASSARSQANSIQ-----SQLEII-----QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1708 IAEQELldaservqllhTQNTSLINTkkkletDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLE 1787
Cdd:pfam15921 342 DKIEEL-----------EKQLVLANS------ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1788 RMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLEARVRELEGEVENEQKRNVEAIKGLRKHERRVKELTYQTEEDrKN 1867
Cdd:pfam15921 405 DRDTGNSITIDHLRRELDDRNM--------EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEST-KE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1868 VLR-------------------LQDLVDKLQSKVKAYK-RQAEEAEEQSNVNLaKFRKIQHELEEAEERADI-AESQVNK 1926
Cdd:pfam15921 476 MLRkvveeltakkmtlessertVSDLTASLQEKERAIEaTNAEITKLRSRVDL-KLQELQHLKNEGDHLRNVqTECEALK 554
|
570
....*....|....*.
gi 82524274 1927 LRVKSREVHTKIISEE 1942
Cdd:pfam15921 555 LQMAEKDKVIEILRQQ 570
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
850-1307 |
1.21e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 850 AETEKEMANMKEEFEKAKENLAKAEAKR-------KELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQL 922
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREReelaeevRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 923 EAKIKEV--------------TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEE 988
Cdd:PRK02224 327 RDRLEECrvaaqahneeaeslREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 989 MAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVN---TLTKA--------KIKLEQQVDDLEGSLEQEKKIRMDLER 1057
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATLRTARERVEeaeALLEAgkcpecgqPVEGSPHVETIEEDRERVEELEAELED 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1058 AKRKLEG-DLKLAQ-ESTMDVENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERAS 1135
Cdd:PRK02224 487 LEEEVEEvEERLERaEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1136 RAKAEKQRSDLSRELEEISERLE--EAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAEL-GE 1212
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIEslERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFdEA 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1213 QIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRL------INELTAQRGR 1286
Cdd:PRK02224 647 RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALealydeAEELESMYGD 726
|
490 500
....*....|....*....|....*.
gi 82524274 1287 LQTE-----SGEYSRQLDEKDSLVSQ 1307
Cdd:PRK02224 727 LRAElrqrnVETLERMLNETFDLVYQ 752
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
854-1523 |
1.62e-11 |
|
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: 69.66 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 854 KEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKIKEVTERA 933
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 934 EDEEEINAELTAKKRKLEDECSELKKDIDdleltlakvekekhatenKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQT 1013
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQ------------------KNKSLESQISELKKQNNQLKDNIEKKQQEINEK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1014 LDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKlaqestmDVENDKQQ-----LDEKLK 1088
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS-------DLNNQKEQdwnkeLKSELK 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1089 KKEFEMSNLQSKIEDEQALGMQLQKKIKELqarieeleeeieaerasrakaEKQRSDLSRELEEISERLEEaggaTSAQI 1168
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNKIISQLNEQISQL---------------------KKELTNSESENSEKQRELEE----KQNEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1169 EMNKKreaEFQKMRRDLEEATLQHEATAATLRKKHADSvAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKS 1248
Cdd:TIGR04523 373 EKLKK---ENQSYKQEIKNLESQINDLESKIQNQEKLN-QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1249 KGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELK---RQ 1325
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKekiEK 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1326 LEEEIKAKSALAHALQS------SRHDCDLLREQYEEEQEAKAEL---QRAMSKANSEVAQWRTKYET---DAIQRTEEL 1393
Cdd:TIGR04523 529 LESEKKEKESKISDLEDelnkddFELKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQELIDQKEKekkDLIKEIEEK 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1394 EEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAE 1473
Cdd:TIGR04523 609 EKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKE 688
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 82524274 1474 LEASQKE---SRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQI 1523
Cdd:TIGR04523 689 LSLHYKKyitRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKF 741
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
844-1525 |
1.86e-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: 69.37 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 844 KPLLKSAETEKEMANM-KEEFEKAKENLAKAEAKRKELEEKMVALmqeKNDLQLQVQSEADSLADAEercdqliKTKIQL 922
Cdd:pfam05483 144 KDLIKENNATRHLCNLlKETCARSAEKTKKYEYEREETRQVYMDL---NNNIEKMILAFEELRVQAE-------NARLEM 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 923 EAKIKEVTERAED-EEEINAELTAKKRK---LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAK 998
Cdd:pfam05483 214 HFKLKEDHEKIQHlEEEYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDH 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 999 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKL----EQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTM 1074
Cdd:pfam05483 294 LTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1075 DVENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEIS 1154
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIH 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1155 ERLEEAGGATSAQIEMNKkreaEFQKMRRDLEEATLQHeataatlrkkhadsvAELGEQIDNLQRVKQKLEKEKSEMKME 1234
Cdd:pfam05483 454 DLEIQLTAIKTSEEHYLK----EVEDLKTELEKEKLKN---------------IELTAHCDKLLLENKELTQEASDMTLE 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1235 iddLASNMEVISKSKGNLEKMCRTLEdqvselkTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKdslvsqlsrgkqa 1314
Cdd:pfam05483 515 ---LKKHQEDIINCKKQEERMLKQIE-------NLEEKEMNLRDELESVREEFIQKGDEVKCKLDKS------------- 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1315 ftqqiEELKRQLEEEIKAKSALAHALQSSrhdCDLLREQYEEEQEAKAELQ---RAMSKANSEVAQWRTKYETDAIQRTE 1391
Cdd:pfam05483 572 -----EENARSIEYEVLKKEKQMKILENK---CNNLKKQIENKNKNIEELHqenKALKKKGSAENKQLNAYEIKVNKLEL 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1392 ELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAAC--------AALDKKQRNFDKILAEW 1463
Cdd:pfam05483 644 ELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCqhkiaemvALMEKHKHQYDKIIEER 723
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 82524274 1464 KQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAE 1525
Cdd:pfam05483 724 DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
850-1276 |
1.98e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 850 AETEKEMANMKEEFEKAKENLAKAEAKRKeLEEKMVALMQEKNDLQLQ----------VQSEADSLADAEERCDQLIKTK 919
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRlsrleeeingIEERIKELEEKEERLEELKKKL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 920 IQLEAKIKEVTERAEDEEEINAeLTAKKRKLEDECSELkkDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKL 999
Cdd:PRK03918 348 KELEKRLEELEERHELYEEAKA-KKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1000 TKEKKALQEAHQQ--TLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTM--- 1074
Cdd:PRK03918 425 KKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeq 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1075 --DVENDKQQLD-EKLKKKEFEMSNLQSK---IEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR 1148
Cdd:PRK03918 505 lkELEEKLKKYNlEELEKKAEEYEKLKEKlikLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGF 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1149 E-LEEISERLEEAGGATSAQIEM-NKKREAEFQKMRRDLEEATLqhEATAATLRKKHADsVAELGEQIDNLQRV-----K 1221
Cdd:PRK03918 585 EsVEELEERLKELEPFYNEYLELkDAEKELEREEKELKKLEEEL--DKAFEELAETEKR-LEELRKELEELEKKyseeeY 661
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 82524274 1222 QKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRL 1276
Cdd:PRK03918 662 EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL 716
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
898-1609 |
2.47e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.10 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 898 VQSEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRkledecSELKKDIDDLELTLAKVEKEKHA 977
Cdd:pfam12128 239 IRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 978 TENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAE-----------EDKVNTLT------KAKIKlEQQVDD 1040
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSElenleerlkalTGKHQDVTakynrrRSKIK-EQNNRD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1041 LEGSLEQEKKIRMDLERAKRKLEGDLKlAQESTMDVENDKQQLDEKLKKKEFE--MSNLQSKIEDEQA---LGMQLQKKI 1115
Cdd:pfam12128 392 IAGIKDKLAKIREARDRQLAVAEDDLQ-ALESELREQLEAGKLEFNEEEYRLKsrLGELKLRLNQATAtpeLLLQLENFD 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1116 KEL---QARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRR----DLEEA 1188
Cdd:pfam12128 471 ERIeraREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRkeapDWEQS 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1189 TLQHEATAATLRKK-HADSVAELGEQIDNLQRVKQKLEK-EKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSEL 1266
Cdd:pfam12128 551 IGKVISPELLHRTDlDPEVWDGSVGGELNLYGVKLDLKRiDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1267 KTKEEEQQRlinELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKaksALAHALQssrhd 1346
Cdd:pfam12128 631 NGELEKASR---EETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLK---QLDKKHQ----- 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1347 cDLLREQYEEEQEAKAELQramskansevAQWRtkyetdaiqrteELEEAKKKLAQRLqDAEEHVEAVNAKcASLEKTKQ 1426
Cdd:pfam12128 700 -AWLEEQKEQKREARTEKQ----------AYWQ------------VVEGALDAQLALL-KAAIAARRSGAK-AELKALET 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1427 RLQNEVEDLMIDVERtnaacaaldkkqrnfdkiLAEWKQKYEETHAELE-ASQKESRSLSTELFKiknaYEESLDHLETL 1505
Cdd:pfam12128 755 WYKRDLASLGVDPDV------------------IAKLKREIRTLERKIErIAVRRQEVLRYFDWY----QETWLQRRPRL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1506 KRENKNLQQEISDLTEQIAeggKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRI-QLELNQVKSEIDRKIA 1584
Cdd:pfam12128 813 ATQLSNIERAISELQQQLA---RLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLaTLKEDANSEQAQGSIG 889
|
730 740
....*....|....*....|....*
gi 82524274 1585 EKDEEIDQLKRNHIRVVESMQSTLD 1609
Cdd:pfam12128 890 ERLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1533-1937 |
2.62e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1533 LEKIKKQIEQEKS--------ELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKiAEKDEEIDQLKRNhirvVESM 1604
Cdd:PRK02224 189 LDQLKAQIEEKEEkdlherlnGLESELAELDEEIERYEEQREQARETRDEADEVLEEH-EERREELETLEAE----IEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1605 QSTLDAEIRSRNDAIRlkkkmegdlnemEIQlnhSNRMAAEALRNYRNtqGILKDTQLhlDDAlrGQEDLKEQLAMVERR 1684
Cdd:PRK02224 264 RETIAETEREREELAE------------EVR---DLRERLEELEEERD--DLLAEAGL--DDA--DAEAVEARREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1685 ANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKK 1764
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1765 AITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLaLKGGK---------------------KQIQKLE 1823
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-LEAGKcpecgqpvegsphvetieedrERVEELE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1824 ARVRELEGEVENEQKRnVEAIKGLRKHERRVKELtyqtEEDRKNVlrlQDLVDKLQSKVKAYKRQAEEAEEQSNvnlakf 1903
Cdd:PRK02224 482 AELEDLEEEVEEVEER-LERAEDLVEAEDRIERL----EERREDL---EELIAERRETIEEKRERAEELRERAA------ 547
|
410 420 430
....*....|....*....|....*....|....
gi 82524274 1904 rKIQHELEEAEERADIAESQVNKLRVKSREVHTK 1937
Cdd:PRK02224 548 -ELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
854-1242 |
5.41e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.87 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 854 KEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDL--QLQVQSEADSLADAEERCDQLIKTKIQLEAKIKEVTE 931
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 932 RAEDEEEINAELTAKKRKLEDEC-----------SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 1000
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1001 KEKKALQE-----------AHQQTLDDLQAEEDKV---------------NTLTKAKIKLEQQVDDLEGSLEQEKKIRMD 1054
Cdd:COG4717 241 LEERLKEArlllliaaallALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1055 LERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKKEfemsnlqskIEDEQALGMQLQKKIKELqarIEELEEEIEAERA 1134
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAE---------ELEEELQLEELEQEIAAL---LAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1135 SRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKR--EAEFQKMRRDLEEATLQHEAtaatLRKKHADSVAELG- 1211
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEE----LREELAELEAELEq 464
|
410 420 430
....*....|....*....|....*....|..
gi 82524274 1212 -EQIDNLQRVKQKLEKEKSEMKMEIDDLASNM 1242
Cdd:COG4717 465 lEEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1250-1857 |
1.25e-10 |
|
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: 66.70 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1250 GNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQL-------DEKDSLVSQLSrGKQAFTQQIEEL 1322
Cdd:pfam07111 59 QALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAvaekagqAEAEGLRAALA-GAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1323 KRQLEEEIKA--KSALAHALQSSRHDCDLLREQYE--EEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKK 1398
Cdd:pfam07111 138 SQRELEEIQRlhQEQLSSLTQAHEEALSSLTSKAEglEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1399 KLAQRLQD--AEEHVEAVNAKCASLEKtkQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILA----EWKQKYEETHA 1472
Cdd:pfam07111 218 TLVESLRKyvGEQVPPEVHSQTWELER--QELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLAlqeeELTRKIQPSDS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1473 ELEASQKESRSLstelfkIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEggkrihELEKIKKQiEQEKSELQAALE 1552
Cdd:pfam07111 296 LEPEFPKKCRSL------LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAE------LQEQVTSQ-SQEQAILQRALQ 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1553 EAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKrnhiRVVESMQSTldaeirsrndAIRLKKKMeGDLNEM 1632
Cdd:pfam07111 363 DKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLK----FVVNAMSST----------QIWLETTM-TRVEQA 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1633 EIQLNHSNRMAAEALRNYRNTQGILKD----TQLHLDD------ALRGQEDLKEQLAMVERRANLLQAEIeELRATLEQT 1702
Cdd:pfam07111 428 VARIPSLSNRLSYAVRKVHTIKGLMARkvalAQLRQEScpppppAPPVDADLSLELEQLREERNRLDAEL-QLSAHLIQQ 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1703 ERSRKIAEQElldaSERVQllhtqntsLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDT 1782
Cdd:pfam07111 507 EVGRAREQGE----AERQQ--------LSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEI 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1783 SAH-----LERMKKNLEQTVKDLQHRLDEA--EQLALKGGKKQIQKLEARVRELEGEVE--NEQKRNVEAikglRKHERR 1853
Cdd:pfam07111 575 YGQalqekVAEVETRLREQLSDTKRRLNEArrEQAKAVVSLRQIQHRATQEKERNQELRrlQDEARKEEG----QRLARR 650
|
....
gi 82524274 1854 VKEL 1857
Cdd:pfam07111 651 VQEL 654
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
851-1236 |
1.35e-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: 66.58 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 851 ETEKEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEK-----NDLQLQVQSEADSLADAEERCDQLIKTKIQLEAK 925
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 926 I----KEVTERAEDEEEINAELTAKKRKLEDecseLKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTK 1001
Cdd:TIGR04523 344 IsqlkKELTNSESENSEKQRELEEKQNEIEK----LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1002 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDVEND-- 1079
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKElk 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1080 -----KQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEaerasRAKAEKQRSDLSRELEEIS 1154
Cdd:TIGR04523 500 klneeKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEELK 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1155 ERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEatlqHEATAATLRKKHADSVAE---LGEQIDNLQRVKQKLEKEKSEM 1231
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE----KEKKISSLEKELEKAKKEnekLSSIIKNIKSKKNKLKQEVKQI 650
|
....*
gi 82524274 1232 KMEID 1236
Cdd:TIGR04523 651 KETIK 655
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1083-1633 |
1.60e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 66.46 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1083 LDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEEleeeieaerasrakAEKQRSDLSRELEEISERLEEAGG 1162
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN--------------AMDDYNNLKSALNELSSLEDMKNR 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1163 ATS--AQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMkmeiDDLAS 1240
Cdd:PRK01156 254 YESeiKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKY----HAIIK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1241 NMEVISKSKGNLEKMCRTLED---QVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQ 1317
Cdd:PRK01156 330 KLSVLQKDYNDYIKKKSRYDDlnnQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1318 QIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEeeqeakaelqraMSKANSEVAQWRTKYETDAIQR-TEELEEA 1396
Cdd:PRK01156 410 ELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNME------------MLNGQSVCPVCGTTLGEEKSNHiINHYNEK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1397 KKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQ-----------NEVEDLMIDVERTNAACAALDKKQRNFDKILAEWK- 1464
Cdd:PRK01156 478 KSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLEseeinksineyNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKs 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1465 -------QKYEE--------THAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKN----LQQEISDLTEQIAE 1525
Cdd:PRK01156 558 lkledldSKRTSwlnalaviSLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKsireIENEANNLNNKYNE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1526 GGKRIHELEKIKKQIEQEKSELqAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEeidqlKRNHIRVVESMQ 1605
Cdd:PRK01156 638 IQENKILIEKLRGKIDNYKKQI-AEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR-----LESTIEILRTRI 711
|
570 580
....*....|....*....|....*...
gi 82524274 1606 STLDAEIRSRNDAIRLKKKMEGDLNEME 1633
Cdd:PRK01156 712 NELSDRINDINETLESMKKIKKAIGDLK 739
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1233-1706 |
1.68e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1233 MEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGK 1312
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1313 QAFT--QQIEELKRQLEEEIKAKSALAHALQSSRHdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRT 1390
Cdd:COG4717 126 QLLPlyQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1391 EELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQ--NEVEDLMIDVERTNAACAALDKKQRNFDKILAEWK---- 1464
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1465 ------QKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKK 1538
Cdd:COG4717 282 vlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1539 QIEQEKSELQAALEEAEASLEHEEGkiLRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQ-STLDAEIRSRND 1617
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVEDEEE--LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeEELEEELEELEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1618 AIRLKKKMEGDLNEMEIQLNHSNRMAAEALRnyrntqgilkdtqlhLDDALRGQEDLKEQLAMVERRANLLQAEIEELRA 1697
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEEDGE---------------LAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
....*....
gi 82524274 1698 TLEQTERSR 1706
Cdd:COG4717 505 AREEYREER 513
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1272-1844 |
1.81e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1272 EQQRLINELTaQRGRLQtesgEYSRQLDEKDSLVSQLSRGKQaftQQIEELKRQLEE-EIKAKSALAHALQSSRHDCDLL 1350
Cdd:PRK02224 150 DRQDMIDDLL-QLGKLE----EYRERASDARLGVERVLSDQR---GSLDQLKAQIEEkEEKDLHERLNGLESELAELDEE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1351 REQYEEEQEAKAELQRAMSKANSEVAQWRtkyetdaiQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQN 1430
Cdd:PRK02224 222 IERYEEQREQARETRDEADEVLEEHEERR--------EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1431 EVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEE-------THAELEASQKESRSLSTELFKIKNAYEESLDHLE 1503
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEcrvaaqaHNEEAESLREDADDLEERAEELREEAAELESELE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1504 TLKRENKNLQQEISDLTEQIAEGGKRIH-------ELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVK 1576
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGdapvdlgNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1577 ----------SEIDRKIAEKDEEIDQLKRNhIRVVESMQSTLDAEIRSRNDAIRLKKKMEgDLNEMEIQLNHSNRMAAEA 1646
Cdd:PRK02224 454 cpecgqpvegSPHVETIEEDRERVEELEAE-LEDLEEEVEEVEERLERAEDLVEAEDRIE-RLEERREDLEELIAERRET 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1647 LRNYRNTQGILKDTQLHLDDALRGQED----LKEQLAMVERRANLLQAEIEELRATLEQTERSRKI------AEQELLDA 1716
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREaaaeAEEEAEEAREEVAELNSKLAELKERIESLERIRTLlaaiadAEDEIERL 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1717 SERVQLLHTQNTSLINTKKKLETDISQIQGEM-EDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQ 1795
Cdd:PRK02224 612 REKREALAELNDERRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE 691
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 82524274 1796 TVKDLQHRLD--EAEQLALKGGKKQIQKLEARVRELEGEVeneQKRNVEAI 1844
Cdd:PRK02224 692 ELEELRERREalENRVEALEALYDEAEELESMYGDLRAEL---RQRNVETL 739
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1513-1765 |
3.30e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.40 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1513 QQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNqvksEIDRKIAEKDEEIDQ 1592
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1593 LKRNHIRVVESMQSTLDAEIRSrndairlkkkmeGDLNEMEIQLNHSNrmAAEALRNYRNTQGILKDTQLHLddalrgqE 1672
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRL------------GRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQA-------E 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1673 DLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIV 1752
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250
....*....|...
gi 82524274 1753 QEARNAEEKAKKA 1765
Cdd:COG4942 234 AEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1474-1921 |
6.72e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1474 LEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEe 1553
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1554 aeasleheegkilriQLELNQVKSEIDRKIAEKDEEIDQLKRnhirvvesmqstldaEIRSRNDAIRLKKKMEGDLNEME 1633
Cdd:COG4717 127 ---------------LLPLYQELEALEAELAELPERLEELEE---------------RLEELRELEEELEELEAELAELQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1634 IQLNHSNRMAAEALRNYrntqgiLKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQEL 1713
Cdd:COG4717 177 EELEELLEQLSLATEEE------LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1714 LDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKK 1791
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1792 NLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENE-QKRNVEAIKGLRKH----------ERRVKELTYQ 1860
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlAEAGVEDEEELRAAleqaeeyqelKEELEELEEQ 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 82524274 1861 TEEDRKNVLRLQDLVDK--LQSKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAE 1921
Cdd:COG4717 411 LEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
897-1881 |
8.54e-10 |
|
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: 64.30 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 897 QVQSEADSLADAEERCDQLIKTKIqlEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKE-- 974
Cdd:TIGR01612 519 EVPSKNIIGFDIDQNIKAKLYKEI--EAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEii 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 975 -----KHATENKVKNLTEEmaglDETIAKLTKEKKALqEAHQQTLDDLqaeedkvntltkAKIKLEQQVDDLEGSLEQEK 1049
Cdd:TIGR01612 597 yinklKLELKEKIKNISDK----NEYIKKAIDLKKII-ENNNAYIDEL------------AKISPYQVPEHLKNKDKIYS 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1050 KIRMDLERAkrkLEGDL-KLAQE-STMDVENDKQQLDEKLKkkefeMSNLQSKIEDEQALGMQLQKKIKELQARIEELEE 1127
Cdd:TIGR01612 660 TIKSELSKI---YEDDIdALYNElSSIVKENAIDNTEDKAK-----LDDLKSKIDKEYDKIQNMETATVELHLSNIENKK 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1128 EIEAERASRAKaEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADS- 1206
Cdd:TIGR01612 732 NELLDIIVEIK-KHIHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAk 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1207 --VAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISkskgNLEKMCRtledqvSELKTKEEEQQRLINELTAQR 1284
Cdd:TIGR01612 811 qnYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFI----NFENNCK------EKIDSEHEQFAELTNKIKAEI 880
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1285 GRLQTEsgEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRqLEEEIKAKSALAHALQSSRHDCDLLRE------------ 1352
Cdd:TIGR01612 881 SDDKLN--DYEKKFNDSKSLINEINKSIEEEYQNINTLKK-VDEYIKICENTKESIEKFHNKQNILKEilnknidtikes 957
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1353 -----QYEEEQE-----AKAELQRAMSKA--------NSEVAQW--------RTKYETDAIQRTEELEEAKKKLAQRLQD 1406
Cdd:TIGR01612 958 nliekSYKDKFDntlidKINELDKAFKDAslndyeakNNELIKYfndlkanlGKNKENMLYHQFDEKEKATNDIEQKIED 1037
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1407 AEEHVEAVN-AKCASLEKTKQRLQNE----VEDLMIDV-ERTNAACAALDK-----KQRNFDKILAEWKQKYEEthaele 1475
Cdd:TIGR01612 1038 ANKNIPNIEiAIHTSIYNIIDEIEKEigknIELLNKEIlEEAEINITNFNEikeklKHYNFDDFGKEENIKYAD------ 1111
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1476 asqkESRSLSTELFKIKNAYEESLDHLETLKRENKN----LQQEISDLtEQIAEGGKRIHELEKIKKQIEQ--EKSELQA 1549
Cdd:TIGR01612 1112 ----EINKIKDDIKNLDQKIDHHIKALEEIKKKSENyideIKAQINDL-EDVADKAISNDDPEEIEKKIENivTKIDKKK 1186
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1550 ALEEAEASLEHEEGKILRIQLELNQVKS-------EIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDaEIRSRNDAIRLK 1622
Cdd:TIGR01612 1187 NIYDEIKKLLNEIAEIEKDKTSLEEVKGinlsygkNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLD-EIKEKSPEIENE 1265
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1623 KKMEGDLN-EMEIqLNHSN----------RMAAEALRNYRN-----TQG---------ILKDTQLHLDDALRGQEDLKEQ 1677
Cdd:TIGR01612 1266 MGIEMDIKaEMET-FNISHdddkdhhiisKKHDENISDIREkslkiIEDfseesdindIKKELQKNLLDAQKHNSDINLY 1344
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1678 LAMVERRANLLQAE-----IEELRATLEQTERSRKIAEQElLDASERVQLLHTQNTSLINTKKKLETDI----------- 1741
Cdd:TIGR01612 1345 LNEIANIYNILKLNkikkiIDEVKEYTKEIEENNKNIKDE-LDKSEKLIKKIKDDINLEECKSKIESTLddkdidecikk 1423
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1742 -----SQIQGEMEDIVQEARNAEE-------------------------KAKKAITDAAMMAEELKKEQDTS-------- 1783
Cdd:TIGR01612 1424 ikelkNHILSEESNIDTYFKNADEnnenvlllfkniemadnksqhilkiKKDNATNDHDFNINELKEHIDKSkgckdead 1503
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1784 ---AHLERMKKNLEQTVKDLQHRLDEAEQLALKGG----KKQIQKLEARVRELEGEVENEQKRNVEAIKGLRKHERRVKE 1856
Cdd:TIGR01612 1504 knaKAIEKNKELFEQYKKDVTELLNKYSALAIKNKfaktKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIED 1583
|
1130 1140
....*....|....*....|....*
gi 82524274 1857 LTYQTEEDRKNVLRLQDLVDKLQSK 1881
Cdd:TIGR01612 1584 DAAKNDKSNKAAIDIQLSLENFENK 1608
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
837-1333 |
1.12e-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: 63.59 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 837 MKLYFKIKpllksaETEKEMANMKEEFEKAKENlakaeaKRKELEEKMVALMQEKN---DLQLQVQSEADSLADAEErcd 913
Cdd:pfam05483 211 LEMHFKLK------EDHEKIQHLEEEYKKEIND------KEKQVSLLLIQITEKENkmkDLTFLLEESRDKANQLEE--- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 914 qliKTKIQLEakikEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLD 993
Cdd:pfam05483 276 ---KTKLQDE----NLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHS 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 994 ETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTkakIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQEST 1073
Cdd:pfam05483 349 FVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIIT---MELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1074 M------DVENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLS 1147
Cdd:pfam05483 426 QfekiaeELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELT 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1148 RELEEISERLEEaggaTSAQIEMNKKREAEFQKMRRDLEEATLQheataatLRkkhadsvaelgeqiDNLQRVKQKLEKE 1227
Cdd:pfam05483 506 QEASDMTLELKK----HQEDIINCKKQEERMLKQIENLEEKEMN-------LR--------------DELESVREEFIQK 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1228 KSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQ 1307
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNK 640
|
490 500
....*....|....*....|....*.
gi 82524274 1308 LSRGKQAFTQQIEELKRQLEEEIKAK 1333
Cdd:pfam05483 641 LELELASAKQKFEEIIDNYQKEIEDK 666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
947-1571 |
1.15e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 947 KRKLEDECSELKKDIDDLELTLAKVEKEKH---------ATENKVKNLTEEMAGLDETIAKLT-----KEKKALQEAHQQ 1012
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREqiellepirELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1013 TLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMD-LERAKRKLEGDLKLAQESTMDVENDKQQLDEKLK--K 1089
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLPasA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1090 KEFE--MSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQ 1167
Cdd:COG4913 380 EEFAalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1168 -------IEMnKKREAEFqkmrRDLEEATLQHEATAATLRKKHADSVAELGEQID-----NLQRVKQKLEKEKSE----- 1230
Cdd:COG4913 460 lpfvgelIEV-RPEEERW----RGAIERVLGGFALTLLVPPEHYAAALRWVNRLHlrgrlVYERVRTGLPDPERPrldpd 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1231 ---MKMEIDD----------LASNMEVISkskgnlekmCRTLED------------QVSELKTKEEEQ------------ 1273
Cdd:COG4913 535 slaGKLDFKPhpfrawleaeLGRRFDYVC---------VDSPEElrrhpraitragQVKGNGTRHEKDdrrrirsryvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1274 ---QRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQ----------------QIEELKRQLEEEIKAKS 1334
Cdd:COG4913 606 fdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvasaerEIAELEAELERLDASSD 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1335 ALAhALQSSRhdcDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTkyETDAIQRTEELEEAKKKLAQRlQDAEEHVEAV 1414
Cdd:COG4913 686 DLA-ALEEQL---EELEAELEELEEELDELKGEIGRLEKELEQAEE--ELDELQDRLEAAEDLARLELR-ALLEERFAAA 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1415 NAKcASLEKTKQRLQNEVEDLMidvertnaacAALDKKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKN- 1493
Cdd:COG4913 759 LGD-AVERELRENLEERIDALR----------ARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEd 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1494 ---AYEESLdhletLKRENKNLQQEISDLTEQIAEggkrihELEKIKKQIEqeksELQAALEEaeasLEHEEGKILRIQL 1570
Cdd:COG4913 828 glpEYEERF-----KELLNENSIEFVADLLSKLRR------AIREIKERID----PLNDSLKR----IPFGPGRYLRLEA 888
|
.
gi 82524274 1571 E 1571
Cdd:COG4913 889 R 889
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
921-1121 |
1.53e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 921 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 1000
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1001 KEKK----ALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDV 1076
Cdd:COG4942 104 EELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 82524274 1077 ENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQAR 1121
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
838-1511 |
1.64e-09 |
|
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: 63.14 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 838 KLYFKIKPLLKSAETEKEMANMKEEFEKAKENLAKAE--AKRKELEEKMVALMQEKNDLQLQVQSEADSLAD------AE 909
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQlnhhttTR 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 910 ERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKV 982
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 983 KNLTEEMAGLDETIAKLTKekkalQEAHQQTLDDLQAEEDKVNT----LTKAKIKLEQQVDDLEGSLEQEKKIRMDLERA 1058
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCG-----SQDEESDLERLKEEIEKSSKqramLAGATAVYSQFITQLTDENQSCCPVCQRVFQT 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1059 KRKLEGDLKLAQESTMDVENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELqarieeleeeieaerasRAK 1138
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPEL-----------------RNK 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1139 AEKQRSDLSRELEEISERlEEAGGATSAQIEMNKKREAEFQKMRRdLEEATLQHEataatlrKKHADSVAELgeQIDNLQ 1218
Cdd:TIGR00606 753 LQKVNRDIQRLKNDIEEQ-ETLLGTIMPEEESAKVCLTDVTIMER-FQMELKDVE-------RKIAQQAAKL--QGSDLD 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1219 RVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKT---------------------KEEEQQRLI 1277
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklqigtnlqrrqqfeeqlveLSTEVQSLI 901
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1278 NELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEE 1357
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNT 981
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1358 QEAK-AELQRAMSKANSEVAQWRTKYETDAIQ------------RTEELEEAKKKLAQRLQDAEEhveavnAKCASLEKT 1424
Cdd:TIGR00606 982 VNAQlEECEKHQEKINEDMRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELKQHLKEMGQ------MQVLQMKQE 1055
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1425 KQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWK-QKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLE 1503
Cdd:TIGR00606 1056 HQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQfRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFH 1135
|
....*...
gi 82524274 1504 TLKRENKN 1511
Cdd:TIGR00606 1136 SMKMEEIN 1143
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
851-1410 |
1.79e-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: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 851 ETEKEMANMKEEFEK---AKENLAKAEAKRK---ELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKI-QLE 923
Cdd:COG4913 222 DTFEAADALVEHFDDlerAHEALEDAREQIEllePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELeELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 924 AKIKEVTERAEDEEEINAELTAKKRKLEDECSELK-KDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKE 1002
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1003 KKALQEAHQQTLDDLQAEEDKVNT----LTKAKIKLEQQVDDLEG---SLEQEKK-IRMDLERAKRKLEGDLKLAQE--- 1071
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAeiaSLERRKSnIPARLLALRDALAEALGLDEAelp 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1072 ---------------------------------------------------------------STMDVENDKQQLDEKLK 1088
Cdd:COG4913 462 fvgelievrpeeerwrgaiervlggfaltllvppehyaaalrwvnrlhlrgrlvyervrtglpDPERPRLDPDSLAGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1089 KK--------EFEMSNLQS--KIEDEQALGmQLQKKI-KELQARIEELEEEIEAERASRAK------AEKQRSDLSRELE 1151
Cdd:COG4913 542 FKphpfrawlEAELGRRFDyvCVDSPEELR-RHPRAItRAGQVKGNGTRHEKDDRRRIRSRyvlgfdNRAKLAALEAELA 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1152 EISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEAtaatlrkkhADSVAELGEQIDNLQRVKQKLEkeksem 1231
Cdd:COG4913 621 ELEEELAEA----EERLEALEAELDALQERREALQRLAEYSWD---------EIDVASAEREIAELEAELERLD------ 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1232 kmeiddlASNMEViskskgnlekmcRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRG 1311
Cdd:COG4913 682 -------ASSDDL------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1312 KQAftQQIEELKRQLEEEIKAKSA--LAHALQSSRHDCDLLREQYEEeqeakaELQRAMSKANSE----VAQWRTKYET- 1384
Cdd:COG4913 743 ARL--ELRALLEERFAAALGDAVEreLRENLEERIDALRARLNRAEE------ELERAMRAFNREwpaeTADLDADLESl 814
|
650 660 670
....*....|....*....|....*....|..
gi 82524274 1385 ---DAI---QRTEELEEAKKKLAQRLQDAEEH 1410
Cdd:COG4913 815 peyLALldrLEEDGLPEYEERFKELLNENSIE 846
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
855-1800 |
2.30e-09 |
|
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: 63.15 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 855 EMANMkeEFEKAKENLAKAEAKRKELEEKMVALMQE-----KNDLQLQVQSEADSLADAEERCDQLIKTKIQL---EAKI 926
Cdd:TIGR01612 711 KIQNM--ETATVELHLSNIENKKNELLDIIVEIKKHihgeiNKDLNKILEDFKNKEKELSNKINDYAKEKDELnkyKSKI 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 927 KEVTERAEDEEEINAELTAKKRKLEDECSELKKDI----DDLELTLAKVEKEKHATENKV-------KNLTEEMAGLDET 995
Cdd:TIGR01612 789 SEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTIsikeDEIFKIINEMKFMKDDFLNKVdkfinfeNNCKEKIDSEHEQ 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 996 IAKLTKEKKAlqEAHQQTLDDLQAE----EDKVNTLTKAKIKLEQQVDDL----------EGSLEQEKKIRMDLERAKRK 1061
Cdd:TIGR01612 869 FAELTNKIKA--EISDDKLNDYEKKfndsKSLINEINKSIEEEYQNINTLkkvdeyikicENTKESIEKFHNKQNILKEI 946
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1062 LEGDLKLAQESTMDVENDKQQLDEKL--KKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASraKA 1139
Cdd:TIGR01612 947 LNKNIDTIKESNLIEKSYKDKFDNTLidKINELDKAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFD--EK 1024
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1140 EKQRSDLSRELEE------------------ISERLEEAGGATSAQIEMNKKREAE-----FQKMRRDLEEATLQHEATA 1196
Cdd:TIGR01612 1025 EKATNDIEQKIEDanknipnieiaihtsiynIIDEIEKEIGKNIELLNKEILEEAEinitnFNEIKEKLKHYNFDDFGKE 1104
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1197 ATLR-----KKHADSVAELGEQIDN----LQRVKQKLEKEKSEMKMEIDDL--ASNMEVISKSKGNLEKMCRTLEDQVSE 1265
Cdd:TIGR01612 1105 ENIKyadeiNKIKDDIKNLDQKIDHhikaLEEIKKKSENYIDEIKAQINDLedVADKAISNDDPEEIEKKIENIVTKIDK 1184
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1266 LKTKEEEQQRLINELTaqrgrlQTESGEYSrqLDEKDSLvsQLSRGK---QAFTQQIEELKRQLEEEIKAKSALAHALQS 1342
Cdd:TIGR01612 1185 KKNIYDEIKKLLNEIA------EIEKDKTS--LEEVKGI--NLSYGKnlgKLFLEKIDEEKKKSEHMIKAMEAYIEDLDE 1254
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1343 SRHDCDLLREQYEEEQEAKAELQ------------RAMSKANSE-VAQWRTKYE--TDAIQRTEELEEAKKKLAQRLQDA 1407
Cdd:TIGR01612 1255 IKEKSPEIENEMGIEMDIKAEMEtfnishdddkdhHIISKKHDEnISDIREKSLkiIEDFSEESDINDIKKELQKNLLDA 1334
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1408 EEHVEAVNAKCASLEKTKQRLQ--------NEVEDLMIDVERTNAAC-AALDKKQRNFDKI-----LAEWKQKYEETHAE 1473
Cdd:TIGR01612 1335 QKHNSDINLYLNEIANIYNILKlnkikkiiDEVKEYTKEIEENNKNIkDELDKSEKLIKKIkddinLEECKSKIESTLDD 1414
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1474 LEASQ-----KESRS--LSTE-----LFKIKNAYEESL--------------DHLETLKREN--KNLQQEISDLTEQIAE 1525
Cdd:TIGR01612 1415 KDIDEcikkiKELKNhiLSEEsnidtYFKNADENNENVlllfkniemadnksQHILKIKKDNatNDHDFNINELKEHIDK 1494
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1526 GGKRIHELEKIKKQIEQEKselqaaleEAEASLEHEEGKILRIQLELnQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQ 1605
Cdd:TIGR01612 1495 SKGCKDEADKNAKAIEKNK--------ELFEQYKKDVTELLNKYSAL-AIKNKFAKTKKDSEIIIKEIKDAHKKFILEAE 1565
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1606 STLDAEIRSRNDAIRLKKKMEGDlnemeiqlNHSNRMAAE---ALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVe 1682
Cdd:TIGR01612 1566 KSEQKIKEIKKEKFRIEDDAAKN--------DKSNKAAIDiqlSLENFENKFLKISDIKKKINDCLKETESIEKKISSF- 1636
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1683 rranllqaeieelraTLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKA 1762
Cdd:TIGR01612 1637 ---------------SIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGI 1701
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 82524274 1763 KKAITDAAMMAEElkkeqdtsaHLERMKKNLEQTVKDL 1800
Cdd:TIGR01612 1702 IEKIKEIAIANKE---------EIESIKELIEPTIENL 1730
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1318-1704 |
2.83e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 61.83 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1318 QIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEqeaKAELQRAMSKANSEVAQWRtkyetdaiQRTEELEEAK 1397
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQ---RRELESRVAELKEELRQSR--------EKHEELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1398 KKLAQRlqdAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEE---THAEL 1474
Cdd:pfam07888 104 KELSAS---SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAErkqLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1475 EASQKESRSLSTELFKIKNAYEESLDHLETlkrenknLQQEISDLTEQIAEGGKRIHELEKIKKqieqeksELQAALEEA 1554
Cdd:pfam07888 181 QQTEEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLE-------ELRSLQERL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1555 EASLEHEEGkilriqlelnqVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEI 1634
Cdd:pfam07888 247 NASERKVEG-----------LGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1635 QLNHSNRMAAEALRNYRNTQ-------------GILKDTQL-HLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLE 1700
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQeermereklevelGREKDCNRvQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIR 395
|
....
gi 82524274 1701 QTER 1704
Cdd:pfam07888 396 QLEQ 399
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1179-1922 |
3.02e-09 |
|
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: 62.55 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1179 QKMRRDLEEATLQHEATAATLRKKHadSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRT 1258
Cdd:pfam12128 217 RLNRQQVEHWIRDIQAIAGIMKIRP--EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRT 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1259 LEDQVSElktkeeeqqrLINELtaqRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAftqQIEELKRQLEEEIKAKSALah 1338
Cdd:pfam12128 295 LDDQWKE----------KRDEL---NGELSAADAAVAKDRSELEALEDQHGAFLDA---DIETAAADQEQLPSWQSEL-- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1339 ALQSSRHDCdLLREQYEEEQEAKAELQRAMSKANSEVAqwrtkyetDAIQRTEELEEAKKKLAQRLQDAEEHVEA----- 1413
Cdd:pfam12128 357 ENLEERLKA-LTGKHQDVTAKYNRRRSKIKEQNNRDIA--------GIKDKLAKIREARDRQLAVAEDDLQALESelreq 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1414 VNAKCASLEKTKQRLQNEVEDLMIdveRTNAACAALDKK--QRNFDKILaewkqkyEETHAELEASQKESRSLSTELFKI 1491
Cdd:pfam12128 428 LEAGKLEFNEEEYRLKSRLGELKL---RLNQATATPELLlqLENFDERI-------ERAREEQEAANAEVERLQSELRQA 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1492 KNAYEESLDHLETLKRENKNLQQEISDLTEQ-IAEGGKRIHEL--------EKIKKQIEQE---KSELQAALEEAEASle 1559
Cdd:pfam12128 498 RKRRDQASEALRQASRRLEERQSALDELELQlFPQAGTLLHFLrkeapdweQSIGKVISPEllhRTDLDPEVWDGSVG-- 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1560 hEEGKILRIQLELNQVkseidrKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEiqlnhs 1639
Cdd:pfam12128 576 -GELNLYGVKLDLKRI------DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREET------ 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1640 nrMAAEALRNYRNTQGILKDTQLHLDDALrgQEDLKEQLAMVERRANLLQaeieelratleqtersrkiAEQELLDASER 1719
Cdd:pfam12128 643 --FARTALKNARLDLRRLFDEKQSEKDKK--NKALAERKDSANERLNSLE-------------------AQLKQLDKKHQ 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1720 VQLLHTQNTSLINTKKKLETdISQIQGEM---EDIVQEARNAEEKAKKAITDA--AMMAEELKK---EQDTSAHLERMKK 1791
Cdd:pfam12128 700 AWLEEQKEQKREARTEKQAY-WQVVEGALdaqLALLKAAIAARRSGAKAELKAleTWYKRDLASlgvDPDVIAKLKREIR 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1792 NLEQTVKDLQHRLDEA---EQLALKGGKKQIQKLEARVRELEGEVENEQKRnveaikgLRKHERRVKELTYQTEEDRKNV 1868
Cdd:pfam12128 779 TLERKIERIAVRRQEVlryFDWYQETWLQRRPRLATQLSNIERAISELQQQ-------LARLIADTKLRRAKLEMERKAS 851
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 82524274 1869 LRLQDLVDKLQSKVKAYKRQAEEAEEQSNVNLAKFrKIQHELEEAEERADIAES 1922
Cdd:pfam12128 852 EKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQG-SIGERLAQLEDLKLKRDY 904
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
949-1540 |
3.11e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 62.23 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 949 KLEDECSELKKDIDDLELTLAK---VEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDD---LQAEED 1022
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNidyLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDynnLKSALN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1023 KVNTLTKAKIKLEQQVDDLEGSLEQEK----KIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKkefeMSNLQ 1098
Cdd:PRK01156 243 ELSSLEDMKNRYESEIKTAESDLSMELeknnYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQI----LSNID 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1099 SKIEDEQALgmqlQKKIKELQARIEELEeeieaerasraKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEF 1178
Cdd:PRK01156 319 AEINKYHAI----IKKLSVLQKDYNDYI-----------KKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYS 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1179 QKMRR---DLEEATLQHEATAATLRKKHAdsvaELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSkgNLEKM 1255
Cdd:PRK01156 384 KNIERmsaFISEILKIQEIDPDAIKKELN----EINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQ--SVCPV 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1256 CRTledqvselKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQqiEELKRQLEEEIKAKSA 1335
Cdd:PRK01156 458 CGT--------TLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKSINEYNKIESA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1336 lAHALQSSRHDCDLLREQYEEEQEAKAE--------LQRAMSKANSEVAQwRTKYETDAIQ-RTEELEEAKKKLAQRLQD 1406
Cdd:PRK01156 528 -RADLEDIKIKINELKDKHDKYEEIKNRykslkledLDSKRTSWLNALAV-ISLIDIETNRsRSNEIKKQLNDLESRLQE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1407 AEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEwKQKYEETHAELEASQKESrslST 1486
Cdd:PRK01156 606 IEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAE-IDSIIPDLKEITSRINDI---ED 681
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 82524274 1487 ELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQI 1540
Cdd:PRK01156 682 NLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
873-1216 |
3.21e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 873 AEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLiktkiqleAKIKEVTERAEDEEEINAELTAKKRKLEd 952
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL--------QRLAEYSWDEIDVASAEREIAELEAELE- 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 953 ecsELKKDIDDLEltlaKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKi 1032
Cdd:COG4913 679 ---RLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL- 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1033 kLEQQVDDLEGSlEQEKKIRMDLERAKRKLEGDLKLAQESTMDvendkqQLDEKLKKKEFEMSNLQSKIED--------- 1103
Cdd:COG4913 751 -LEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELER------AMRAFNREWPAETADLDADLESlpeylalld 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1104 ---EQALgMQLQKKIKELqarieeleeeieaerasRAKAEKQ-----RSDLSRELEEISERLEEA---------GGATSA 1166
Cdd:COG4913 823 rleEDGL-PEYEERFKEL-----------------LNENSIEfvadlLSKLRRAIREIKERIDPLndslkripfGPGRYL 884
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 82524274 1167 QIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDN 1216
Cdd:COG4913 885 RLEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1237-1593 |
4.23e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.90 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1237 DLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQ----RLINELTAQR-----GRLQTESGEYSRQLDEKdSLVSQ 1307
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQaasdHLNLVQTALRqqekiERYQADLEELEERLEEQ-NEVVE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1308 LSRGKQAftqQIEELKRQLEEEIK-AKSALAHALQSsrhdCDLLREQYEEEQEAKAELQRA------MSKANSEVAQWRT 1380
Cdd:PRK04863 373 EADEQQE---ENEARAEAAEEEVDeLKSQLADYQQA----LDVQQTRAIQYQQAVQALERAkqlcglPDLTADNAEDWLE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1381 KYETDAIQRTEELEEakkkLAQRLQDAEEHVEAVnAKCASLektkqrlqneVEDLMIDVERTNAACAALDK-KQRNFDKI 1459
Cdd:PRK04863 446 EFQAKEQEATEELLS----LEQKLSVAQAAHSQF-EQAYQL----------VRKIAGEVSRSEAWDVARELlRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1460 LAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQ 1539
Cdd:PRK04863 511 LAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82524274 1540 IEQEKSEL----------QAALE-------EAEASLEHEEGKILRIQL---ELNQVKSEIDRKIAEKDEEIDQL 1593
Cdd:PRK04863 591 LQARIQRLaarapawlaaQDALArlreqsgEEFEDSQDVTEYMQQLLErerELTVERDELAARKQALDEEIERL 664
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
925-1461 |
5.91e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.46 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 925 KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT---K 1001
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSsleD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1002 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDD--------------LEGSLEQEKKIRMDLERAKRKLEGDLK 1067
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDpvyknrnyindyfkYKNDIENKKQILSNIDAEINKYHAIIK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1068 LAQestmDVENDKQQLDEKLKKKE---FEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRS 1144
Cdd:PRK01156 330 KLS----VLQKDYNDYIKKKSRYDdlnNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1145 DLSRELEEISERLEE-AGGATSAQIEMNKKREAEfQKMRRDLEE----------ATLQHEATAATLRKKHADSVAELGEQ 1213
Cdd:PRK01156 406 AIKKELNEINVKLQDiSSKVSSLNQRIRALRENL-DELSRNMEMlngqsvcpvcGTTLGEEKSNHIINHYNEKKSRLEEK 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1214 IDNLQRVKQKLEKEKSEMKMEIDDLASnmEVISKSKGNLEKM------CRTLEDQVSELKTKEEEQQRLINELTAQR-GR 1286
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLES--EEINKSINEYNKIesaradLEDIKIKINELKDKHDKYEEIKNRYKSLKlED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1287 LQTESGEYSRQLDEKDSL-VSQLSRGKQAFTQQIEELKRQLEEEI----KAKSALAHALQSSRHDCDLLREQYEEEQEAK 1361
Cdd:PRK01156 563 LDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRLQEIEigfpDDKSYIDKSIREIENEANNLNNKYNEIQENK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1362 aelqRAMSKANSEVAQWRTKyetdaIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVER 1441
Cdd:PRK01156 643 ----ILIEKLRGKIDNYKKQ-----IAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINE 713
|
570 580
....*....|....*....|
gi 82524274 1442 TNAACAALDKKQRNFDKILA 1461
Cdd:PRK01156 714 LSDRINDINETLESMKKIKK 733
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1667-1896 |
8.11e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1667 ALRGQEDLKEQLamvERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQG 1746
Cdd:COG4942 14 AAAAQADAAAEA---EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1747 EMEDIVQEARNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNLEQTVKDLQHRLDE--AEQLALKGGKKQIQ 1820
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 1821 KLEARVRELEGEVENEQKRNVEAIKglrKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQS 1896
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1098-1344 |
8.19e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 8.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1098 QSKIEDEQALGMQLQKKIKELQARieeleeeieaerasRAKAEKQRSDLSRELEEISERLEeaggATSAQIemnKKREAE 1177
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKE--------------LAALKKEEKALLKQLAALERRIA----ALARRI---RALEQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1178 FQKMRRDLEEATLQHEAtaatLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCR 1257
Cdd:COG4942 78 LAALEAELAELEKEIAE----LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1258 TLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALA 1337
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*..
gi 82524274 1338 HALQSSR 1344
Cdd:COG4942 234 AEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1395-1595 |
8.48e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 8.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1395 EAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAEL 1474
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1475 EASQKESRSLSTELFKIKNA-----------YEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQE 1543
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 82524274 1544 KSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKR 1595
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1277-1723 |
1.19e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1277 INELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFtQQIEELKRQLEEEIKAKSALA--HALQSSRHDCDLLREQY 1354
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL-EELREELEKLEKLLQLLPLYQelEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1355 EEEQEAKAELQRAMSKANSEVAQWRTkyetdaiQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVED 1434
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQE-------ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1435 LMIDVERTNAACAALDKKQRnfdkiLAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEES---LDHLETLKRENKN 1511
Cdd:COG4717 225 LEEELEQLENELEAAALEER-----LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLgllALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1512 LQQEISDLteqiaEGGKRIHELEkiKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSeidrkiAEKDEEID 1591
Cdd:COG4717 300 LGKEAEEL-----QALPALEELE--EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE------LEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1592 QLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLnhsnrmaAEALRNYRNTQGILKDTQLHLDDalrgq 1671
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQL-------EELLGELEELLEALDEEELEEEL----- 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 82524274 1672 EDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAE--QELLDASERVQLL 1723
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEEDGELAEllQELEELKAELREL 488
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
987-1860 |
1.47e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 987 EEMAGLDETIAKLTKEK---KALQEAHQQTLDDLQAEEDkvnTLTKAKIKLEQQVDDLEGSL----------EQEKKIRM 1053
Cdd:PRK04863 279 NERRVHLEEALELRRELytsRRQLAAEQYRLVEMARELA---ELNEAESDLEQDYQAASDHLnlvqtalrqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1054 DLERAKRKLEGDL---KLAQESTMDVENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQarieeleeeie 1130
Cdd:PRK04863 356 DLEELEERLEEQNevvEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE----------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1131 aerasRAKAEKQRSDLsrELEEISERLEEAggATSAQIEMNKKREAEfQKMRrDLEEATLQHEATAATLRKkhadsvaeL 1210
Cdd:PRK04863 425 -----RAKQLCGLPDL--TADNAEDWLEEF--QAKEQEATEELLSLE-QKLS-VAQAAHSQFEQAYQLVRK--------I 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1211 GEQID--NLQRVKQKLEKEKSEMKMEIDDLA------SNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTA 1282
Cdd:PRK04863 486 AGEVSrsEAWDVARELLRRLREQRHLAEQLQqlrmrlSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1283 QRGRLQtesgEYSRQLDEKDSlvsQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHaLQSSRHDCDLLREQYEEEQEAKA 1362
Cdd:PRK04863 566 RLESLS----ESVSEARERRM---ALRQQLEQLQARIQRLAARAPAWLAAQDALAR-LREQSGEEFEDSQDVTEYMQQLL 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1363 ELQRAMSKANSEVAQwrtkyetdaiqRTEELEEAKKKLAQ-------RLQDAEEHVEAV--------------------- 1414
Cdd:PRK04863 638 ERERELTVERDELAA-----------RKQALDEEIERLSQpggsedpRLNALAERFGGVllseiyddvsledapyfsaly 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1415 -NAKCA----SLEKTKQRLQNEvEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEEthAELeasqKESRSLSTELF 1489
Cdd:PRK04863 707 gPARHAivvpDLSDAAEQLAGL-EDCPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIAD--RQW----RYSRFPEVPLF 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1490 KiKNAYEEsldHLETLkrenknlQQEISDLTEQIAEGGKRIHELEKIKKQI----------------EQEKSELQAALEE 1553
Cdd:PRK04863 780 G-RAAREK---RIEQL-------RAEREELAERYATLSFDVQKLQRLHQAFsrfigshlavafeadpEAELRQLNRRRVE 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1554 AEASLEHEEGKILRIQLELNQVKSEID--RKIAEkdeEIDQLKRNHI--RVVEsmqstLDAEIRSRNDAIRLKKKMEGDL 1629
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSalNRLLP---RLNLLADETLadRVEE-----IREQLDEAEEAKRFVQQHGNAL 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1630 NEMEIQLN--HSNRMAAEALR-NYRNTQGILKDTQLHLDDalrgqedLKEqlaMVERRA--------NLLQAE---IEEL 1695
Cdd:PRK04863 921 AQLEPIVSvlQSDPEQFEQLKqDYQQAQQTQRDAKQQAFA-------LTE---VVQRRAhfsyedaaEMLAKNsdlNEKL 990
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1696 RATLEQTERSRKIAEQELLDASERvqllHTQNT-------SLINTKKKLETDISQiqgEMEDI-VQEARNAEEKakkait 1767
Cdd:PRK04863 991 RQRLEQAEQERTRAREQLRQAQAQ----LAQYNqvlaslkSSYDAKRQMLQELKQ---ELQDLgVPADSGAEER------ 1057
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1768 dAAMMAEELKKEQDTSahleRMKKN-LEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVRELEGEVENEQKRNVEAIKG 1846
Cdd:PRK04863 1058 -ARARRDELHARLSAN----RSRRNqLEKQLTFCEAEMDNLT--------KKLRKLERDYHEMREQVVNAKAGWCAVLRL 1124
|
970
....*....|....*...
gi 82524274 1847 LRKH--ERRV--KELTYQ 1860
Cdd:PRK04863 1125 VKDNgvERRLhrRELAYL 1142
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1392-1935 |
1.77e-08 |
|
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: 59.98 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1392 ELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVE---RTNAACAALDKKQRNFDKILAEwKQKYE 1468
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAyltQKREAQEEQLKKQQLLKQLRAR-IEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1469 ETHAELEASQKEsRSLSTELFKIknayeesLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQ----IEQEK 1544
Cdd:TIGR00618 274 AQEAVLEETQER-INRARKAAPL-------AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQqssiEEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1545 SELQAALEEAEASLEHEEGKILRIQLElnQVKSEIDR-----KIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDai 1619
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAHEVATSIREISC--QQHTLTQHihtlqQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD-- 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1620 rlkkkMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVErraNLLQAEIE----EL 1695
Cdd:TIGR00618 422 -----LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE---QIHLQETRkkavVL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1696 RATLEQTERSRKIAEQELLDASERVQLLHTQNTS-----LINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAA 1770
Cdd:TIGR00618 494 ARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTrrmqrGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFS 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1771 MMAEelkKEQDTSAHLERMKkNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNVEAIKGLRKH 1850
Cdd:TIGR00618 574 ILTQ---CDNRSKEDIPNLQ-NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1851 eRRVKELTYQTEedrknvlRLQDLVDKLQSKVKAYKRQAEEAEEQSnvnlaKFRKIQHELEEAEERADIAESQVNKLRVK 1930
Cdd:TIGR00618 650 -ALQLTLTQERV-------REHALSIRVLPKELLASRQLALQKMQS-----EKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
....*
gi 82524274 1931 SREVH 1935
Cdd:TIGR00618 717 DREFN 721
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1394-1595 |
2.40e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1394 EEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAAcaaLDKKQRNFDKILAEWKQKYEETHAE 1473
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1474 LEASQKESRSLS--TELFKIKNaYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAAL 1551
Cdd:COG3883 92 ARALYRSGGSVSylDVLLGSES-FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 82524274 1552 EEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKR 1595
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
976-1206 |
2.57e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 976 HATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSL----EQEKKI 1051
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1052 RMDLERAKRKLEGDLKLAQEStmdveNDKQQLDEKLKKKEFE-----MSNLQSKIEDEQALGMQLQKKIKELQARIEELE 1126
Cdd:COG4942 96 RAELEAQKEELAELLRALYRL-----GRQPPLALLLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1127 EEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADS 1206
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARL----EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1671-1907 |
2.64e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.87 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1671 QEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKI--AEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEM 1748
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1749 EDIvQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNLEQTVKDLQHRLDEAEQLALKGGKKQ 1818
Cdd:COG3206 243 AAL-RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1819 IQKLEARVRELEGEVENEQKRnveaIKGLRKHERRVKELTYQTEEDRKNvlrLQDLVDKLQskvkaykrqaeEAEEQSNV 1898
Cdd:COG3206 322 LEALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVAREL---YESLLQRLE-----------EARLAEAL 383
|
....*....
gi 82524274 1899 NLAKFRKIQ 1907
Cdd:COG3206 384 TVGNVRVID 392
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1160-1420 |
2.83e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1160 AGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATlRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIddla 1239
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAEL---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1240 snmeviskskgnlekmcRTLEDQVSELKTKEEEQQRLINEL--TAQRGRLQTE-----SGEYSRQLDEKDSLVSQLSRGK 1312
Cdd:COG4942 86 -----------------AELEKEIAELRAELEAQKEELAELlrALYRLGRQPPlalllSPEDFLDAVRRLQYLKYLAPAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1313 QaftQQIEELKRQLEEEIKAKSALAHALQSsrhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAiQRTEE 1392
Cdd:COG4942 149 R---EQAEELRADLAELAALRAELEAERAE-------LEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAE 217
|
250 260
....*....|....*....|....*...
gi 82524274 1393 LEEAKKKLAQRLQDAEEHVEAVNAKCAS 1420
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1388-1834 |
3.71e-08 |
|
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: 58.16 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1388 QRTEELE-------EAKKKLAQ---RLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFD 1457
Cdd:pfam05622 14 QRCHELDqqvsllqEEKNSLQQenkKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1458 KILAEWKQKYEEthaeLEASQKESRSLSTELFKIKNA-------------YEESLDHLETLKRENKNLQQEISDLTEQIA 1524
Cdd:pfam05622 94 KEVLELQHRNEE----LTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAEYMQRTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1525 EGGKRIHELEKIKKQIEQEKSELQaaleEAEASLEHEEGKILRIQLELNQ-------VKSEIDRKIAEKD---EEIDQLK 1594
Cdd:pfam05622 170 QLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKleekleaLQKEKERLIIERDtlrETNEELR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1595 RNHIRVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQgiLKDTQLHLDDALRGQEDL 1674
Cdd:pfam05622 246 CAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRER--LTELQQLLEDANRRKNEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1675 KEQLAMVERRANLLQAEIEELRATLeqtersrkiaeqelldaservQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQE 1754
Cdd:pfam05622 324 ETQNRLANQRILELQQQVEELQKAL---------------------QEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1755 ARNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNLEQ---TVKDLQHRLDEAEQLALKGGKKQIQKLEARV 1826
Cdd:pfam05622 383 KEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPASPPEIQALKNQLLEKDKKI 462
|
....*...
gi 82524274 1827 RELEGEVE 1834
Cdd:pfam05622 463 EHLERDFE 470
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1008-1497 |
4.00e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1008 EAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQestmdVENDKQQLDEKL 1087
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-----LEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1088 KKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEEleeeieaeraSRAKAEKQRSDLSRELEEISERLEEAGGATSAQ 1167
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQ----------LSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1168 IEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEkseMKMEIDDLASNMEVISK 1247
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV---LFLVLGLLALLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1248 SKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRG-KQAFTQQIEELKRQL 1326
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELeEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1327 EEEIKAKS--ALAHALQssrhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAiqrteeleeakkkLAQRL 1404
Cdd:COG4717 376 LAEAGVEDeeELRAALE--------QAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-------------LEEEL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1405 QDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVErtnaacaaldkkqrnfdkiLAEWKQKYEETHAELEASQKESRSL 1484
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEEDGE-------------------LAELLQELEELKAELRELAEEWAAL 495
|
490
....*....|...
gi 82524274 1485 STELFKIKNAYEE 1497
Cdd:COG4717 496 KLALELLEEAREE 508
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
853-1616 |
4.98e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 58.52 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 853 EKEMANMKEEFEKA--KENLAKAEAKRKELEEKMVALMQ-----EKNDLQLQVQSEADSLADAEERCDQLIKT----KIQ 921
Cdd:TIGR01612 969 DNTLIDKINELDKAfkDASLNDYEAKNNELIKYFNDLKAnlgknKENMLYHQFDEKEKATNDIEQKIEDANKNipniEIA 1048
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 922 LEAKIKEVTERAEDEEEINAELTAKK--RKLEDECSELKKDIDDLEL----TLAKVEKEKHATE-NKVKNlteEMAGLDE 994
Cdd:TIGR01612 1049 IHTSIYNIIDEIEKEIGKNIELLNKEilEEAEINITNFNEIKEKLKHynfdDFGKEENIKYADEiNKIKD---DIKNLDQ 1125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 995 TIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIkleqQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTm 1074
Cdd:TIGR01612 1126 KIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAI----SNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIA- 1200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1075 DVENDK----------------------QQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELqARIEELEEEIEAE 1132
Cdd:TIGR01612 1201 EIEKDKtsleevkginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEM-GIEMDIKAEMETF 1279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1133 RASRAKAEKQRSDLSRELEEISERLEEaggatSAQIEMNKKREAEFQKMRRDLEEATLQHEataatlrkKHADSVAELGE 1212
Cdd:TIGR01612 1280 NISHDDDKDHHIISKKHDENISDIREK-----SLKIIEDFSEESDINDIKKELQKNLLDAQ--------KHNSDINLYLN 1346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1213 QIDNLQRVKQ--KLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVS--ELKTKEEEQ------QRLINELTA 1282
Cdd:TIGR01612 1347 EIANIYNILKlnKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINleECKSKIESTlddkdiDECIKKIKE 1426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1283 QRGRLQTESGE---YSRQLDEKDSLVSQLSRgkqaftqQIEELKRQLEEEIKAKSALAhalqSSRHDCDLlreqyeeeqe 1359
Cdd:TIGR01612 1427 LKNHILSEESNidtYFKNADENNENVLLLFK-------NIEMADNKSQHILKIKKDNA----TNDHDFNI---------- 1485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1360 akAELQRAMSKANsevaqwrtKYETDAIQRTEELEEAKKKLAQRLQDAEEHVE-----AVNAKCASLEKTKQRLQNEVED 1434
Cdd:TIGR01612 1486 --NELKEHIDKSK--------GCKDEADKNAKAIEKNKELFEQYKKDVTELLNkysalAIKNKFAKTKKDSEIIIKEIKD 1555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1435 LmidverTNAACAALDKKQRNFDKILAEwKQKYEETHAELEASQKES-------RSLSTELFKIKNAYEESLDHLetlkR 1507
Cdd:TIGR01612 1556 A------HKKFILEAEKSEQKIKEIKKE-KFRIEDDAAKNDKSNKAAidiqlslENFENKFLKISDIKKKINDCL----K 1624
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1508 ENKNLQQEISDLT-----EQIAEGGKRIHELEKIKKQIEQEKSELqaalEEAEASLEHEEGKILRIQLELNQVKSEIDRK 1582
Cdd:TIGR01612 1625 ETESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQKKNI----EDKKKELDELDSEIEKIEIDVDQHKKNYEIG 1700
|
810 820 830
....*....|....*....|....*....|....*
gi 82524274 1583 IAEKDEEIDQLKRNHIRVV-ESMQSTLDAEIRSRN 1616
Cdd:TIGR01612 1701 IIEKIKEIAIANKEEIESIkELIEPTIENLISSFN 1735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1069-1287 |
5.37e-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: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1069 AQESTMDVENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR 1148
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1149 ELEEISERLEE-----------------AGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELG 1211
Cdd:COG4942 98 ELEAQKEELAEllralyrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82524274 1212 EQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINE--LTAQRGRL 1287
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAagFAALKGKL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1537-1775 |
8.85e-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: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1537 KKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQvkseIDRKIAEKDEEIDQLkrnhirvvESMQSTLDAEIRSRN 1616
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRAL--------EQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1617 DAIrlkKKMEGDLNEMEIQLNhsnRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELR 1696
Cdd:COG4942 90 KEI---AELRAELEAQKEELA---ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 82524274 1697 ATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEE 1775
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
921-1301 |
9.35e-08 |
|
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: 56.83 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 921 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 1000
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1001 KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDK 1080
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1081 QQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSreleeiserlEEA 1160
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS----------SMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1161 GGATSAQIEMNKKReAEFQKMRRDLEEATLQ---HEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDD 1237
Cdd:pfam07888 265 AQRDRTQAELHQAR-LQAAQLTLQLADASLAlreGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREK 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 82524274 1238 LASNMEVISK-SKGNLEKMCRTLEDQVSELKTKEEEQQRLINEltaqrgrlQTESGEYSRQLDEK 1301
Cdd:pfam07888 344 LEVELGREKDcNRVQLSESRRELQELKASLRVAQKEKEQLQAE--------KQELLEYIRQLEQR 400
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1169-1883 |
1.08e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 57.37 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1169 EMNKKREAEFQKMRrDLEEATLQ-HEATAATLRKKHADSVAEL-----GEQIDNLQRVKQKLEKEKSEMKMEIDDLASNM 1242
Cdd:TIGR01612 700 DLKSKIDKEYDKIQ-NMETATVElHLSNIENKKNELLDIIVEIkkhihGEINKDLNKILEDFKNKEKELSNKINDYAKEK 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1243 EVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINeltaqrgrlqtESGEYSRQLDEKDSLVSQLsrgkqaftqqIEEL 1322
Cdd:TIGR01612 779 DELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYD-----------KSKEYIKTISIKEDEIFKI----------INEM 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1323 KrQLEEEIKAKSALAHALQSSRhdcdllREQYEEEQEAKAELqraMSKANSEVAQWR-TKYETDAIQRTEELEEAKKKLA 1401
Cdd:TIGR01612 838 K-FMKDDFLNKVDKFINFENNC------KEKIDSEHEQFAEL---TNKIKAEISDDKlNDYEKKFNDSKSLINEINKSIE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1402 QRLQD------AEEHVEAVNAKCASLEK--TKQRLQNEVEDLMIDV-ERTNaacaALDKKQRN-FDKILAEWKQKYEETH 1471
Cdd:TIGR01612 908 EEYQNintlkkVDEYIKICENTKESIEKfhNKQNILKEILNKNIDTiKESN----LIEKSYKDkFDNTLIDKINELDKAF 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1472 AELEASQKESRslSTELFKIKNAYEESL---------DHLETLKRENKNLQQEISDLTEQIAEGGKRIH--------ELE 1534
Cdd:TIGR01612 984 KDASLNDYEAK--NNELIKYFNDLKANLgknkenmlyHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHtsiyniidEIE 1061
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1535 K-IKKQIEQEKSELqaaLEEAEASLEHEEGkiLRIQLELNQVKSEIDRKIAEKDEEIDQLKRNhirvVESMQSTLDAEIr 1613
Cdd:TIGR01612 1062 KeIGKNIELLNKEI---LEEAEINITNFNE--IKEKLKHYNFDDFGKEENIKYADEINKIKDD----IKNLDQKIDHHI- 1131
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1614 srNDAIRLKKKMEGDLNEMEIQLNHSNRMAAEALRNyRNTQGILKDTQlhlddalrgqedlkEQLAMVERRANLLQaEIE 1693
Cdd:TIGR01612 1132 --KALEEIKKKSENYIDEIKAQINDLEDVADKAISN-DDPEEIEKKIE--------------NIVTKIDKKKNIYD-EIK 1193
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1694 ELRATLEQTERsrkiaEQELLDASERVQLLHTQNTSLI------NTKKKLETDISQIQGEMEDI--VQEARNAEEKAKKA 1765
Cdd:TIGR01612 1194 KLLNEIAEIEK-----DKTSLEEVKGINLSYGKNLGKLflekidEEKKKSEHMIKAMEAYIEDLdeIKEKSPEIENEMGI 1268
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1766 ITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRL-----DEAEQLALKGGKKQIQKLEARVRELEGEV-----EN 1835
Cdd:TIGR01612 1269 EMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSlkiieDFSEESDINDIKKELQKNLLDAQKHNSDInlylnEI 1348
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 82524274 1836 EQKRNVEAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVK 1883
Cdd:TIGR01612 1349 ANIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIK 1396
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1439-1887 |
1.09e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1439 VERTNAACAALDKKQRNFDKILAEwKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDhLETLKRENKNLQQEISD 1518
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1519 LTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHI 1598
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1599 RVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHSNRMAAEALrnyrntQGILKDTQLHLDDALRGQEDLKEQL 1678
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL------FLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1679 AMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLEtdISQIQGEMEDIVQEARNA 1758
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1759 EEKakkaitDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALkggKKQIQKLEARVRELEGEVENEQK 1838
Cdd:COG4717 383 DEE------ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL---EEELEELEEELEELEEELEELRE 453
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 82524274 1839 RnveaikgLRKHERRVKELTYQTEEDRKNvLRLQDLVDKLQSKVKAYKR 1887
Cdd:COG4717 454 E-------LAELEAELEQLEEDGELAELL-QELEELKAELRELAEEWAA 494
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1502-1936 |
1.27e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 56.75 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1502 LETL--KRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALE-EAEASLEHEEGKILRIQLELNQVK-S 1577
Cdd:pfam10174 164 LEMLqsKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHrRNQLQPDPAKTKALQTVIEMKDTKiS 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1578 EIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKME---GDLNEMEIQLnHSNRMAAEALRNYRNtq 1654
Cdd:pfam10174 244 SLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDqlkQELSKKESEL-LALQTKLETLTNQNS-- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1655 gilkDTQLHLddalrgqEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTK 1734
Cdd:pfam10174 321 ----DCKQHI-------EVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1735 KKLETDISQIQGEMEDIVQEARNAE-------EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNL-EQTVKDLQHRLDE 1806
Cdd:pfam10174 390 DVKERKINVLQKKIENLQEQLRDKDkqlaglkERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1807 AEQL--ALKGGKKQIQKLEARVRELEGEVENEQKRNVEAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQskvka 1884
Cdd:pfam10174 470 LESLkkENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH----- 544
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 82524274 1885 ykrQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHT 1936
Cdd:pfam10174 545 ---NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVEN 593
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1465-1704 |
1.46e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1465 QKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEK 1544
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1545 SELQAALEEAEASLeHEEGKILRIQLELNQVKSEidrKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKK 1624
Cdd:COG4942 100 EAQKEELAELLRAL-YRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1625 MEGDLNEMEIQlnhsnRMAAEALRNYRNTQgilkdtqlhLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTER 1704
Cdd:COG4942 176 LEALLAELEEE-----RAALEALKAERQKL---------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
658-682 |
1.67e-07 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 53.12 E-value: 1.67e-07
10 20
....*....|....*....|....*
gi 82524274 658 FRENLNKLMTNLRSTHPHFVRCIIP 682
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1496-1694 |
2.13e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 56.02 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1496 EESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKikkqieqEKSELQAALEEAEASLEHEEGKILRIQLELNQv 1575
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-------EVEELEAELEEKDERIERLERELSEARSEERR- 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1576 KSEIDRKIAEKDEEIDQLKrnhiRVVESMQSTLDaEIRSRNDaiRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQG 1655
Cdd:COG2433 460 EIRKDREISRLDREIERLE----RELEEERERIE-ELKRKLE--RLKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYG 532
|
170 180 190
....*....|....*....|....*....|....*....
gi 82524274 1656 ILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEE 1694
Cdd:COG2433 533 LKEGDVVYLRDASGAGRSTAELLAEAGPRAVIVPGELSE 571
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
917-1247 |
2.87e-07 |
|
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: 55.53 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 917 KTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDD-LELTLAKVEK----EKHATENKVKNLTEEMAG 991
Cdd:pfam09731 86 KKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEvLKEAISKAESatavAKEAKDDAIQAVKAHTDS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 992 LDETIAklTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDL-EGSLEQEKKIRMDLERAKRKLEGDLKLAQ 1070
Cdd:pfam09731 166 LKEASD--TAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLlDAAPETPPKLPEHLDNVEEKVEKAQSLAK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1071 ---ESTMDVENDKQQLDEKLKKKE------------FEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEaeras 1135
Cdd:pfam09731 244 lvdQYKELVASERIVFQQELVSIFpdiipvlkednlLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERAL----- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1136 rakaEKQRSDLSRELEEISERLEEAGGATSAQIEmnKKREAEFQKMRRDLEE---ATLQHEATAATLRKKHADSVAELGE 1212
Cdd:pfam09731 319 ----EKQKEELDKLAEELSARLEEVRAADEAQLR--LEFEREREEIRESYEEklrTELERQAEAHEEHLKDVLVEQEIEL 392
|
330 340 350
....*....|....*....|....*....|....*
gi 82524274 1213 QIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISK 1247
Cdd:pfam09731 393 QREFLQDIKEKVEEERAGRLLKLNELLANLKGLEK 427
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1204-1448 |
3.04e-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: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1204 ADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELktkEEEQQRLINELTAQ 1283
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1284 RGRLQTESGEYSRQLDeKDSLVSQLSRGKQAFTQQieelkrQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAE 1363
Cdd:COG4942 96 RAELEAQKEELAELLR-ALYRLGRQPPLALLLSPE------DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1364 LQRAMSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTN 1443
Cdd:COG4942 169 LEAERAELEALLAE--------LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
....*
gi 82524274 1444 AACAA 1448
Cdd:COG4942 241 ERTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
936-1367 |
3.66e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 936 EEEINAELTAKKRKLEDECSELKKDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKAL--QEAHQQT 1013
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1014 LDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEgdlKLAQESTMDVENDKQQLDEKLKKKEFE 1093
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE---ELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1094 MSNLQSKIEdeqalgmQLQKKIKELQARIEELEEEIEAERASRAKAEKQRS--------DLSRELEEISERLEEAGGATS 1165
Cdd:COG4717 208 LAELEEELE-------EAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1166 AQIEM-----------NKKREAEFQKMRRDLEEATLQHEATAATLRKKH------ADSVAELGEQIDNLQRVKQKLEKEK 1228
Cdd:COG4717 281 LVLGLlallflllareKASLGKEAEELQALPALEELEEEELEELLAALGlppdlsPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1229 SEmkMEIDDLASNMEVIskskgnLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSlvSQL 1308
Cdd:COG4717 361 EE--LQLEELEQEIAAL------LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EEL 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 82524274 1309 SRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDcDLLREQYEEEQEAKAELQRA 1367
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELREL 488
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
850-1553 |
4.00e-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: 55.61 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 850 AETEKEMANMKEEFEKAKENLakaEAKRKELEEKMVALMQEKNDLQLQVQSE-ADSLADAEERCDQLIKTKIQLEAKIKE 928
Cdd:pfam12128 339 IETAAADQEQLPSWQSELENL---EERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAED 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 929 VTERAEdeEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKvKNLTEEMAGLDETIAKLTKEKKALQE 1008
Cdd:pfam12128 416 DLQALE--SELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQL-ENFDERIERAREEQEAANAEVERLQS 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1009 -------AHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSL-EQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDK 1080
Cdd:pfam12128 493 elrqarkRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDG 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1081 QQLDE------KLKKKEFEMSnlqSKIEDEQALGMQLQKKIKELQARIEeleeeieaeraSRAKAEKQRSDLSRELEEIS 1154
Cdd:pfam12128 573 SVGGElnlygvKLDLKRIDVP---EWAASEEELRERLDKAEEALQSARE-----------KQAAAEEQLVQANGELEKAS 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1155 ERLEEAGGAtsaqiemnkkreaeFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKME 1234
Cdd:pfam12128 639 REETFARTA--------------LKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEE 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1235 IDDLASnmEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQrlinelTAQRGRLQTESGEYSRQLDEKD---SLVSQLSRG 1311
Cdd:pfam12128 705 QKEQKR--EARTEKQAYWQVVEGALDAQLALLKAAIAARR------SGAKAELKALETWYKRDLASLGvdpDVIAKLKRE 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1312 KQAFTQQIEELKRQLEEEIKAKSALAHALQSSRhdcDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYET------D 1385
Cdd:pfam12128 777 IRTLERKIERIAVRRQEVLRYFDWYQETWLQRR---PRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMerkaseK 853
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1386 AIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQrlqneVEDLMIDVERtnaACAALDKKQRNFDKILAewKQ 1465
Cdd:pfam12128 854 QQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQ-----LEDLKLKRDY---LSESVKKYVEHFKNVIA--DH 923
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1466 KYEETHAELEASQKESRSLSTELFKIKNaYEESLDHLETLKreNKNLQQEISDLTEQIAEGGKRIHE----LEKIKKQIE 1541
Cdd:pfam12128 924 SGSGLAETWESLREEDHYQNDKGIRLLD-YRKLVPYLEQWF--DVRVPQSIMVLREQVSILGVDLTEfydvLADFDRRIA 1000
|
730
....*....|..
gi 82524274 1542 QEKSELQAALEE 1553
Cdd:pfam12128 1001 SFSRELQREVGE 1012
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
859-1300 |
4.00e-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: 55.21 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 859 MKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLiktkiqlEAKIKEVTERAEDEEE 938
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL-------QTEVDALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 939 INAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQ------ 1012
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalt 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1013 TLDDLQAEEDKVNTLTKAKIKLEQQVDDLEgsLEQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKKEF 1092
Cdd:pfam10174 440 TLEEALSEKERIIERLKEQREREDRERLEE--LESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDS 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1093 EMS----NLQSKIEDEQALGMQLQKkikelqarieeleeEIEAERASRAKAEkqRSDLSRELEEISERLEEAGGATSAQI 1168
Cdd:pfam10174 518 KLKsleiAVEQKKEECSKLENQLKK--------------AHNAEEAVRTNPE--INDRIRLLEQEVARYKEESGKAQAEV 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1169 E--MNKKREAEFQKMRRDLEEATLqhEATAATLRKKHADSVAELgeqidnlqRVKQKLEKEKSEMKMEIDDLASNMEVIS 1246
Cdd:pfam10174 582 ErlLGILREVENEKNDKDKKIAEL--ESLTLRQMKEQNKKVANI--------KHGQQEMKKKGAQLLEEARRREDNLADN 651
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 82524274 1247 KSKGNLEKMCRTLEDQVSELktkEEEQQRLIN---ELTAQRGRLQTESGEYSRQLDE 1300
Cdd:pfam10174 652 SQQLQLEELMGALEKTRQEL---DATKARLSStqqSLAEKDGHLTNLRAERRKQLEE 705
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1682-1941 |
4.39e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1682 ERRANL--LQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAE 1759
Cdd:PRK02224 248 ERREELetLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1760 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELEGEVEN--EQ 1837
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE-AVEDRREEIEELEEEIEELRERFGDapVD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1838 KRNVEAIKGLRKHER-----RVKELTYQTEEDRKNVLRLQDLVDKLQ--------------SKVKAYKRQAEEAEEQsnv 1898
Cdd:PRK02224 407 LGNAEDFLEELREERdelreREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAE--- 483
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 82524274 1899 nLAKFRKIQHELEEAEERADI---AESQVNKLRVKsREVHTKIISE 1941
Cdd:PRK02224 484 -LEDLEEEVEEVEERLERAEDlveAEDRIERLEER-REDLEELIAE 527
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1488-1934 |
4.58e-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: 54.86 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1488 LFKIKNAYEEsLDHLETLKRE--NKNLQQEISDLtEQIAEGGKRIHELEKIKKQ----IEQEKSELQAALEEAEASLEhe 1561
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1562 EGKILRIQLELNQVKS---EIDRKIAEKDEEIDQLK------RNHIRVVESMQSTLDAEIRSRNDAI-RLKKKMEGDLNE 1631
Cdd:pfam06160 78 KYRFKKAKKALDEIEElldDIEEDIKQILEELDELLeseeknREEVEELKDKYRELRKTLLANRFSYgPAIDELEKQLAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1632 MEIQLNH-SNRMAAEalrNYRNTQGILKDTQLHLDDAlrgQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAE 1710
Cdd:pfam06160 158 IEEEFSQfEELTESG---DYLEAREVLEKLEEETDAL---EELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1711 QelLDASERVQLLHTQNTSLINTKKKLETD-----ISQIQGEMEDIvQEARNAEEKAKKaitdaammaeELKKEQDT-SA 1784
Cdd:pfam06160 232 H--LNVDKEIQQLEEQLEENLALLENLELDeaeeaLEEIEERIDQL-YDLLEKEVDAKK----------YVEKNLPEiED 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1785 HLERMKKNLEQTVKDLQH-----RLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNV-------EAIKGLRKHER 1852
Cdd:pfam06160 299 YLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSelqeeleEILEQLEEIEE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1853 RVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAE----------------EAEEQSNVNLAKFRKIQHELEEAEER 1916
Cdd:pfam06160 379 EQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEksnlpglpesyldyffDVSDEIEDLADELNEVPLNMDEVNRL 458
|
490
....*....|....*...
gi 82524274 1917 ADIAESQVNKLRVKSREV 1934
Cdd:pfam06160 459 LDEAQDDVDTLYEKTEEL 476
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1458-1702 |
6.36e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1458 KILAEWKQKYEETHAEL--EASQKESRSLSTELFKIKNAYEESLDHLETLKRENK--NLQQEISDLTEQIAEggkriheL 1533
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE-------L 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1534 EKIKKQIEQEKSELQAALEEAEASLEHEEGKI--LRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVEsmqstLDAE 1611
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA-----LRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1612 IRSrndairLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAE 1691
Cdd:COG3206 300 IAA------LRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQR 373
|
250
....*....|.
gi 82524274 1692 IEELRATLEQT 1702
Cdd:COG3206 374 LEEARLAEALT 384
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1135-1337 |
6.79e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1135 SRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAEFQKMRRDLEEATLQHEATAATLRKKHADsVAELGEQI 1214
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAA--------------QAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1215 DNLQrvkQKLEKEKSEMKM----------------------EIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEE 1272
Cdd:COG3883 75 AEAE---AEIEERREELGEraralyrsggsvsyldvllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 82524274 1273 QQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALA 1337
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
854-1615 |
8.77e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 854 KEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKiQLEAKIKEVTERA 933
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIE-RYQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 934 EDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKekhatenkvknlteemaGLD--ETIA-KLTKEKKALQEAH 1010
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQ-----------------ALDvqQTRAiQYQQAVQALERAK 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1011 QQT-LDDLQAE--EDKVNTLtKAKiklEQQVDDLEGSLEQekkiRMDL-ERAKRKLEGDLKLAQESTMDVenDKQQLDEK 1086
Cdd:PRK04863 428 QLCgLPDLTADnaEDWLEEF-QAK---EQEATEELLSLEQ----KLSVaQAAHSQFEQAYQLVRKIAGEV--SRSEAWDV 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1087 LKKKEFEMSNLQSKIEDEQALGMQLqkkiKELQARIEELEEEIeaerasRAKAE-KQRSDLSRELEEISERLEEAGGATS 1165
Cdd:PRK04863 498 ARELLRRLREQRHLAEQLQQLRMRL----SELEQRLRQQQRAE------RLLAEfCKRLGKNLDDEDELEQLQEELEARL 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1166 AQIEMNKKREAEFQ-KMRRDLEEATLQHEATAATLRKKHA--DSVAELGEQ----IDNLQRV----KQKLEKEKsEMKME 1234
Cdd:PRK04863 568 ESLSESVSEARERRmALRQQLEQLQARIQRLAARAPAWLAaqDALARLREQsgeeFEDSQDVteymQQLLERER-ELTVE 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1235 IDDLASNMEVI--------SKSKGNLEKMcRTLEDQ-----VSELK---TKEE-----------EQQRLINELTAQRGRL 1287
Cdd:PRK04863 647 RDELAARKQALdeeierlsQPGGSEDPRL-NALAERfggvlLSEIYddvSLEDapyfsalygpaRHAIVVPDLSDAAEQL 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1288 QTE------------------SGEYSRQLDEKDSLV------SQLSR-------GKQAFTQQIEELKRQLEEEIKAKSAL 1336
Cdd:PRK04863 726 AGLedcpedlyliegdpdsfdDSVFSVEELEKAVVVkiadrqWRYSRfpevplfGRAAREKRIEQLRAEREELAERYATL 805
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1337 AHALQssrhDCDLLREQYE-------------EEQEAKAELQRAMSKANSEVAQwrtkyetdaiqrteeLEEAKKKLAQR 1403
Cdd:PRK04863 806 SFDVQ----KLQRLHQAFSrfigshlavafeaDPEAELRQLNRRRVELERALAD---------------HESQEQQQRSQ 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1404 LQDAEEHVEAVNaKCASLEKTKQR--LQNEVEDLMIDVERTNAACAALDKKQRNFDKI-------------LAEWKQKYE 1468
Cdd:PRK04863 867 LEQAKEGLSALN-RLLPRLNLLADetLADRVEEIREQLDEAEEAKRFVQQHGNALAQLepivsvlqsdpeqFEQLKQDYQ 945
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1469 ETHAELEASQKESRSLsTELFKIKN--AYEESLDHLEtlkrenknlqqEISDLTEQIAEggkRIhelekikKQIEQEKSE 1546
Cdd:PRK04863 946 QAQQTQRDAKQQAFAL-TEVVQRRAhfSYEDAAEMLA-----------KNSDLNEKLRQ---RL-------EQAEQERTR 1003
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 82524274 1547 LQAALEEAEAslEHEEGKILRIQLelnqvKSEIDRK---IAEKDEEIDQLkrnhirvveSMQSTLDAEIRSR 1615
Cdd:PRK04863 1004 AREQLRQAQA--QLAQYNQVLASL-----KSSYDAKrqmLQELKQELQDL---------GVPADSGAEERAR 1059
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
846-1073 |
9.47e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 846 LLKSAETEKEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAK 925
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 926 IKEVTERAEDEEEINAELTAKKRKLEDEcSELK-----KDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 1000
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQ-PPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 82524274 1001 KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQEST 1073
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
853-1106 |
1.06e-06 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 53.70 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 853 EKEMANMKEEFEKAKENlakAEAKRKELEEKMVALMQE--------------KNDLQ-LQVQSEADSLADAEERCDQLik 917
Cdd:PLN03229 485 QERLENLREEFSKANSQ---DQLMHPVLMEKIEKLKDEfnkrlsrapnylslKYKLDmLNEFSRAKALSEKKSKAEKL-- 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 918 tKIQLEAKIKEVTERAEDEEEINAeltakkRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMaGLDETIA 997
Cdd:PLN03229 560 -KAEINKKFKEVMDRPEIKEKMEA------LKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSM-GLEVIGV 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 998 KltkeKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKkirmdLERAKRKLEGDLKLAQEstmdVE 1077
Cdd:PLN03229 632 T----KKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSKIELLK-----LEVAKASKTPDVTEKEK----IE 698
|
250 260
....*....|....*....|....*....
gi 82524274 1078 NDKQQLDEKLKKKeFEMSNLQSKIEDEQA 1106
Cdd:PLN03229 699 ALEQQIKQKIAEA-LNSSELKEKFEELEA 726
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
870-1024 |
1.09e-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: 51.85 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 870 LAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKIKEVTER-AEDEEEINAELTAKKR 948
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARiKKYEEQLGNVRNNKEY 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 82524274 949 K-LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKV 1024
Cdd:COG1579 92 EaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
852-1323 |
1.12e-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: 53.96 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 852 TEKEMANMkEEFEKAKEN----LAKAEAKRKELEEKMVALMQ--EKNDLQLQVQSEadSLADAEERCDQLIKTKIQLEAK 925
Cdd:pfam05483 330 TEEKEAQM-EELNKAKAAhsfvVTEFEATTCSLEELLRTEQQrlEKNEDQLKIITM--ELQKKSSELEEMTKFKNNKEVE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 926 IKEV-TERAEDE---------EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDET 995
Cdd:pfam05483 407 LEELkKILAEDEklldekkqfEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLK 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 996 IAKLT--------KEKKALQEAHQQTLDdLQAEEDKVNTLTKAKIKLEQQVDDLEgslEQEKKIRMDLERAKRKL--EGD 1065
Cdd:pfam05483 487 NIELTahcdklllENKELTQEASDMTLE-LKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFiqKGD 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1066 -----LKLAQESTMDVENDKQQLDEKLKKKEFEMSNLQSKIEDEQalgmqlqKKIKELQARIEELEEEIEAERASRAKAE 1140
Cdd:pfam05483 563 evkckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-------KNIEELHQENKALKKKGSAENKQLNAYE 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1141 KQRSDLSRELEEISERLEEAGGATSAQIEMNKKREaefQKMRRDLEEAtlqheataatlrKKHADSVAELGEQIDnlQRV 1220
Cdd:pfam05483 636 IKVNKLELELASAKQKFEEIIDNYQKEIEDKKISE---EKLLEEVEKA------------KAIADEAVKLQKEID--KRC 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1221 KQKlekeksemkmeiddLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDE 1300
Cdd:pfam05483 699 QHK--------------IAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEI 764
|
490 500
....*....|....*....|...
gi 82524274 1301 KDSLVSQLSRGKQAFTQQIEELK 1323
Cdd:pfam05483 765 EKEEKEKLKMEAKENTAILKDKK 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1257-1498 |
1.22e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1257 RTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSAL 1336
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1337 AHALQssrhdcDLLREQYEEEQEAKAELqrAMSKANSEVAQWRTKYETDAIQ----RTEELEEAKKKLAQRLQDAEEHVE 1412
Cdd:COG4942 103 KEELA------ELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAParreQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1413 AVNAKCASLEKTKQRLQNEvedlmidvertnaacaaldKKQRNfdKILAEWKQKYEETHAELEASQKESRSLSTELFKIK 1492
Cdd:COG4942 175 ELEALLAELEEERAALEAL-------------------KAERQ--KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*.
gi 82524274 1493 NAYEES 1498
Cdd:COG4942 234 AEAAAA 239
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1579-1922 |
1.62e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 53.37 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1579 IDRKIAEKDEEIDQLKRNHIRVVESM--QSTLDAEIRSRNDAIRLKKKMEGDLNEMEiqlnhsNRMAAEALRNYR--NTQ 1654
Cdd:PLN02939 61 SNSKLQSNTDENGQLENTSLRTVMELpqKSTSSDDDHNRASMQRDEAIAAIDNEQQT------NSKDGEQLSDFQleDLV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1655 GILKDTQ---LHLDDA-LRGQEDLKEQLAmvERRAnlLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSL 1730
Cdd:PLN02939 135 GMIQNAEkniLLLNQArLQALEDLEKILT--EKEA--LQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNEL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1731 INTKKKLETDISQIQGEMEDIVQEarNAEEKAkkaitDAAMMAEELKKEQDTS---AHLERMKKNLEQTVKDLQHRLDEA 1807
Cdd:PLN02939 211 LIRGATEGLCVHSLSKELDVLKEE--NMLLKD-----DIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1808 EQLALKGGKKQIQKLEARVRELEGEVENEQKRNVEAIKGLRKH---ERRVKELTYQTEEdrKNVLRLQ-DLVDKLQSKVK 1883
Cdd:PLN02939 284 QEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNqdlRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLK 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 82524274 1884 AYKR--QAEEAEEQSNVNL-----AKFRKIQHELEEAEERADIAES 1922
Cdd:PLN02939 362 LLEErlQASDHEIHSYIQLyqesiKEFQDTLSKLKEESKKRSLEHP 407
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1135-1935 |
1.64e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.51 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1135 SRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATlqHEATAATLRKKHADSVAELGEQI 1214
Cdd:TIGR00606 166 SEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKAC--EIRDQITSKEAQLESSREIVKSY 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1215 DNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQqrlINELTAQRGRLQTESGEY 1294
Cdd:TIGR00606 244 ENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ---LNDLYHNHQRTVREKERE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1295 ----SRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLE---EEIKAKSALAHALQSSRHDCDLLREQYEEEQ-----EAKA 1362
Cdd:TIGR00606 321 lvdcQRELEKLNKERRLLNQEKTELLVEQGRLQLQADrhqEHIRARDSLIQSLATRLELDGFERGPFSERQiknfhTLVI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1363 ELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERT 1442
Cdd:TIGR00606 401 ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1443 NAACAALDKKQRNfdkILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQ 1522
Cdd:TIGR00606 481 RKAERELSKAEKN---SLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1523 IAEG--------------GKRIHELEKIKKQIEQEKSELQAALEEAEasleheegkilriqlelnQVKSEIDRKIAEKDE 1588
Cdd:TIGR00606 558 HSDEltsllgyfpnkkqlEDWLHSKSKEINQTRDRLAKLNKELASLE------------------QNKNHINNELESKEE 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1589 EIDQLKRNHIRVVESMQSTLDAEirsrndaiRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQlhldDAL 1668
Cdd:TIGR00606 620 QLSSYEDKLFDVCGSQDEESDLE--------RLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQ----RVF 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1669 RGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEM 1748
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1749 E--DIVQEARNAEEK-AKKAITDAAMMaeelkkeQDTSAHLERMKKNLEQTVKDLQhrlDEAEQLALKGGKKQIQKLEAR 1825
Cdd:TIGR00606 768 EeqETLLGTIMPEEEsAKVCLTDVTIM-------ERFQMELKDVERKIAQQAAKLQ---GSDLDRTVQQVNQEKQEKQHE 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1826 VRELEGEVENEQKRNVEAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYK---RQAEEAEEQSNVNLAK 1902
Cdd:TIGR00606 838 LDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQsliREIKDAKEQDSPLETF 917
|
810 820 830
....*....|....*....|....*....|....*..
gi 82524274 1903 FRKIQHELEEA----EERADIAESQVNKLRVKSREVH 1935
Cdd:TIGR00606 918 LEKDQQEKEELisskETSNKKAQDKVNDIKEKVKNIH 954
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
860-1435 |
1.69e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 860 KEEFEKAKENLAKAEaKRKELEEKMVALMQEKNDLQLQVQSEADS---LADAEERCDQLIKTKIQLEAKIKEVTERAEDE 936
Cdd:PRK04863 492 SEAWDVARELLRRLR-EQRHLAEQLQQLRMRLSELEQRLRQQQRAerlLAEFCKRLGKNLDDEDELEQLQEELEARLESL 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 937 EEINAELTAKKRKLEDECSELKKDIDdlelTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTkekkalqEAHQQTLDD 1016
Cdd:PRK04863 571 SESVSEARERRMALRQQLEQLQARIQ----RLAARAPAWLAAQDALARLREQSGEEFEDSQDVT-------EYMQQLLER 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1017 LQAEEDKVNTLTKAKIKLEQQVDDL---EGSlEQEKKIRM--------------------------------------DL 1055
Cdd:PRK04863 640 ERELTVERDELAARKQALDEEIERLsqpGGS-EDPRLNALaerfggvllseiyddvsledapyfsalygparhaivvpDL 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1056 ERAKRKLEG------DLKLaqestmdVENDKQQLDEK-LKKKEFE------MSNLQ---SKIEDEQALGmqlqkkikelq 1119
Cdd:PRK04863 719 SDAAEQLAGledcpeDLYL-------IEGDPDSFDDSvFSVEELEkavvvkIADRQwrySRFPEVPLFG----------- 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1120 arieeleeeieaerasRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAEFQKMRR---DLEEATLQH---- 1192
Cdd:PRK04863 781 ----------------RAAREKRIEQLRAEREELAERYATL--------------SFDVQKLQRlhqAFSRFIGSHlava 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1193 -----EATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMeIDDLASNMEVISKSkgNLEKMCRTLEDQVSELK 1267
Cdd:PRK04863 831 feadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSA-LNRLLPRLNLLADE--TLADRVEEIREQLDEAE 907
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1268 TKE---EEQQRLINELTAQRGRLQTESGEYS---RQLDEKDSLVSQLSRGKQAFTQQI--------EELKRQLEEEIKAK 1333
Cdd:PRK04863 908 EAKrfvQQHGNALAQLEPIVSVLQSDPEQFEqlkQDYQQAQQTQRDAKQQAFALTEVVqrrahfsyEDAAEMLAKNSDLN 987
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1334 SALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEvaqWRTKYET--DAIQRTEEL-----EEAKKKLAQRLQD 1406
Cdd:PRK04863 988 EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSS---YDAKRQMlqELKQELQDLgvpadSGAEERARARRDE 1064
|
650 660
....*....|....*....|....*....
gi 82524274 1407 AEEHVEAVNAKCASLEKTKQRLQNEVEDL 1435
Cdd:PRK04863 1065 LHARLSANRSRRNQLEKQLTFCEAEMDNL 1093
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
855-1415 |
2.02e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 855 EMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQsEADSLADAEERCDQLIKT----KIQLEAKIKEVT 930
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN-ELSSLEDMKNRYESEIKTaesdLSMELEKNNYYK 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 931 ERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIakltkEKKALQEAH 1010
Cdd:PRK01156 277 ELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYI-----KKKSRYDDL 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1011 QQTLDDLQAEEDKVNTLTKakikleqQVDDLEGSLEQEKKirmDLERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKK 1090
Cdd:PRK01156 352 NNQILELEGYEMDYNSYLK-------SIESLKKKIEEYSK---NIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1091 EFEMSNLQSKIEdeqalgmQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEM 1170
Cdd:PRK01156 422 SSKVSSLNQRIR-------ALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKD 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1171 NKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMK-MEIDDLASNMEVISKSK 1249
Cdd:PRK01156 495 IDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKsLKLEDLDSKRTSWLNAL 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1250 GNLEKM-CRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLeE 1328
Cdd:PRK01156 575 AVISLIdIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKI-D 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1329 EIKAKSALAHALQSSRHDcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDaIQRTEELEEAKKKLAQRLQDAE 1408
Cdd:PRK01156 654 NYKKQIAEIDSIIPDLKE---ITSRINDIEDNLKKSRKALDDAKANRARLESTIEIL-RTRINELSDRINDINETLESMK 729
|
....*..
gi 82524274 1409 EHVEAVN 1415
Cdd:PRK01156 730 KIKKAIG 736
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1447-1624 |
2.63e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1447 AALDKKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAY---EESLDHLETLKRENKNLQQEISDlTEQI 1523
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEQLGNVRN-NKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1524 AEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNhirvVES 1603
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE----REE 167
|
170 180
....*....|....*....|.
gi 82524274 1604 MQSTLDAEIRSRNDAIRLKKK 1624
Cdd:COG1579 168 LAAKIPPELLALYERIRKRKN 188
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1253-1525 |
2.68e-06 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 52.55 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1253 EKMCRtLEDQVSELKTK-------EEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQ 1325
Cdd:pfam09726 395 DALVR-LEQDIKKLKAElqasrqtEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKR 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1326 LEEEIKAKSALAHALQSSRHdcdllREQYEEEQEAKAELQRAMSKANSevaqwrtkyeTDAI-QRTEELEEAKKKLAQRL 1404
Cdd:pfam09726 474 LKAEQEARASAEKQLAEEKK-----RKKEEEATAARAVALAAASRGEC----------TESLkQRKRELESEIKKLTHDI 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1405 QDAEEHVEAVNAKCASLEKTKQRlQNEVEDLMidvertnAACAALDKKQRNFDKILAewkqkyEETHAELEasqkesrsL 1484
Cdd:pfam09726 539 KLKEEQIRELEIKVQELRKYKES-EKDTEVLM-------SALSAMQDKNQHLENSLS------AETRIKLD--------L 596
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 82524274 1485 STELFKIKNAYEesLDHLETLKREnknlqQEISDLTEQIAE 1525
Cdd:pfam09726 597 FSALGDAKRQLE--IAQGQIYQKD-----QEIKDLKQKIAE 630
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1458-1883 |
2.71e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1458 KILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKR--ENKNLQQEISDLTEQIAEGGKRIHELEK 1535
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1536 IKKQIEqeksELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDaeiRSR 1615
Cdd:COG4717 154 RLEELR----ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE---ELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1616 NDAIRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDAL---------------RGQEDLKEQLAM 1680
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallflllaREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1681 VERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQ-------------GE 1747
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaallaeagvedeEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1748 MEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVR 1827
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD--EEELEEELEELEEELEELEE-ELEELREELAELEAELE 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 1828 ELEGEVENEQKRnveaikglRKHERRVKELTYQTEEDRKNVLrLQDLVDKLQSKVK 1883
Cdd:COG4717 464 QLEEDGELAELL--------QELEELKAELRELAEEWAALKL-ALELLEEAREEYR 510
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1460-1941 |
3.48e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1460 LAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQ 1539
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1540 IEQEKSELQAALEEAEASLEHeegkiLRIQLElnQVKSEIDRKIAEKDEEIDQLKRNHIRVV---ESMQSTLDAEIRSRN 1616
Cdd:pfam05483 181 TRQVYMDLNNNIEKMILAFEE-----LRVQAE--NARLEMHFKLKEDHEKIQHLEEEYKKEIndkEKQVSLLLIQITEKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1617 DAIR----LKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEI 1692
Cdd:pfam05483 254 NKMKdltfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1693 EELRATLEQTERSRKIAEQELLDASERVQ-LLHTQNTSLINTKKKLETDISQIQ---GEMEDIVQEARNAE---EKAKKA 1765
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFEATTCSLEeLLRTEQQRLEKNEDQLKIITMELQkksSELEEMTKFKNNKEvelEELKKI 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1766 ITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEqLALKGGKKQIQKLEARVRELEGEVENEQKRNVEAIK 1845
Cdd:pfam05483 414 LAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLE-IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1846 G---------------------LRKHERRVKELTYQTEEDRKNVLRLQD----LVDKLQSKVKAYKRQAEEAEEQSNVNL 1900
Cdd:pfam05483 493 HcdklllenkeltqeasdmtleLKKHQEDIINCKKQEERMLKQIENLEEkemnLRDELESVREEFIQKGDEVKCKLDKSE 572
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 82524274 1901 AKFRKIQHELEEAEERADIAESQVNKLRvKSREVHTKIISE 1941
Cdd:pfam05483 573 ENARSIEYEVLKKEKQMKILENKCNNLK-KQIENKNKNIEE 612
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1140-1431 |
4.56e-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: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1140 EKQRSDLSRELEEISERLEEAggatsaQIEMNKKREAEFQKMRRDLEEATLQHEAT---AATLRKKHADSVAELGEQIDN 1216
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQE------RLRQEKEEKAREVERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1217 LQRVKQKLEKEK---SEMKMEIDDLaSNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESgE 1293
Cdd:pfam17380 353 IRQEERKRELERirqEEIAMEISRM-RELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ-E 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1294 YSRQL------DEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAE---- 1363
Cdd:pfam17380 431 EARQRevrrleEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQamie 510
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 82524274 1364 -------LQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNE 1431
Cdd:pfam17380 511 eerkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESE 585
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
847-1063 |
5.51e-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: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 847 LKSAETEKEMANMKEEFEKAKENLAKAEAKRKE---------LEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLik 917
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL-- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 918 tKIQLEAKIKEVTERAEDEEEinaeltakkrkledecSELKKDIDDLELTLAkvEKEKHATEN--KVKNLTEEMAGLdet 995
Cdd:COG3206 246 -RAQLGSGPDALPELLQSPVI----------------QQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL--- 303
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82524274 996 iakltkeKKALQEAHQQTLDDLQAEedkVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLE 1063
Cdd:COG3206 304 -------RAQLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
987-1761 |
5.75e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 987 EEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEED---KVNTLTKAKIKLEQQVDDLEgsleqekkirmDLERAKRKLE 1063
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlnLVQTALRQQEKIERYQEDLE-----------ELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1064 GDLKLAQESTMDVENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQarieeleeeieaerasRAKAEKQR 1143
Cdd:COG3096 368 EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALE----------------KARALCGL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1144 SDLSreLEEISERLEEAGGATSAQIEmnKKREAEfQKMRrDLEEATLQHEATAATLRK-------KHADSVA-ELGEQID 1215
Cdd:COG3096 432 PDLT--PENAEDYLAAFRAKEQQATE--EVLELE-QKLS-VADAARRQFEKAYELVCKiageverSQAWQTArELLRRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1216 NLQRVKQKLEkeksEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQrlinELTAQRGRLQTESGEYS 1295
Cdd:COG3096 506 SQQALAQRLQ----QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA----ELEAQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1296 RQLdekdslvSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHalqssrhdcdlLREQYEEEQEAKAELQRAMSK-ANSE 1374
Cdd:COG3096 578 EQR-------SELRQQLEQLRARIKELAARAPAWLAAQDALER-----------LREQSGEALADSQEVTAAMQQlLERE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1375 VAQWRTKYEtdAIQRTEELEEAKKKLAQ-------RLQDAEEHVEAV------------NAKCAS--------------L 1421
Cdd:COG3096 640 REATVERDE--LAARKQALESQIERLSQpggaedpRLLALAERLGGVllseiyddvtleDAPYFSalygparhaivvpdL 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1422 EKTKQRLQNeVEDLMIDV------------------ERTNAACAALDKKQRNFDKI-------LAEWKQKYEETHAELEA 1476
Cdd:COG3096 718 SAVKEQLAG-LEDCPEDLyliegdpdsfddsvfdaeELEDAVVVKLSDRQWRYSRFpevplfgRAAREKRLEELRAERDE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1477 SQKESRSLSTELFKIKNAYEesldHLETLKRENKNL------QQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAA 1550
Cdd:COG3096 797 LAEQYAKASFDVQKLQRLHQ----AFSQFVGGHLAVafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQ 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1551 LEE-----AEASLEHEEGKILRIQlelnQVKSEIDrkIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSrNDAIRLkkkm 1625
Cdd:COG3096 873 LQLlnkllPQANLLADETLADRLE----ELREELD--AAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQ-FEQLQA---- 941
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1626 egDLNEMEIQLnHSNRMAAEALR---------NYRNTQGILKDTQlHLDDALRGQ-EDLKEQLAMVERRANLLQAEIEEL 1695
Cdd:COG3096 942 --DYLQAKEQQ-RRLKQQIFALSevvqrrphfSYEDAVGLLGENS-DLNEKLRARlEQAEEARREAREQLRQAQAQYSQY 1017
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1696 RATLEQTERSR-------KIAEQELLD------------ASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEAR 1756
Cdd:COG3096 1018 NQVLASLKSSRdakqqtlQELEQELEElgvqadaeaeerARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLR 1097
|
....*
gi 82524274 1757 NAEEK 1761
Cdd:COG3096 1098 KAERD 1102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1352-1564 |
6.12e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1352 EQYEEEQEAKAELQRAMSKANSEVAQWRTKyETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNE 1431
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1432 VEDLMIDVERTNAACAALDKKQR-----------NFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLD 1500
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPlalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82524274 1501 HLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGK 1564
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1299-1585 |
7.08e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 51.08 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1299 DEKDSLVSQLsRGKQAFtqQIEELKRQLEEEiKAKSALAHALQSSRHdCDLLREQYEEEQEAKAELQRamskansevaqw 1378
Cdd:PRK05771 16 SYKDEVLEAL-HELGVV--HIEDLKEELSNE-RLRKLRSLLTKLSEA-LDKLRSYLPKLNPLREEKKK------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1379 rtkyetdaiQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLmidvertnaacaaldKKQRNFDk 1458
Cdd:PRK05771 79 ---------VSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL---------------EPWGNFD- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1459 ILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLE------TLKRENKNLQQEISDLT---EQIAEGGKR 1529
Cdd:PRK05771 134 LDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvVLKELSDEVEEELKKLGferLELEEEGTP 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 1530 IHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELnqvksEIDRKIAE 1585
Cdd:PRK05771 214 SELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYL-----EIELERAE 264
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1680-1942 |
7.25e-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: 51.21 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1680 MVERranLLQAEIEELRATLEQ-------TERsRKIAEQELLDASE---RVQLLHTQntslinTKKKLETdiSQIQGEME 1749
Cdd:TIGR02168 145 KISE---IIEAKPEERRAIFEEaagiskyKER-RKETERKLERTREnldRLEDILNE------LERQLKS--LERQAEKA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1750 DIVQEARNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLEARVREL 1829
Cdd:TIGR02168 213 ERYKELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEELRLEVSEL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1830 EGEVENEQKRNVEAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNVNLAKFRKIQHE 1909
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
250 260 270
....*....|....*....|....*....|...
gi 82524274 1910 LEEAEERADIAESQVNKLRVKSREVHTKIISEE 1942
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
842-1437 |
8.22e-06 |
|
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: 51.27 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 842 KIKPLLKSAETEKEM-ANMKEEFEKAKENLAKAEAKRKEL----EEKMVAL---------MQEKNDLQLQ----VQSEAD 903
Cdd:pfam15921 462 KVSSLTAQLESTKEMlRKVVEELTAKKMTLESSERTVSDLtaslQEKERAIeatnaeitkLRSRVDLKLQelqhLKNEGD 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 904 SLADAEERCDQLiktKIQLEAK---IKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATEN 980
Cdd:pfam15921 542 HLRNVQTECEAL---KLQMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 981 KVKNLTEEMAGLDETIAKLTKEKKALQEAhqqtLDDLQAEEDKV-NTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAK 1059
Cdd:pfam15921 619 KIRELEARVSDLELEKVKLVNAGSERLRA----VKDIKQERDQLlNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1060 RKLEGDLKLAQEstmDVENDKQQLdeklkkKEFEMSNLQSKiedEQALGMQLQ-----KKIKELQARIEELEEEIEAERA 1134
Cdd:pfam15921 695 NKLKMQLKSAQS---ELEQTRNTL------KSMEGSDGHAM---KVAMGMQKQitakrGQIDALQSKIQFLEEAMTNANK 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1135 SRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQ----------HEATAATLRKKHA 1204
Cdd:pfam15921 763 EKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQfaecqdiiqrQEQESVRLKLQHT 842
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1205 DSVAEL-GEQIDNLQRVKQKLEKEKSEMKMEiDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINEL-TA 1282
Cdd:pfam15921 843 LDVKELqGPGYTSNSSMKPRLLQPASFTRTH-SNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEpTV 921
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1283 QRGRLQ-----TESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQ-SSRHDCDLLREQYEE 1356
Cdd:pfam15921 922 QLSKAEdkgraPSLGALDDRVRDCIIESSLRSDICHSSSNSLQTEGSKSSETCSREPVLLHAGElEDPSSCFTFPSTASP 1001
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1357 EQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKK-KLAQRLQDAEEH-VEAVNAKCASLEKTKQRLQNEVED 1434
Cdd:pfam15921 1002 SVKNSASRSFHSSPKKSPVHSLLTSSAEGSIGSSSQYRSAKTiHSPDSVKDSQSLpIETTGKTCRKLQNRLESLQTLVED 1081
|
...
gi 82524274 1435 LMI 1437
Cdd:pfam15921 1082 LQL 1084
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
856-1720 |
8.91e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.11 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 856 MANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLAdaeercdqLIKTKIQLEAKIK-------E 928
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLN--------LVQTALRQQEKIEryqedleE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 929 VTERAEDEEEINAELTAKkrkledecselkkdiddleltLAKVEKEKHATENKVKNLTEEMA----GLDE--TIA-KLTK 1001
Cdd:COG3096 359 LTERLEEQEEVVEEAAEQ---------------------LAEAEARLEAAEEEVDSLKSQLAdyqqALDVqqTRAiQYQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1002 EKKALQEAHQQT-LDDLQAE--EDKVNTLtKAKiklEQQVDDLEGSLEQekkiRMDL-ERAKRKLEGDLKLAQESTMDVE 1077
Cdd:COG3096 418 AVQALEKARALCgLPDLTPEnaEDYLAAF-RAK---EQQATEEVLELEQ----KLSVaDAARRQFEKAYELVCKIAGEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1078 ndKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQarieeleeeieaeraSRAKAEKQRSDLSR--------- 1148
Cdd:COG3096 490 --RSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLR---------------QQQNAERLLEEFCQrigqqldaa 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1149 -ELEEISERLEeaggatsAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKK-----HADSVAE-----LGEQIDNL 1217
Cdd:COG3096 553 eELEELLAELE-------AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlAAQDALErlreqSGEALADS 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1218 QRV----KQKLEKEKsEMKMEIDDLA-------SNMEVISKSKGNLEKMCRTLEDQ-----VSELK---TKEE------- 1271
Cdd:COG3096 626 QEVtaamQQLLERER-EATVERDELAarkqaleSQIERLSQPGGAEDPRLLALAERlggvlLSEIYddvTLEDapyfsal 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1272 ----EQQRLINELTAQRGRLQT-------------------ESGEYSRQLDEKDSLVS---QL--SR-------GKQAFT 1316
Cdd:COG3096 705 ygpaRHAIVVPDLSAVKEQLAGledcpedlyliegdpdsfdDSVFDAEELEDAVVVKLsdrQWrySRfpevplfGRAARE 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1317 QQIEELKRQLEEEIK--AKSA--------LAHALQS--SRHDCDLLREQYEEE----QEAKAELQRAMSKANSEVAQWRT 1380
Cdd:COG3096 785 KRLEELRAERDELAEqyAKASfdvqklqrLHQAFSQfvGGHLAVAFAPDPEAElaalRQRRSELERELAQHRAQEQQLRQ 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1381 KY---------------------ETDAIQRTEELEEAkkklAQRLQDAEEHVEAVNAKCASLEKTKQRLQN---EVEDLM 1436
Cdd:COG3096 865 QLdqlkeqlqllnkllpqanllaDETLADRLEELREE----LDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpeQFEQLQ 940
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1437 IDVERTNAACAALdkKQRNFdkILAEWKQK-----YEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKN 1511
Cdd:COG3096 941 ADYLQAKEQQRRL--KQQIF--ALSEVVQRrphfsYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQ 1016
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1512 LQQEISDLT-------EQIAEGGKRIHELE-----KIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLE---LNQVK 1576
Cdd:COG3096 1017 YNQVLASLKssrdakqQTLQELEQELEELGvqadaEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEmdsLQKRL 1096
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1577 SEIDRKIAEKDEEIDQLKRNHIRVVEsmqstldaeiRSRNDAirlkkkMEGDLN--EMEIQLNHSNR-MAAEALRNYRNT 1653
Cdd:COG3096 1097 RKAERDYKQEREQVVQAKAGWCAVLR----------LARDND------VERRLHrrELAYLSADELRsMSDKALGALRLA 1160
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1654 QGILKdtqlHLDDALRGQEDLKEQLAMV-----------ER-----------RANLLQAEIEELRATLEQTERsrkiaEQ 1711
Cdd:COG3096 1161 VADNE----HLRDALRLSEDPRRPERKVqfyiavyqhlrERirqdiirtddpVEAIEQMEIELARLTEELTSR-----EQ 1231
|
....*....
gi 82524274 1712 ELLDASERV 1720
Cdd:COG3096 1232 KLAISSESV 1240
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1008-1192 |
9.06e-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: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1008 EAHQQTLDDLQAEEDKVNTLTKAK-------IKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQEstmDVENDK 1080
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLkelpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1081 QQLDEKLKKKEFEmsNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIeaerasrAKAEKQRSDLSRELEEISERLEEA 1160
Cdd:COG1579 80 EQLGNVRNNKEYE--ALQKEIESLKRRISDLEDEILELMERIEELEEEL-------AELEAELAELEAELEEKKAELDEE 150
|
170 180 190
....*....|....*....|....*....|..
gi 82524274 1161 GGATSAQIEmnkKREAEFQKMRRDLEEATLQH 1192
Cdd:COG1579 151 LAELEAELE---ELEAEREELAAKIPPELLAL 179
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1505-1910 |
1.03e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.74 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1505 LKRENKNLQQEISDLTE-----QIAEGGKRIHELEKIKKQIEQEKSEL--------QAALEEAEASLEHEEGKILRIQLE 1571
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPldqytQLALMEFAKKKSLHGKAELLTLRSQLltlctpcmPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1572 LNQVKSEIDRKIaEKDEEIDQLKRNHIRVVESMQS--TLDAEIRSRNDAIRLKKKMEGDLNEMEiQLNHSNRMAAEALRN 1649
Cdd:TIGR00618 238 TQQSHAYLTQKR-EAQEEQLKKQQLLKQLRARIEElrAQEAVLEETQERINRARKAAPLAAHIK-AVTQIEQQAQRIHTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1650 YRNTQGILKDTQLHLDDALRGQEDLKEQlamvERRANLLQAEIEELRATLEQTERSRKIAEQELLDaSERVQLLHTQNTS 1729
Cdd:TIGR00618 316 LQSKMRSRAKLLMKRAAHVKQQSSIEEQ----RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL-TQHIHTLQQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1730 LINTKKKLETDISQIQGEMEDivQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVK-----DLQHRL 1804
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQAT--IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEkihlqESAQSL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1805 DEAEQLalKGGKKQIQKLEARVRELEGEVENEQKRNVEAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKA 1884
Cdd:TIGR00618 469 KEREQQ--LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEED 546
|
410 420
....*....|....*....|....*.
gi 82524274 1885 YKRQAEEAEEQSNVNLAKFRKIQHEL 1910
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQSF 572
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1319-1938 |
1.12e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1319 IEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYE--TDAIQRTEELEEA 1396
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1397 KKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLqNEVEDLMIDVERTNAACAALDKKQ-RNFDKILAEWK---QKYEETHA 1472
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYKELEERH-MKIINDPVYKNRNYINDYFKYKNDiENKKQILSNIDaeiNKYHAIIK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1473 ELEasqkesrslstELFKIKNAYEEsldhletLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALE 1552
Cdd:PRK01156 330 KLS-----------VLQKDYNDYIK-------KKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1553 EAEASLEHEEGKILRIQLELNQVKSEIDRkiaekdeeidqlkrnhirvVESMQSTLDAEIRSRNDairlkkkmegdlNEM 1632
Cdd:PRK01156 392 FISEILKIQEIDPDAIKKELNEINVKLQD-------------------ISSKVSSLNQRIRALRE------------NLD 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1633 EIQLNhsnrMAAEALRNYRNTQGilkdTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELratleqTERSRKIAEQE 1712
Cdd:PRK01156 441 ELSRN----MEMLNGQSVCPVCG----TTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDI------DEKIVDLKKRK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1713 LLDASERVQllhtqntSLINTKKKLETDISQIQGEMEDIvQEARNAEEKAKKAITDAAMMAEELKKEQDTSaHLERMKKN 1792
Cdd:PRK01156 507 EYLESEEIN-------KSINEYNKIESARADLEDIKIKI-NELKDKHDKYEEIKNRYKSLKLEDLDSKRTS-WLNALAVI 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1793 LEQTVKDLQHRLDEAeqlalkggKKQIQKLEARVRELEGEVENEQKRNVEAIkglrkheRRVKELTYQTEEDRKNVLRLQ 1872
Cdd:PRK01156 578 SLIDIETNRSRSNEI--------KKQLNDLESRLQEIEIGFPDDKSYIDKSI-------REIENEANNLNNKYNEIQENK 642
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1873 DLVDKLQSKVKAYKRQAEEAEE----QSNVNlAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKI 1938
Cdd:PRK01156 643 ILIEKLRGKIDNYKKQIAEIDSiipdLKEIT-SRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1673-1942 |
1.40e-05 |
|
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: 50.44 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1673 DLKEQLAMVERRanLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIV 1752
Cdd:TIGR02168 217 ELKAELRELELA--LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1753 QEARNAEEKakKAITDAAMmaeelkkeqdtsAHLERMKKNLEQTVKDLQHRLDEAEQLAlkggkkqiQKLEARVRELEGE 1832
Cdd:TIGR02168 295 NEISRLEQQ--KQILRERL------------ANLERQLEELEAQLEELESKLDELAEEL--------AELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1833 VENEQKRNVEAIKGLRKHERRVKELtyqteedrknvlrlQDLVDKLQSKVKaykrqaeEAEEQSNVNLAKFRKIQHELEE 1912
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEEL--------------EEQLETLRSKVA-------QLELQIASLNNEIERLEARLER 411
|
250 260 270
....*....|....*....|....*....|
gi 82524274 1913 AEERADIAESQVNKLRVKSREVHTKIISEE 1942
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKELQAE 441
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1507-1942 |
1.43e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1507 RENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGKilriqlelnqvKSEIDRKIAEK 1586
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-----------KAEDARKAEEA 1145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1587 DEEIDQLKRNHIRVVESMQSTldAEIRSRNDAirlkKKMEGDLNEMEIQLNHSNRMA-----AEALRNYRNTQGIlkdtq 1661
Cdd:PTZ00121 1146 RKAEDAKRVEIARKAEDARKA--EEARKAEDA----KKAEAARKAEEVRKAEELRKAedarkAEAARKAEEERKA----- 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1662 lhldDALRGQEDLKEQLAMveRRANLLQAEIEELRATLEQ--TERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLET 1739
Cdd:PTZ00121 1215 ----EEARKAEDAKKAEAV--KKAEEAKKDAEEAKKAEEErnNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1740 DISQIQ---GEMEDIVQEARNAEEKAKKAiTDAAMMAEELKKEQDTsahlerMKKNLEQTVKDlqhrlDEAEQLALKGGK 1816
Cdd:PTZ00121 1289 KKKADEakkAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADA------AKKKAEEAKKA-----AEAAKAEAEAAA 1356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1817 KQIQKLEARVRELEGEVEnEQKRNVEAIKGLRKHERRVKELTYQTEEDRKnvlRLQDLVDKLQSKVKA--YKRQAEEAEE 1894
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKE-EAKKKADAAKKKAEEKKKADEAKKKAEEDKK---KADELKKAAAAKKKAdeAKKKAEEKKK 1432
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 82524274 1895 QSNV-NLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1942
Cdd:PTZ00121 1433 ADEAkKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1093-1335 |
1.54e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1093 EMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEaggatsaqiemnk 1172
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1173 kREAEFQKMRRDLEEATLQHEATAATLrkkHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKGNL 1252
Cdd:COG3883 84 -RREELGERARALYRSGGSVSYLDVLL---GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1253 EKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKA 1332
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
...
gi 82524274 1333 KSA 1335
Cdd:COG3883 240 AAA 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
850-982 |
1.73e-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: 48.38 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 850 AETEKEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQ--EKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKIK 927
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAriKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 82524274 928 EVTERAEDEE----EINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV 982
Cdd:COG1579 114 ELMERIEELEeelaELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1458-1585 |
1.85e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1458 KILAEWKQKYEETHAELEASQKESRSlstelfKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIK 1537
Cdd:PRK12704 57 EALLEAKEEIHKLRNEFEKELRERRN------ELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 82524274 1538 KQIEQEKSELQAALEEAeASLEHEEGKilriQLELNQVKSEIDRKIAE 1585
Cdd:PRK12704 131 EELEELIEEQLQELERI-SGLTAEEAK----EILLEKVEEEARHEAAV 173
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1355-1475 |
1.95e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1355 EEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqdaeehVEAVNAKCASLEKTKQRLQNEVED 1434
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK-------EENLDRKLELLEKREEELEKKEKE 118
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 82524274 1435 lmidvertnaacaaLDKKQRNFDKILAEWKQKYEETHAELE 1475
Cdd:PRK12704 119 --------------LEQKQQELEKKEEELEELIEEQLQELE 145
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1351-1712 |
3.17e-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: 48.98 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1351 REQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQD-AEEHVEAVNAKCASLEKTKQRLQ 1429
Cdd:pfam09731 77 GESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEvLKEAISKAESATAVAKEAKDDAI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1430 NEVEDLMIDVERTNAACAALDKKQRNFDKILAE-WKQKYEETHAELEASQKES-RSLSTELFKIKNAYEESLDHLETLKR 1507
Cdd:pfam09731 157 QAVKAHTDSLKEASDTAEISREKATDSALQKAEaLAEKLKEVINLAKQSEEEAaPPLLDAAPETPPKLPEHLDNVEEKVE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1508 ENKNLQQEISDLTEQIAEG-GKRIHELEKIKKQIEQEKSELQAAL-EEAEASLEHEEGKILRIQLELN----QVKSEIDR 1581
Cdd:pfam09731 237 KAQSLAKLVDQYKELVASErIVFQQELVSIFPDIIPVLKEDNLLSnDDLNSLIAHAHREIDQLSKKLAelkkREEKHIER 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1582 KIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIR--LKKKMEgdlNEMEIQLNHSNRMAAEALRNYRNTQGILKD 1659
Cdd:pfam09731 317 ALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREReeIRESYE---EKLRTELERQAEAHEEHLKDVLVEQEIELQ 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 1660 tqlhlddaLRGQEDLKEQlamVERRANLLQAEIEELRATLEQTER---SRKIAEQE 1712
Cdd:pfam09731 394 --------REFLQDIKEK---VEEERAGRLLKLNELLANLKGLEKatsSHSEVEDE 438
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1309-1585 |
3.52e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.99 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1309 SRGKQAFTQQIEELKRQLEEEIKAKsalahalqssrhdcdllreqyeeeqeAKAELQRamSKANSEVAQWRTKYETDAIQ 1388
Cdd:pfam00038 46 SRLYSLYEKEIEDLRRQLDTLTVER--------------------------ARLQLEL--DNLRLAAEDFRQKYEDELNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1389 RTeELEEAKKKLAQRLQDA-------EEHVEAVNAKCASLEKTKQR----LQNEVEDLMIDVERTNAACAALdkkqrnfD 1457
Cdd:pfam00038 98 RT-SAENDLVGLRKDLDEAtlarvdlEAKIESLKEELAFLKKNHEEevreLQAQVSDTQVNVEMDAARKLDL-------T 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1458 KILAEWKQKYEEtHAELeasqkeSRSLSTELFKIKnaYEESLDHLETLKRENKNLQQEISDLTEQIAEggkRIHELEKIK 1537
Cdd:pfam00038 170 SALAEIRAQYEE-IAAK------NREEAEEWYQSK--LEELQQAAARNGDALRSAKEEITELRRTIQS---LEIELQSLK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 82524274 1538 KQieqeKSELQAALEEAEASLEHE----EGKILRIQLELNQVKSEIDRKIAE 1585
Cdd:pfam00038 238 KQ----KASLERQLAETEERYELQladyQELISELEAELQETRQEMARQLRE 285
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
850-1037 |
3.57e-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: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 850 AETEKEMANMKEEFEKAKENLAKAEAK----RKELEEKMVALMQEKNDLQ-LQVQSEADSLADAEERCDQLikTKIqlea 924
Cdd:COG3883 54 NELQAELEALQAEIDKLQAEIAEAEAEieerREELGERARALYRSGGSVSyLDVLLGSESFSDFLDRLSAL--SKI---- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 925 kikevterAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKK 1004
Cdd:COG3883 128 --------ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
170 180 190
....*....|....*....|....*....|...
gi 82524274 1005 ALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQ 1037
Cdd:COG3883 200 ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1045-1548 |
4.13e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1045 LEQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKKEFEMSNLQSKIEDEQalgmqLQKKIKELQARIEE 1124
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-----LEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1125 LEeeieaerasraKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkreaefqkmRRDLEEATLQHEATAATLRKKHA 1204
Cdd:COG4717 151 LE-----------ERLEELRELEEELEELEAELAEL---------------------QEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1205 DSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKgNLEKMCRTLEdQVSELKTKEEEQQRLINELTAQR 1284
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLL-IAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1285 GRLQTESGEYSrqldekdSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAEL 1364
Cdd:COG4717 277 GVLFLVLGLLA-------LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1365 QRAMSKANSEVAQWRTKYETDAIQrtEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNa 1444
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIA--ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1445 acaaldkkqrnfdkiLAEWKQKYEETHAELEASQKESRSLSTELFKIKNAyeesldhLETLKRENK--NLQQEISDLTEQ 1522
Cdd:COG4717 427 ---------------EEELEEELEELEEELEELEEELEELREELAELEAE-------LEQLEEDGElaELLQELEELKAE 484
|
490 500
....*....|....*....|....*.
gi 82524274 1523 IAEGGKRIHELEKIKKQIEQEKSELQ 1548
Cdd:COG4717 485 LRELAEEWAALKLALELLEEAREEYR 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
941-1167 |
4.21e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 941 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAE 1020
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1021 EDKVNTLTkakIKLE--------QQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKlaqestmDVENDKQQLDEKLKKKEF 1092
Cdd:COG3883 99 GGSVSYLD---VLLGsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKA-------ELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 82524274 1093 EMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQ 1167
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1136-1564 |
4.46e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1136 RAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATlQHEATAATLRKKHADSVAELGEQID 1215
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELE-EELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1216 NLQRVK--QKLEKEKSEMKMEIDDLASNMEVISkskgNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQR-GRLQTESG 1292
Cdd:COG4717 127 LLPLYQelEALEAELAELPERLEELEERLEELR----ELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1293 EYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLE-----EEIKAKSALAhALQSSRHDCDLLREQYEEEQEAKAELQRA 1367
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEaaaleERLKEARLLL-LIAAALLALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1368 MSKANSEVAQWRTKYETDAIQRTEELEEAKKKlaQRLQDAEehveaVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACA 1447
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPAL--EELEEEE-----LEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1448 ALDK--KQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENK---------NLQQEI 1516
Cdd:COG4717 355 EAEEleEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEellealdeeELEEEL 434
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 82524274 1517 SDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEGK 1564
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELK 482
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1500-1942 |
4.63e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 48.36 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1500 DHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAAL--------EEAEASLEHEEGKILRIQLE 1571
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1572 LNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYR 1651
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1652 NTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLI 1731
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1732 NTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLA 1811
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1812 LKGGKKQIQKLEARVRELEGEVENEQKRNVEAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEE 1891
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 82524274 1892 AEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1942
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1672-1917 |
5.43e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1672 EDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQllhTQNTSLINTKKKLETDISQIQGEMEDI 1751
Cdd:pfam07888 16 EEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYK---RDREQWERQRRELESRVAELKEELRQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1752 VQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEqLALKGGKKQIQKLEARVRELEG 1831
Cdd:pfam07888 93 REKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE-TELERMKERAKKAGAQRKEEEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1832 EVENEQKRNVEAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQsnvnLAKFRKIQHELE 1911
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL----LEELRSLQERLN 247
|
....*.
gi 82524274 1912 EAEERA 1917
Cdd:pfam07888 248 ASERKV 253
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1522-1721 |
5.85e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1522 QIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEAsleheegKILRIQLELNQVKSEID---RKIAEKDEEIDQLKRNHI 1598
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNE-------EYNELQAELEALQAEIDklqAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1599 RVVESMQ------STLDAEIRSRNDairlkkkmeGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQE 1672
Cdd:COG3883 90 ERARALYrsggsvSYLDVLLGSESF---------SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 82524274 1673 DLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQ 1721
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1753-1942 |
6.57e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1753 QEARNAEE----KAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAE------QLALKGGKKQIQKL 1822
Cdd:COG1196 207 RQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEaeleelRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1823 EARVRELEGEVENEQKRNVEAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNVNLAK 1902
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 82524274 1903 FRKIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1942
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1734-1933 |
7.24e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1734 KKKLETDISQIQGEMEDIVqEARNAEEKAKKAI---TDAAMMAEELKKEQDTSAHLERMKKNLEqtVKDLQHRLDEAEQl 1810
Cdd:COG4913 220 EPDTFEAADALVEHFDDLE-RAHEALEDAREQIellEPIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEA- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1811 ALKGGKKQIQKLEARVRELEGEVENEQKRNVEAIKGLRKH--------ERRVKELTYQTEEDRKNVLRLQDLVDKLQSKV 1882
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 82524274 1883 KAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNK-LRVKSRE 1933
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRReLRELEAE 427
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1468-1836 |
7.69e-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: 47.37 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1468 EETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSEL 1547
Cdd:pfam19220 37 EAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1548 QAALEEAEASLEHEEGKILRIQLELNQVKSEI---DRKIAEKDEEIDQLKRNHIRvvesmqstLDAEIRsrndaiRLKKK 1624
Cdd:pfam19220 117 TAQAEALERQLAAETEQNRALEEENKALREEAqaaEKALQRAEGELATARERLAL--------LEQENR------RLQAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1625 ME---GDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAmVERRAnlLQAEIEELRATLEQ 1701
Cdd:pfam19220 183 SEeqaAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHR-AERAS--LRMKLEALTARAAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1702 TERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDivQEARNAE-EKAKKAITD-AAMMAEELKke 1779
Cdd:pfam19220 260 TEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLER--RTQQFQEmQRARAELEErAEMLTKALA-- 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 82524274 1780 qDTSAHLERMkknlEQTVKDLQHRLDEAEQLALKggkkQIQKLEARVRELEGEVENE 1836
Cdd:pfam19220 336 -AKDAALERA----EERIASLSDRIAELTKRFEV----ERAALEQANRRLKEELQRE 383
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1194-1409 |
7.79e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1194 ATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLAsnmEVISKSKGNLEKmcrtLEDQVSELKTKEEEQ 1273
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ---AELEALQAEIDK----LQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1274 QrlinELTAQRGRLQTESGEYSRQLD------------EKDSLVSQLSRGKQAFTQQIEELKRQLEEeikAKSALAHALQ 1341
Cdd:COG3883 85 R----EELGERARALYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEA---KKAELEAKLA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82524274 1342 SsrhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEE 1409
Cdd:COG3883 158 E-------LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1258-1416 |
8.33e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1258 TLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAK--SA 1335
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1336 LAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVN 1415
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
.
gi 82524274 1416 A 1416
Cdd:COG1579 174 P 174
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
851-1086 |
9.09e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 851 ETEKEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERcDQLIKTKIQLEAKIKEVT 930
Cdd:pfam05483 556 EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQE-NKALKKKGSAENKQLNAY 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 931 ERAEDEEEInaELTAKKRKLEDECSELKKDIDDLELT----LAKVEKEKHATENKVKNLTEemagLDETIAKLTKEKKAL 1006
Cdd:pfam05483 635 EIKVNKLEL--ELASAKQKFEEIIDNYQKEIEDKKISeeklLEEVEKAKAIADEAVKLQKE----IDKRCQHKIAEMVAL 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1007 QEAHQQTLDDLQAEEDKVNTLTKAKiklEQQVDDLEGSLEQE-KKIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLDE 1085
Cdd:pfam05483 709 MEKHKHQYDKIIEERDSELGLYKNK---EQEQSSAKAALEIElSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
.
gi 82524274 1086 K 1086
Cdd:pfam05483 786 K 786
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
847-1091 |
1.02e-04 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 47.46 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 847 LKSAETEKEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEK--NDLQLQVQSEADSLADaeercdqliktkiQLEA 924
Cdd:pfam18971 596 FNKAVAEAKSTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKsgNKNKMEAKAQANSQKD-------------EIFA 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 925 KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL-------DETIA 997
Cdd:pfam18971 663 LINKEANRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSvkdlginPEWIS 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 998 KLTKEKKALQEAHQQTLDDLqaeedkvNTLTKAKIKLEQQVDDLEGSLEQEKKI-RMDLERAKRKLEGDLKLAQESTMDV 1076
Cdd:pfam18971 743 KVENLNAALNEFKNGKNKDF-------SKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADL 815
|
250
....*....|....*.
gi 82524274 1077 EN-DKQQLDEKLKKKE 1091
Cdd:pfam18971 816 KNfSKEQLAQQAQKNE 831
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1257-1581 |
1.03e-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: 47.64 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1257 RTLEdQVSELKTKEEEQQRLINELTAQRgrlqteSGEYSRQLDEKDSLVSQL---------SRGKQAFTQQ-IEELKRQL 1326
Cdd:COG3096 243 MTLE-AIRVTQSDRDLFKHLITEATNYV------AADYMRHANERRELSERAlelrrelfgARRQLAEEQYrLVEMAREL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1327 EEEIKAKSALAHALQSSRHDCDLLR---------EQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAK 1397
Cdd:COG3096 316 EELSARESDLEQDYQAASDHLNLVQtalrqqekiERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLK 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1398 KKLA--QRLQD-----AEEHVEAVNAkcasLEKTKQRLQNEveDLMIDvertNAA--CAALDKKQRNFDKILAEWKQKY- 1467
Cdd:COG3096 396 SQLAdyQQALDvqqtrAIQYQQAVQA----LEKARALCGLP--DLTPE----NAEdyLAAFRAKEQQATEEVLELEQKLs 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1468 --EETHAELEA------------SQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEIS---DLTEQIAEGGKRI 1530
Cdd:COG3096 466 vaDAARRQFEKayelvckiagevERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRqqqNAERLLEEFCQRI 545
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 82524274 1531 HELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDR 1581
Cdd:COG3096 546 GQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE 596
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1258-1377 |
1.09e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.50 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1258 TLEDQVS----ELKTKEEEQQRL---INELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLeeei 1330
Cdd:PRK09039 78 DLQDSVAnlraSLSAAEAERSRLqalLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQL---- 153
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 82524274 1331 kakSALAHALQSSRhdcdllreqyEEEQEAKAELQRAMSKANSEVAQ 1377
Cdd:PRK09039 154 ---AALEAALDASE----------KRDRESQAKIADLGRRLNVALAQ 187
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1664-1942 |
1.46e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1664 LDDALRGQEDLKEQLAMVER-----RANLLQAEIEELRATLEQTERSRKIAEQELLDASERVqllhtqntslintkkkle 1738
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEADEVL------------------ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1739 TDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQhrLDEAEQLALKGGKKQ 1818
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER---LEELEEERDDLLAEAG--LDDADAEAVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1819 IQKLEARVRELEGEVENEQKRNVEAIKGLRKherRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNV 1898
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLRE---DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 82524274 1899 NLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1942
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1306-1545 |
1.68e-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: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1306 SQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRtkyetd 1385
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1386 aiqrtEELEEAKKKLAQRLQDAEEHVEAVNAKCAslekTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQ 1465
Cdd:COG4942 97 -----AELEAQKEELAELLRALYRLGRQPPLALL----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1466 KYEETHAELEASQKESRSLSTELFKIKNAYEESLdhlETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKS 1545
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1529-1763 |
1.75e-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: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1529 RIHELEKIKKQIEQEKSELQAALEEAEASLEH--EEGKILRIQLELNQV---KSEIDRKIAEKDEEIDQLKRNHIRVVES 1603
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLlqqLSELESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1604 MQSTLDAEIRSRNDAIRlkKKMEGDLNEMEIQLnhsnrmaAEALRNYRNTQGILKDTQLHLDDALRG-QEDLKEQLAMVE 1682
Cdd:COG3206 249 LGSGPDALPELLQSPVI--QQLRAQLAELEAEL-------AELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1683 RRANLLQAEIEELRATLEQTERSRKI---AEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEdIVQEARNAE 1759
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR-VIDPAVVPL 398
|
....
gi 82524274 1760 EKAK 1763
Cdd:COG3206 399 KPVS 402
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1689-1916 |
1.78e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.66 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1689 QAEIEELRATLEQTERSRKiaEQELLDASERVQLLHTQNTSlintKKKLETDISQIQgEMEDIVQEARNAEEKAKKAITD 1768
Cdd:pfam05557 1 RAELIESKARLSQLQNEKK--QMELEHKRARIELEKKASAL----KRQLDRESDRNQ-ELQKRIRLLEKREAEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1769 AAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRL-DEAEQLalkggKKQIQKLEARVRELEGEVENEQKRNVEAIKGL 1847
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSEL-----RRQIQRAELELQSTNSELEELQERLDLLKAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 82524274 1848 RKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVkaykrQAEEAEEQSNVNLAKFRKIQHELEEAEER 1916
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQE-----QDSEIVKNSKSELARIPELEKELERLREH 212
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
855-1095 |
1.92e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.43 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 855 EMANMKEEFEKAKENLAKAEAKRKELEEKmvaLMQEKNDLQLQVQSEADSLADAEERCDQLIKTKI-------QLEAKIK 927
Cdd:PLN02939 132 DLVGMIQNAEKNILLLNQARLQALEDLEK---ILTEKEALQGKINILEMRLSETDARIKLAAQEKIhveileeQLEKLRN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 928 EVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKekhaTENKVKNLTEEMAGLDETIAKLTKEKKALQ 1007
Cdd:PLN02939 209 ELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAE----TEERVFKLEKERSLLDASLRELESKFIVAQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1008 EAHQQtLDDLQAEE--DKVNTLT-----------KAKIKLEQ------QVDDLEGSLEQ--------------EKKIRM- 1053
Cdd:PLN02939 285 EDVSK-LSPLQYDCwwEKVENLQdlldratnqveKAALVLDQnqdlrdKVDKLEASLKEanvskfssykvellQQKLKLl 363
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 82524274 1054 --DLERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKKEFEMS 1095
Cdd:PLN02939 364 eeRLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEHP 407
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
852-1107 |
1.94e-04 |
|
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: 46.29 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 852 TEKEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADS--LADAEERCDQLIKTKIQLEAKIKEV 929
Cdd:pfam09731 159 VKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPplLDAAPETPPKLPEHLDNVEEKVEKA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 930 TERAEDEEEINaELTAKKRklEDECSELKKDIDDLELTLAKVEKEKHATENKVknlteeMAGLDETIAKLTKE----KKA 1005
Cdd:pfam09731 239 QSLAKLVDQYK-ELVASER--IVFQQELVSIFPDIIPVLKEDNLLSNDDLNSL------IAHAHREIDQLSKKlaelKKR 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1006 LQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLDE 1085
Cdd:pfam09731 310 EEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQE 389
|
250 260
....*....|....*....|..
gi 82524274 1086 KLKKKEFeMSNLQSKIEDEQAL 1107
Cdd:pfam09731 390 IELQREF-LQDIKEKVEEERAG 410
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1643-1843 |
2.06e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1643 AAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERV-- 1720
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELge 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1721 QLLHTQNTSLINTK-------KKLETDISQIQGeMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNL 1793
Cdd:COG3883 91 RARALYRSGGSVSYldvllgsESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 82524274 1794 EQTVKDLQHRLDEAEQLaLKGGKKQIQKLEARVRELEGEVENEQKRNVEA 1843
Cdd:COG3883 167 EAAKAELEAQQAEQEAL-LAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1566-1927 |
2.17e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1566 LRIQLELNQVKSEIDRKIAEKDE-------EIDQLKRNhirvvesmQSTLDAEIRSRND-------AIRLKKKME---GD 1628
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYrlvemarELAELNEA--------ESDLEQDYQAASDhlnlvqtALRQQEKIEryqAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1629 LNEMEIQLNHSNRMAAEAlrnyrntQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKI 1708
Cdd:PRK04863 357 LEELEERLEEQNEVVEEA-------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1709 ---AEQELLDASERVQLLHTQNTSLINTKKKLETDISqiqgemedIVQEARNAEEKAKKAIT---------DAAMMAEEL 1776
Cdd:PRK04863 430 cglPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLS--------VAQAAHSQFEQAYQLVRkiagevsrsEAWDVAREL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1777 KKEQDTSAHLERMKKNLEQTVKDLQHRLDE---AEQLALKGGKKQIQKL-------------EARVRELEGEVENEQKRN 1840
Cdd:PRK04863 502 LRRLREQRHLAEQLQQLRMRLSELEQRLRQqqrAERLLAEFCKRLGKNLddedeleqlqeelEARLESLSESVSEARERR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1841 VEAIKGLRKHERRVKELTYQTEEdrknVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIA 1920
Cdd:PRK04863 582 MALRQQLEQLQARIQRLAARAPA----WLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQAL 657
|
....*..
gi 82524274 1921 ESQVNKL 1927
Cdd:PRK04863 658 DEEIERL 664
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1734-1921 |
2.19e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1734 KKKLETDISQIQGEMEDIVQEARN-AEEKAKKAITDAAMMAEELKKEQDtsahlermkknleqtvKDLQHRldeaeqlal 1812
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKeAEAIKKEALLEAKEEIHKLRNEFE----------------KELRER--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1813 kggKKQIQKLEARVRELEGEVENEQKRnveaikgLRKHERRVkeltyqtEEDRKNVLRLQDLVDKLQSKV-KAYKRQAEE 1891
Cdd:PRK12704 81 ---RNELQKLEKRLLQKEENLDRKLEL-------LEKREEEL-------EKKEKELEQKQQELEKKEEELeELIEEQLQE 143
|
170 180 190
....*....|....*....|....*....|
gi 82524274 1892 AEEQSNVNLAKFRKIQHELEEAEERADIAE 1921
Cdd:PRK12704 144 LERISGLTAEEAKEILLEKVEEEARHEAAV 173
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
847-1435 |
2.68e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 847 LKSAETEKEMANM-KEEFEKAKENLAK--AEAKRKELEEKMVALMQEKNDLQLQVQSEAD---SLADAEERCDQLIKTKI 920
Cdd:COG3096 457 VLELEQKLSVADAaRRQFEKAYELVCKiaGEVERSQAWQTARELLRRYRSQQALAQRLQQlraQLAELEQRLRQQQNAER 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 921 QLEA---KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVE---KEKHATENKVKNLTEEMAGLDE 994
Cdd:COG3096 537 LLEEfcqRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRariKELAARAPAWLAAQDALERLRE 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 995 TIAKLTKEKKALQEAHQQTLDD---LQAEEDKvntLTKAKIKLEQQVDDLE--GSLEQEKKIRM---------------- 1053
Cdd:COG3096 617 QSGEALADSQEVTAAMQQLLERereATVERDE---LAARKQALESQIERLSqpGGAEDPRLLALaerlggvllseiyddv 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1054 ----------------------DLERAKRKLEG------DLKLaqestmdVENDKQQLDEK-LKKKEFEMSNLqSKIEDE 1104
Cdd:COG3096 694 tledapyfsalygparhaivvpDLSAVKEQLAGledcpeDLYL-------IEGDPDSFDDSvFDAEELEDAVV-VKLSDR 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1105 Q----------ALGmqlqkkikelqarieeleeeieaerasRAKAEKQRSDLSRELEEISERLeeaggATSAqiemnkkr 1174
Cdd:COG3096 766 QwrysrfpevpLFG---------------------------RAAREKRLEELRAERDELAEQY-----AKAS-------- 805
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1175 eAEFQKMRR---DLEEATLQH---------EATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMeIDDLASNM 1242
Cdd:COG3096 806 -FDVQKLQRlhqAFSQFVGGHlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQL-LNKLLPQA 883
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1243 EVISKSkgNLEKMCRTLEDQVSELktkeEEQQRLINeltaqrgrlqtESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEEL 1322
Cdd:COG3096 884 NLLADE--TLADRLEELREELDAA----QEAQAFIQ-----------QHGKALAQLEPLVAVLQSDPEQFEQLQADYLQA 946
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1323 KRQLEEEIKAKSALAHALQSSRH------------DCDL---LREQYEEEQEAKAELQRAMSKANSEVAQW--------- 1378
Cdd:COG3096 947 KEQQRRLKQQIFALSEVVQRRPHfsyedavgllgeNSDLnekLRARLEQAEEARREAREQLRQAQAQYSQYnqvlaslks 1026
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 1379 --RTKYET--DAIQRTEELE-----EAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDL 1435
Cdd:COG3096 1027 srDAKQQTlqELEQELEELGvqadaEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSL 1092
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1662-1836 |
2.72e-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: 44.53 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1662 LHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKkkletDI 1741
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1742 SQIQGEMEDIVQEARNAEEKAKkaitdAAMMAEELKKEQdtsahLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQK 1821
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEIL-----ELMERIEELEEE-----LAELEAELAELEAELEEKKAELDE-ELAELEAELEE 160
|
170
....*....|....*
gi 82524274 1822 LEARVRELEGEVENE 1836
Cdd:COG1579 161 LEAEREELAAKIPPE 175
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1457-1756 |
2.89e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.05 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1457 DKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKI 1536
Cdd:PLN02939 113 NEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1537 KKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEidrKIAEKDeEIDQLKRNHIRVVESMQSTLDAEirsrn 1616
Cdd:PLN02939 193 KIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEE---NMLLKD-DIQFLKAELIEVAETEERVFKLE----- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1617 daiRLKKKMEGDLNEMEIQLNHSNrmaAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELR 1696
Cdd:PLN02939 264 ---KERSLLDASLRELESKFIVAQ---EDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLE 337
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 1697 ATLEQTERSR------KIAEQELLDASERVQLLHTQNTSLIntkKKLETDISQIQGEMEDIVQEAR 1756
Cdd:PLN02939 338 ASLKEANVSKfssykvELLQQKLKLLEERLQASDHEIHSYI---QLYQESIKEFQDTLSKLKEESK 400
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1456-1917 |
2.89e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1456 FDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEisdlTEQIAEGGKRIHELEK 1535
Cdd:TIGR00618 178 YTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ----TQQSHAYLTQKREAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1536 IKKQIEQEKSELQAALEEAEAslehEEGKILRIQLELNQVKSEIdrKIAEKDEEIDQLKRNHIRVVESMQSTLdaeiRSR 1615
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRA----QEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTELQSKM----RSR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1616 NDAIRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGIL-----KDTQLHLDDALRGQEDLKEQLAMVERRANLLQA 1690
Cdd:TIGR00618 324 AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATsireiSCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1691 EIEELRATLEQTERSRKIAEQELLDASERVQL---------LHTQNTSLINTKKKLE-TDISQIQGEMEDIVQEARNAEE 1760
Cdd:TIGR00618 404 ILQREQATIDTRTSAFRDLQGQLAHAKKQQELqqryaelcaAAITCTAQCEKLEKIHlQESAQSLKEREQQLQTKEQIHL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1761 KAKKAITDAAMMAEELKKEQdtsahLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKR- 1839
Cdd:TIGR00618 484 QETRKKAVVLARLLELQEEP-----CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQr 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1840 ------NVEAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEA 1913
Cdd:TIGR00618 559 aslkeqMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS 638
|
....
gi 82524274 1914 EERA 1917
Cdd:TIGR00618 639 QELA 642
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1740-1938 |
3.08e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1740 DISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEqlalkggkKQI 1819
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE--------KEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1820 QKLEARVRELEGEVEN------------------EQKRNVEAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSK 1881
Cdd:COG4942 93 AELRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 82524274 1882 VKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKI 1938
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
903-1113 |
3.64e-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: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 903 DSLADAEERCDQLIKTKIQLEAKIKEVTERAEdeeeinaELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV 982
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELE-------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 983 KNLTEEM----------------AGLDETIAKLTKEKKaLQEAHQQTLDDLQAEEDKvntLTKAKIKLEQQVDDLEGSLE 1046
Cdd:COG3883 89 GERARALyrsggsvsyldvllgsESFSDFLDRLSALSK-IADADADLLEELKADKAE---LEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 82524274 1047 QEKKIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQK 1113
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
850-1153 |
3.93e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.27 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 850 AETEKEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKIKEV 929
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 930 TERAE-------DEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAkltkE 1002
Cdd:pfam07888 156 KERAKkagaqrkEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEA----E 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1003 KKALQEAHQQTLDDLQAEEDKVNTLTKakikleqqvdDLEGSLEQEKKIRMDLERAKRKL-EGDLKLAQESTmdvendkq 1081
Cdd:pfam07888 232 NEALLEELRSLQERLNASERKVEGLGE----------ELSSMAAQRDRTQAELHQARLQAaQLTLQLADASL-------- 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 1082 QLDEKLKKKEFEMSNLQSKIEDE----QALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEI 1153
Cdd:pfam07888 294 ALREGRARWAQERETLQQSAEADkdriEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQEL 369
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1018-1289 |
4.76e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1018 QAEEDKVNTLTKAKIKLEQQVDDLEGSLEQekkirmdlerAKRKLEgDLKlAQESTMDVENDKQQLDEKLkkkefemSNL 1097
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEE----------AEAALE-EFR-QKNGLVDLSEEAKLLLQQL-------SEL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1098 QSKIEDEQAlgmqlqkkikelqarieeleeeieaerasrakaekQRSDLSRELEEISERLEEAGGATSAQIEmnkkrEAE 1177
Cdd:COG3206 225 ESQLAEARA-----------------------------------ELAEAEARLAALRAQLGSGPDALPELLQ-----SPV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1178 FQKMRRDLEEATLQHEATAATLRKKHADsVAELGEQIDNLQRVKQKlekeksEMKMEIDDLASNMEVISKSKGNLEKMCR 1257
Cdd:COG3206 265 IQQLRAQLAELEAELAELSARYTPNHPD-VIALRAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLA 337
|
250 260 270
....*....|....*....|....*....|..
gi 82524274 1258 TLEDQVSELKTKEEEQQRLINELTAQRGRLQT 1289
Cdd:COG3206 338 QLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1095-1375 |
4.97e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1095 SNLQSKIEDEQALGMQLQKKIKELQARIeeleeeieaerasrAKAEKQRSDLSRELEEISerLEEAGGATSAQIemnkkr 1174
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL--------------EEAEAALEEFRQKNGLVD--LSEEAKLLLQQL------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1175 eAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNlqRVKQKLEKEKSEMKMEIDDLAsnmeviSKSKGNLEK 1254
Cdd:COG3206 222 -SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELS------ARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1255 McRTLEDQVSELKTK-EEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRgKQaftQQIEELKRQLEeeikak 1333
Cdd:COG3206 293 V-IALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE-LE---AELRRLEREVE------ 361
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 82524274 1334 salahalqssrhdcdLLREQYEE--EQEAKAELQRAMSKANSEV 1375
Cdd:COG3206 362 ---------------VARELYESllQRLEEARLAEALTVGNVRV 390
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1674-1942 |
5.19e-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: 45.11 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1674 LKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKklETDISQIQGEMEDIVQ 1753
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQ--ERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1754 EARNAEEKAkkaitdaaMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEV 1833
Cdd:pfam17380 356 EERKRELER--------IRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1834 ENEQKRNVEAIKGLRKHERRVKELTYQTEEDRKNVLRL-QDLVDKLQSKVKAYKRQAE--EAEEQSnvnlakfRKIQHEL 1910
Cdd:pfam17380 428 EQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLrQQEEERKRKKLELEKEKRDrkRAEEQR-------RKILEKE 500
|
250 260 270
....*....|....*....|....*....|..
gi 82524274 1911 EEAEERADIAESQVNKLRVKSREVHTKIISEE 1942
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEE 532
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1499-1754 |
5.22e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1499 LDHLETLKRENKNLQQEISDLTEQIAEGGKRIH-----ELEKIKKQIEQEKSE----------LQAALEEAEASLEHEEG 1563
Cdd:pfam00038 17 IDKVRFLEQQNKLLETKISELRQKKGAEPSRLYslyekEIEDLRRQLDTLTVErarlqleldnLRLAAEDFRQKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1564 K---------ILRIQL-ELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRN-DAIRlKKKMEGDLNEM 1632
Cdd:pfam00038 97 LrtsaendlvGLRKDLdEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEmDAAR-KLDLTSALAEI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1633 EIQL-NHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQedlKEQLAMVERRANLLQAEIEELRATLEQTERSrkIAEQ 1711
Cdd:pfam00038 176 RAQYeEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSA---KEEITELRRTIQSLEIELQSLKKQKASLERQ--LAET 250
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 82524274 1712 ElldasERVQLLHTQNTSLINtkkKLETDISQIQGEMEDIVQE 1754
Cdd:pfam00038 251 E-----ERYELQLADYQELIS---ELEAELQETRQEMARQLRE 285
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
909-1051 |
5.64e-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: 44.24 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 909 EERCDQLIKTKIQLEAKIKEVTEraeDEEEINAELTakkrkledECSELKKDIDDLELTL-AKVEKEKHATENKVKNLTE 987
Cdd:smart00787 136 EWRMKLLEGLKEGLDENLEGLKE---DYKLLMKELE--------LLNSIKPKLRDRKDALeEELRQLKQLEDELEDCDPT 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82524274 988 EMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKI 1051
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGF 268
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1532-1827 |
6.02e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.21 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1532 ELEKIKKQIEQEKSElQAALEEAEasleheegkilriqlelnqvKSEIDRKI--AEKDEEIDQLKRNHIRVVESMQSTLD 1609
Cdd:NF012221 1543 QADAVSKHAKQDDAA-QNALADKE--------------------RAEADRQRleQEKQQQLAAISGSQSQLESTDQNALE 1601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1610 AEIRSRNDAI---------RLKKKMEGdLNEMEIQLNHsnrmAAEALRNYRN--TQGILKDTQLHLDDAlrgQEDLKEQL 1678
Cdd:NF012221 1602 TNGQAQRDAIleesravtkELTTLAQG-LDALDSQATY----AGESGDQWRNpfAGGLLDRVQEQLDDA---KKISGKQL 1673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1679 AMVERR--ANLLQAE--IEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDIS------QIQGEm 1748
Cdd:NF012221 1674 ADAKQRhvDNQQKVKdaVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANaaandaQSRGE- 1752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1749 edivQEARNAEEKAKKAITDA--AMMAEELKKEQD--TSAHLERMKKNLEQTVKDLQH---------------RLDEAEQ 1809
Cdd:NF012221 1753 ----QDASAAENKANQAQADAkgAKQDESDKPNRQgaAGSGLSGKAYSVEGVAEPGSHinpdspaaadgrfseGLTEQEQ 1828
|
330 340
....*....|....*....|
gi 82524274 1810 LALKGGKKQIQKLE--ARVR 1827
Cdd:NF012221 1829 EALEGATNAVNRLQinAGSR 1848
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1316-1590 |
6.29e-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: 44.63 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1316 TQQIEELKRQLEEEIKAksalahalqssrhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQwrTKYETDAIQRT-EELE 1394
Cdd:pfam05667 323 VETEEELQQQREEELEE-----------------LQEQLEDLESSIQELEKEIKKLESSIKQ--VEEELEELKEQnEELE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1395 EA---KKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEdlmidvertnAACAALDKKQRNFDKILAEWKQKYEETH 1471
Cdd:pfam05667 384 KQykvKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWE----------KHRVPLIEEYRALKEAKSNKEDESQRKL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1472 AELEASQKESRSLSTELfKIKnayEESLdhletlkrenKNLQQEISDLTEQIAEGG--KRIHElekIKKQIEQEKSELQA 1549
Cdd:pfam05667 454 EEIKELREKIKEVAEEA-KQK---EELY----------KQLVAEYERLPKDVSRSAytRRILE---IVKNIKKQKEEITK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 82524274 1550 ALEEAEAsleheegkilrIQLELNQVKSEIDRKIAEKDEEI 1590
Cdd:pfam05667 517 ILSDTKS-----------LQKEINSLTGKLDRTFTVTDELV 546
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1494-1711 |
6.37e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.68 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1494 AYEESLDHLETLKRENKNLQQEISDLTEQIAeggkrihELEKIK------KQIEQEKS------ELQAALEEAEASLEHE 1561
Cdd:COG0497 166 AWRALKKELEELRADEAERARELDLLRFQLE-------ELEAAAlqpgeeEELEEERRrlsnaeKLREALQEALEALSGG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1562 EGKILRIqleLNQVKSEIDRkIAEKDEEIDQLKRNhirvVESMQSTLD---AEIRSRNDAIrlkkkmEGD---LNEMEIQ 1635
Cdd:COG0497 239 EGGALDL---LGQALRALER-LAEYDPSLAELAER----LESALIELEeaaSELRRYLDSL------EFDperLEEVEER 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1636 LNHSNRMAaealRNYRNTqgilkdtqlhLDDALRGQEDLKEQLAMVERRANL---LQAEIEELRATLEQ-----TERSRK 1707
Cdd:COG0497 305 LALLRRLA----RKYGVT----------VEELLAYAEELRAELAELENSDERleeLEAELAEAEAELLEaaeklSAARKK 370
|
....
gi 82524274 1708 IAEQ 1711
Cdd:COG0497 371 AAKK 374
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1629-1928 |
6.42e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1629 LNEMEIQLnHSNRMAAEALRNYRNTQGILK-------------------DTQLHLDDALRGQEDL---KEQLAMVERRAN 1686
Cdd:PRK04863 232 FQDMEAAL-RENRMTLEAIRVTQSDRDLFKhlitestnyvaadymrhanERRVHLEEALELRRELytsRRQLAAEQYRLV 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1687 LLQAEIEELratleqtERSRKIAEQELLDASERVQLLhtqNTSLINTKKkletdISQIQGEMEDIVQEArnaeEKAKKAI 1766
Cdd:PRK04863 311 EMARELAEL-------NEAESDLEQDYQAASDHLNLV---QTALRQQEK-----IERYQADLEELEERL----EEQNEVV 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1767 TDAAMMAEELkKEQDTSAHLE--RMKKNLE--QTVKDLQHR-----------LDEAEQ------LALKGGKKQIQKLEAR 1825
Cdd:PRK04863 372 EEADEQQEEN-EARAEAAEEEvdELKSQLAdyQQALDVQQTraiqyqqavqaLERAKQlcglpdLTADNAEDWLEEFQAK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1826 VRELEGEV-ENEQKRNV-EAIKglRKHE------RRV-------------KELTYQTEEDRKNVLRLQDLVDKLQ----- 1879
Cdd:PRK04863 451 EQEATEELlSLEQKLSVaQAAH--SQFEqayqlvRKIagevsrseawdvaRELLRRLREQRHLAEQLQQLRMRLSeleqr 528
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 82524274 1880 -SKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLR 1928
Cdd:PRK04863 529 lRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1541-1784 |
6.62e-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: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1541 EQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDR---KIAEKDEEIDQLKRNhirvvesmQSTLDAEIRSRND 1617
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNElqaELEALQAEIDKLQAE--------IAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1618 AIrlkkkmegdlnemeiqlnhsNRMAAEALRNYRNTQGIlkdtqlhldDALRGQEDLKEQLamveRRANLLQAEIEELRA 1697
Cdd:COG3883 87 EL--------------------GERARALYRSGGSVSYL---------DVLLGSESFSDFL----DRLSALSKIADADAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1698 TLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELK 1777
Cdd:COG3883 134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
....*..
gi 82524274 1778 KEQDTSA 1784
Cdd:COG3883 214 AAAAAAA 220
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1210-1433 |
6.92e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1210 LGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEVISKSKG--NLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRL 1287
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1288 QtesgeysRQLDEKDSLVSQL--SRGKQAFTQQIEELKRQLEEeikaksalahalqssrhdcdlLREQYEEE----QEAK 1361
Cdd:COG3206 246 R-------AQLGSGPDALPELlqSPVIQQLRAQLAELEAELAE---------------------LSARYTPNhpdvIALR 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 82524274 1362 AELQRAMSKANSEVAQWRTKYETDAiqrtEELEEAKKKLAQRLQDAEEHVEAVNAKcaslEKTKQRLQNEVE 1433
Cdd:COG3206 298 AQIAALRAQLQQEAQRILASLEAEL----EALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVE 361
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1353-1557 |
7.81e-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: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1353 QYEEEQEAKAELQRAMSKANSEVAQWRTKYEtdaiqrteELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEV 1432
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE--------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1433 EDLMIDVERTNAA-------------------CAALDKKQRNFDKILAEwkqkYEETHAELEASQKESRSLSTELFKIKN 1493
Cdd:COG3883 89 GERARALYRSGGSvsyldvllgsesfsdfldrLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82524274 1494 AYEESLDHLETLKRENknlQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEAS 1557
Cdd:COG3883 165 ELEAAKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1002-1410 |
7.82e-04 |
|
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: 44.29 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1002 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEgdlkLAQESTMDVENDKQ 1081
Cdd:pfam05622 8 EKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLE----QLQEENFRLETARD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1082 QLDEKLKKKEFEMSNLQSKIEDEQALG---MQLQKKIKELQARIEELEEEIEAERASRAKAEkQRSDLSRELEEISER-- 1156
Cdd:pfam05622 84 DYRIKCEELEKEVLELQHRNEELTSLAeeaQALKDEMDILRESSDKVKKLEATVETYKKKLE-DLGDLRRQVKLLEERna 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1157 --------LEEA---GGATSAQIEMNKKREAEFQKMrrdLEEATLQHEATAATLRKKHadsvaelgEQIDNLQRVKQKLE 1225
Cdd:pfam05622 163 eymqrtlqLEEElkkANALRGQLETYKRQVQELHGK---LSEESKKADKLEFEYKKLE--------EKLEALQKEKERLI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1226 KEKSEMKMEIDDLASnMEVISKSKGNLEKMCRTLEDQVSELKTK------EEEQQRLINE----LTAQRGRLQTESGEYS 1295
Cdd:pfam05622 232 IERDTLRETNEELRC-AQLQQAELSQADALLSPSSDPGDNLAAEimpaeiREKLIRLQHEnkmlRLGQEGSYRERLTELQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1296 RQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAhalqSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEV 1375
Cdd:pfam05622 311 QLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQG----SKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQI 386
|
410 420 430
....*....|....*....|....*....|....*
gi 82524274 1376 AQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEH 1410
Cdd:pfam05622 387 EELEPKQDSNLAQKIDELQEALRKKDEDMKAMEER 421
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1304-1585 |
8.07e-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: 44.23 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1304 LVSQLSRGKQAFTQQIEELKRQLEEEI--KAKSALAHALQSSRHDCDLLREQYEE------EQEAKAELQRAMSKANSEV 1375
Cdd:NF033838 89 LNKKLSDIKTEYLYELNVLKEKSEAELtsKTKKELDAAFEQFKKDTLEPGKKVAEatkkveEAEKKAKDQKEEDRRNYPT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1376 AQWRT----KYETDAIQRTEELEEAKKKlAQRLQDaEEHVEAVNAKCASLEKTKQRLQNevedlmIDVERTNAAcaalDK 1451
Cdd:NF033838 169 NTYKTleleIAESDVEVKKAELELVKEE-AKEPRD-EEKIKQAKAKVESKKAEATRLEK------IKTDREKAE----EE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1452 KQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELF---KIKNAYEESLDHL--ETLKRENKNLQQEISDLTEQIAEG 1526
Cdd:NF033838 237 AKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPAtpdKKENDAKSSDSSVgeETLPSPSLKPEKKVAEAEKKVEEA 316
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82524274 1527 GKRIHELEK---------IKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAE 1585
Cdd:NF033838 317 KKKAKDQKEedrrnyptnTYKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAE 384
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1081-1243 |
8.21e-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: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1081 QQLDEKLKKKEFEMSNLQSKIEDeqalgmqLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEA 1160
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1161 GG-----ATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEI 1235
Cdd:COG1579 86 RNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*...
gi 82524274 1236 DDLASNME 1243
Cdd:COG1579 166 EELAAKIP 173
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1666-1862 |
8.36e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1666 DALRGQEDLKEQLAmverranLLQAEIEELRATLEQTERSRKI----------AEQELLDASERVQLLHTQNTSLINTK- 1734
Cdd:PRK11281 46 DALNKQKLLEAEDK-------LVQQDLEQTLALLDKIDRQKEEteqlkqqlaqAPAKLRQAQAELEALKDDNDEETRETl 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1735 -----KKLETDISQIQGEMEDiVQEA-----------RNAEEKAKKAITDAAMMAEE----LKKEQDTSAHL---ERMKK 1791
Cdd:PRK11281 119 stlslRQLESRLAQTLDQLQN-AQNDlaeynsqlvslQTQPERAQAALYANSQRLQQirnlLKGGKVGGKALrpsQRVLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1792 NLEQTVKDLQHRLdeaEQLALKG-------GKKQIQKLEARVRELEGEVENEQkrnvEAI--KGLRKHERRVKELTYQTE 1862
Cdd:PRK11281 198 QAEQALLNAQNDL---QRKSLEGntqlqdlLQKQRDYLTARIQRLEHQLQLLQ----EAInsKRLTLSEKTVQEAQSQDE 270
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1425-1715 |
8.94e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1425 KQRLQNEVEDLMIDVERTNAACAALDKKQRNFDK---ILAEWKQKYEETHAELEASQKESRslstelfkiknayeesldh 1501
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEER------------------- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1502 letlKRENKNLQQEisdlteQIAEGGKRIHELEKIKKQIEQEKSELQAALEEAEASLEHEEgkilriqlelnqvksEIDR 1581
Cdd:pfam17380 359 ----KRELERIRQE------EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEE---------------ERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1582 KIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKkkmegdlnEMEIQlnhsnrMAAEALRNYRNTQgilKDTQ 1661
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE--------EQERQ------QQVERLRQQEEER---KRKK 476
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 82524274 1662 LHLDDALRGQEDLKEQlamverRANLLQAEIEELRATLEQTERSRKIAEQELLD 1715
Cdd:pfam17380 477 LELEKEKRDRKRAEEQ------RRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
809-1915 |
9.41e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.44 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 809 QKMVERRESIFCIQYNVRAfMNVKHWPWMKLYFKIKPLLKSAETEKEMANMKEEFEKAKENLAkaeakrKELEEKMVALM 888
Cdd:PTZ00440 316 KKIEKGKEYIKRIQNNNIP-PQVKKDELKKKYFESAKHYASFKFSLEMLSMLDSLLIKKEKIL------NNLFNKLFGDL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 889 QEKndlqlqvqseADSLADAEercdQLIKTKIQLEAKIKEVTERAEDEEEINAELTAK-KRKLEDECSELKKDIDDLELT 967
Cdd:PTZ00440 389 KEK----------IETLLDSE----YFISKYTNIISLSEHTLKAAEDVLKENSQKIADyALYSNLEIIEIKKKYDEKINE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 968 LAKvekekhaTENKVKNLTEEMAGLDETIaklTKEKKALQEAHQQTLDDLQAEEdKVNTLTKAKIKLEQQVDDLEGSLEQ 1047
Cdd:PTZ00440 455 LKK-------SINQLKTLISIMKSFYDLI---ISEKDSMDSKEKKESSDSNYQE-KVDELLQIINSIKEKNNIVNNNFKN 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1048 EKKIRMDLERAKRKLEGDLKLaqestmdVENDKQQLdEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEE 1127
Cdd:PTZ00440 524 IEDYYITIEGLKNEIEGLIEL-------IKYYLQSI-ETLIKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDN 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1128 EIEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqieMNKKREAEFQKMRRDLEEATLQHEATAatlrkKHADSV 1207
Cdd:PTZ00440 596 IIQQIEELINEALFNKEKFINEKNDLQEKVKYI---------LNKFYKGDLQELLDELSHFLDDHKYLY-----HEAKSK 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1208 AELGEQIDNLQRVKQKLEKEKSEmkmEIDDLASNMEVISKSKGNLEKmcRTLEDQVSELKTkeeEQQRLINELTAQRGRL 1287
Cdd:PTZ00440 662 EDLQTLLNTSKNEYEKLEFMKSD---NIDNIIKNLKKELQNLLSLKE--NIIKKQLNNIEQ---DISNSLNQYTIKYNDL 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1288 QTESGEYSRQldekdslvsqlsrgkqafTQQIEELKRQLeeeIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRA 1367
Cdd:PTZ00440 734 KSSIEEYKEE------------------EEKLEVYKHQI---INRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNK 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1368 MSKANSEV---------AQWRTKYETDAIQRTE-ELEEAKKKLAQRLQDAEEHVEavNAKCASLEKTKQRLQNEVEDLMI 1437
Cdd:PTZ00440 793 ENKISNDInilkenkknNQDLLNSYNILIQKLEaHTEKNDEELKQLLQKFPTEDE--NLNLKELEKEFNENNQIVDNIIK 870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1438 DVERTNAACAALdkKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKN--AYEESLDHLETLKRENKNLQQE 1515
Cdd:PTZ00440 871 DIENMNKNINII--KTLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINTDNiiQKNEKLNLLNNLNKEKEKIEKQ 948
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1516 ISDltEQIAEGGKRIHE-LEKIKKQIEQEKSELQAALEEAEA---SLEHEEGKILRIQLELN---------------QVK 1576
Cdd:PTZ00440 949 LSD--TKINNLKMQIEKtLEYYDKSKENINGNDGTHLEKLDKekdEWEHFKSEIDKLNVNYNilnkkiddlikkqhdDII 1026
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1577 SEIDRKIAEKDEEIDQLKRNHIRVVESMQSTL-----------DAEIRSRNDAIRLKKKMEGDLNEMEIQLNHSNRMAAE 1645
Cdd:PTZ00440 1027 ELIDKLIKEKGKEIEEKVDQYISLLEKMKTKLssfhfnidikkYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNK 1106
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1646 ALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANllqaEIEELRATLEQTERSRKIAEQELLDasERVQLLHT 1725
Cdd:PTZ00440 1107 SHEHVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELE----NMNLEDITLNEVNEIEIEYERILID--HIVEQINN 1180
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1726 QNTSLINTKKKLETDISQIQGEMEDIVQEARN-AEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQhRL 1804
Cdd:PTZ00440 1181 EAKKSKTIMEEIESYKKDIDQVKKNMSKERNDhLTTFEYNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELK-EI 1259
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1805 DEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNVEAI-KGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVK 1883
Cdd:PTZ00440 1260 KLQVFSYLQQVIKENNKMENALHEIKNMYEFLISIDSEKIlKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAK 1339
|
1130 1140 1150
....*....|....*....|....*....|....
gi 82524274 1884 AYKRQAEEAEE--QSNVNLAKFRKIQHELEEAEE 1915
Cdd:PTZ00440 1340 EHKNKIYGSLEdkQIDDEIKKIEQIKEEISNKRK 1373
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
846-1158 |
1.15e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 846 LLKSAETEKEMANMKEEFEKAKENLAKAEAKRKELEekmvalmQEKNDLQlqvqseaDSLADAEERCDQLIKTKIQLEAK 925
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQ-------QERDELA-------DEIASGASGKSALQDEKRRLEAR 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 926 IKEVTERAEdEEEINAELTAKKRKledecselkkdiddleltlakvekekhATENKVKNLTEEMAGLDETIAKLTKEKKA 1005
Cdd:pfam01576 891 IAQLEEELE-EEQSNTELLNDRLR---------------------------KSTLQVEQLTTELAAERSTSQKSESARQQ 942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1006 LQEAHQQTLDDLQAEEDKVNTLTKAKIK-LEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKlaqESTMDVENDKQQLD 1084
Cdd:pfam01576 943 LERQNKELKAKLQEMEGTVKSKFKSSIAaLEAKIAQLEEQLEQESRERQAANKLVRRTEKKLK---EVLLQVEDERRHAD 1019
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82524274 1085 EklKKKEFEMSNLQSKiedeqalgmQLQKKIKELQarieeleeeieaERASRAKAekQRSDLSRELEEISERLE 1158
Cdd:pfam01576 1020 Q--YKDQAEKGNSRMK---------QLKRQLEEAE------------EEASRANA--ARRKLQRELDDATESNE 1068
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1786-1911 |
1.35e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1786 LERMKK-NLEQTVKDLQHRLDEAEQL------ALKGGKKQIQKLEARVRELEGEVENEQKRNVEAIkglrkheRRVKELT 1858
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEAErsrlqaLLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 82524274 1859 YQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNVNLAkfRKIQhELE 1911
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALA--QRVQ-ELN 193
|
|
| COG6 |
smart01087 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
1379-1514 |
1.46e-03 |
|
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.
Pssm-ID: 215018 Cd Length: 598 Bit Score: 43.46 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1379 RTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQrnfdK 1458
Cdd:smart01087 9 RSDLEKRLLKINGEFLSEFKPVAEQLQRLSEDVQKLNNSCDSMKDQLNTAKNQTQDLISEASELQEELALLELKK----K 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 1459 ILAEWKQKYEETHAELEASQKESRSLSTELFKIknayeesLDHLETLKRENKNLQQ 1514
Cdd:smart01087 85 LLDAFLSKFTLSQDELDVLTSREGPIDDEFFQV-------LDKVQEIHEDCSVLLQ 133
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
1150-1368 |
1.51e-03 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 43.41 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1150 LEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLrkKHADSVAE-LGEQIDNLQRVKQKLEKEK 1228
Cdd:PRK15374 101 LSQLESRLAVWQAMIESQKEMGIQVSKEFQTALGEAQEATDLYEASIKKT--DTAKSVYDaAEKKLTQAQNKLQSLDPAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1229 SEMKMEIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQqrlINELTAQRGRLQTESGEYSRQlDEKDSLvSQL 1308
Cdd:PRK15374 179 PGYAQAEAAVEQAGKEATEAKEALDKATDATVKAGTDAKAKAEKA---DNILTKFQGTANAASQNQVSQ-GEQDNL-SNV 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 82524274 1309 SRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRH-DCDLLREQYEEEQEAKAELQRAM 1368
Cdd:PRK15374 254 ARLTMLMAMFIEIVGKNTEESLQNDLALFNALQEGRQaEMEKKSAEFQEETRKAEETNRIM 314
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
859-1005 |
1.56e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 42.83 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 859 MKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAeercdQLIKTKI-QLEAKIKEVTERAEdee 937
Cdd:pfam10186 17 ARNRLYELRVDLARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKL-----RLLKSEVaISNERLNEIKDKLD--- 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82524274 938 EINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKA 1005
Cdd:pfam10186 89 QLRREIAEKKKKIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRS 156
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1314-1726 |
1.66e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1314 AFTQQIEELKRQLEEEIKAKSALAHAlqssrhdcdllREQYEEEQEAKAELQRAMskansevaqwrtkyetdaiqrtEEL 1393
Cdd:PRK04863 273 DYMRHANERRVHLEEALELRRELYTS-----------RRQLAAEQYRLVEMAREL----------------------AEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1394 EEAKKKLAQRLQDAEEHVEAVNAKCASLEKTkQRLQNEVEDLMIDVERTNAACAALDKKQrnfdkilaewkqkyEETHAE 1473
Cdd:PRK04863 320 NEAESDLEQDYQAASDHLNLVQTALRQQEKI-ERYQADLEELEERLEEQNEVVEEADEQQ--------------EENEAR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1474 LEASQKESRSLSTELFKiknaYEESLDHLETLKRENKNLQQ---------EISDLTEQIAEGgkRIHELEKIKKQIEQEK 1544
Cdd:PRK04863 385 AEAAEEEVDELKSQLAD----YQQALDVQQTRAIQYQQAVQalerakqlcGLPDLTADNAED--WLEEFQAKEQEATEEL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1545 SELQAALEEAEASLE-HEEGKILriqleLNQVKSEIDRKIAEkdeeidqlkrnhirvvESMQSTLDAEIRSRNDAIRLKK 1623
Cdd:PRK04863 459 LSLEQKLSVAQAAHSqFEQAYQL-----VRKIAGEVSRSEAW----------------DVARELLRRLREQRHLAEQLQQ 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1624 kMEGDLNEMEiQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQ----EDLKEQLAMVERRANLLQAEIEELRAtl 1699
Cdd:PRK04863 518 -LRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELearlESLSESVSEARERRMALRQQLEQLQA-- 593
|
410 420
....*....|....*....|....*..
gi 82524274 1700 eQTERSRKIAeQELLDASERVQLLHTQ 1726
Cdd:PRK04863 594 -RIQRLAARA-PAWLAAQDALARLREQ 618
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1247-1329 |
1.91e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 41.07 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1247 KSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQ---IEELK 1323
Cdd:pfam08614 71 RSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQlnmAEEKL 150
|
....*.
gi 82524274 1324 RQLEEE 1329
Cdd:pfam08614 151 RKLEKE 156
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1395-1749 |
1.94e-03 |
|
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: 42.92 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1395 EAKKKLA---QRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMidvertnaacaaldKKQRNFDKILAEWKQKYEETH 1471
Cdd:pfam06160 83 KAKKALDeieELLDDIEEDIKQILEELDELLESEEKNREEVEELK--------------DKYRELRKTLLANRFSYGPAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1472 AELEASQKESRSLSTELFKIKNA--YEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHE-LEKIK----------- 1537
Cdd:pfam06160 149 DELEKQLAEIEEEFSQFEELTESgdYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDqLEELKegyremeeegy 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1538 ----KQIEQEKSELQAALEEAEASLEheegkilriQLELNQVKSEIDrkiaEKDEEIDQLkrnhirvvesmQSTLDAEIR 1613
Cdd:pfam06160 229 alehLNVDKEIQQLEEQLEENLALLE---------NLELDEAEEALE----EIEERIDQL-----------YDLLEKEVD 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1614 SRNDAIRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYrntqgILKDTQLHLddalrgQEDLKEQLAMVERRANLLQAEIE 1693
Cdd:pfam06160 285 AKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSY-----TLNENELER------VRGLEKQLEELEKRYDEIVERLE 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 82524274 1694 -------ELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEME 1749
Cdd:pfam06160 354 ekevaysELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
1492-1714 |
1.97e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 42.25 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1492 KNAYEESLDHLETLKRENKNLQQEISDLTEQIAEG-----------GKRIHELEKI-KKQIEQEKSELQ-------AALE 1552
Cdd:pfam15397 5 RTSLEELKKHEDFLTKLNLELIKAIQDTEDSTALKvrkllqqyekfGTIISILEYSnKKQLQQAKAELQeweekeeSKLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1553 EAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDaeirsrndaiRLKKKMEGDLNEM 1632
Cdd:pfam15397 85 KLEQQLEQLNAKIQKTQEELNFLSTYKDKEYPVKAVQIANLVRQLQQLKDSQQDELD----------ELEEMRRMVLESL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1633 E--IQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRAtleQTERSRKIAE 1710
Cdd:pfam15397 155 SrkIQKKKEKILSSLAEKTLSPYQESLLQKTRDNQVMLKEIEQFREFIDELEEEIPKLKAEVQQLQA---QRQEPREVIF 231
|
....
gi 82524274 1711 QELL 1714
Cdd:pfam15397 232 ADVL 235
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
860-1071 |
1.97e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 860 KEEFEKAkENLAKAEAKRKELEEKMVA-----LMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKIKEVTERAE 934
Cdd:PRK05035 464 REKAARE-ARHKKAAEARAAKDKDAVAaalarVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAA 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 935 DEEE---INAELT---AKKRKLEDECSELKKDIDD----LELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKL----- 999
Cdd:PRK05035 543 ADPKkaaVAAAIArakAKKAAQQAANAEAEEEVDPkkaaVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVaaaia 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82524274 1000 -TKEKKALQEAHQQTLDDLQAEEDKVNT-LTKAKIKLEQQVDDLEGSLEQEK----KIRMDLERAKRKlegdlKLAQE 1071
Cdd:PRK05035 623 rAKAKKAEQQANAEPEEPVDPRKAAVAAaIARAKARKAAQQQANAEPEEAEDpkkaAVAAAIARAKAK-----KAAQQ 695
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
981-1242 |
1.98e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 981 KVKNLTEEMAGLDETIaKLTKEKKALQEAHQQTLDDLQAE-----EDKVNTLTKAKIKLEQQVDDLEgslEQEKKIRMDL 1055
Cdd:PHA02562 175 KIRELNQQIQTLDMKI-DHIQQQIKTYNKNIEEQRKKNGEniarkQNKYDELVEEAKTIKAEIEELT---DELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1056 ErakrKLEGDLKLAQESTMDVENDKQQL--DEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQarieeleeeieaer 1133
Cdd:PHA02562 251 E----DPSAALNKLNTAAAKIKSKIEQFqkVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQ-------------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1134 asrakaeKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEAtLQHEATAATLRKKHADSVAELGEQ 1213
Cdd:PHA02562 313 -------HSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKA-KKVKAAIEELQAEFVDNAEELAKL 384
|
250 260 270
....*....|....*....|....*....|.
gi 82524274 1214 IDNLQrvkqKLEKEKSEMKMEID--DLASNM 1242
Cdd:PHA02562 385 QDELD----KIVKTKSELVKEKYhrGIVTDL 411
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1081-1437 |
2.00e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1081 QQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEea 1160
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKD-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1161 ggATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQID---NLQRVKQKLEKEKSEMKMEIDD 1237
Cdd:pfam07888 119 --ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAerkQLQAKLQQTEEELRSLSKEFQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1238 LASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQ 1317
Cdd:pfam07888 197 LRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1318 ---QIEELKRQLEEeikAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYEtdaiqrTEELE 1394
Cdd:pfam07888 277 arlQAAQLTLQLAD---ASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMERE------KLEVE 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 82524274 1395 EAKKKLAQRLQDAEEHVEAVNAKCA--SLEKTKQRLQNEVEDLMI 1437
Cdd:pfam07888 348 LGREKDCNRVQLSESRRELQELKASlrVAQKEKEQLQAEKQELLE 392
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1391-1926 |
2.07e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 43.09 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1391 EELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKqrlqNEVEDLMIDVERtnaacAALDKKQRNFDKILAewKQKYEET 1470
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTK----RLIEELKLNLER-----AQTEEAQAKQDSELA--KLRVEEM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1471 haELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQEKSELQAA 1550
Cdd:pfam05701 111 --EQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1551 LEEAEASLE------HE-EGKILRIQLELNQVKSEIDRKIAEKDEEIDQLkRNHIRVVESMQSTLDAeirsrndAIRLKK 1623
Cdd:pfam05701 189 LIATKESLEsahaahLEaEEHRIGAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-------ASALLL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1624 KMEGDLNE-MEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLddalrgqEDLKEQLAMVERRANLLQAEIEELRATLEQt 1702
Cdd:pfam05701 261 DLKAELAAyMESKLKEEADGEGNEKKTSTSIQAALASAKKEL-------EEVKANIEKAKDEVNCLRVAAASLRSELEK- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1703 ersrkiaEQELLDaservqllhtqntSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAitdAAMMAEELKKEQDT 1782
Cdd:pfam05701 333 -------EKAELA-------------SLRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEA---REKMVELPKQLQQA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1783 SAHLERMKKNLEQTVKDLQHRLDEAEQLalKGGKKQIQ-KLEARVRELEGEVENEqKRNVEAIKGLRKHER--------- 1852
Cdd:pfam05701 390 AQEAEEAKSLAQAAREELRKAKEEAEQA--KAAASTVEsRLEAVLKEIEAAKASE-KLALAAIKALQESESsaestnqed 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 82524274 1853 RVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNK 1926
Cdd:pfam05701 467 SPRGVTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIALEKAEK 540
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1657-1892 |
2.17e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1657 LKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKK 1736
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1737 LETDISQIqgemeDIVQEARNAEEkakkAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLAlkggk 1816
Cdd:COG3883 98 SGGSVSYL-----DVLLGSESFSD----FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK----- 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 1817 kqiQKLEARVRELEGEVENEQKRNVEAIKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEA 1892
Cdd:COG3883 164 ---AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1318-1557 |
2.22e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1318 QIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQwrtkyetdaiqRTEELEEAK 1397
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-----------AEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1398 KKLAQRLQDAEEHVEAVNA---------------KCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNfdkiLAE 1462
Cdd:COG3883 86 EELGERARALYRSGGSVSYldvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1463 WKQKYEETHAELEASQKESRSLstelfkiknayeesldhLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQIEQ 1542
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEAL-----------------LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
250
....*....|....*
gi 82524274 1543 EKSELQAALEEAEAS 1557
Cdd:COG3883 225 AAAAAAAAAAAAAAA 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
842-1063 |
2.42e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 842 KIKPLLKSAETEKEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQ 921
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 922 LEAKIKEVTERAEDEEEInAELTAKKRKLEDECSELKKDIDDleltLAKVEKEKhatENKVKNLTEEMAGLDETIAKLTK 1001
Cdd:PRK02224 577 LNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREA----LAELNDER---RERLAEKRERKRELEAEFDEARI 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 82524274 1002 EKkaLQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLE 1063
Cdd:PRK02224 649 EE--AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVE 708
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
854-1050 |
2.59e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 854 KEMANMKEEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEA--------- 924
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKaadesergr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 925 KIKEVTERAEDE--EEINAELTAKKRKLED---ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKL 999
Cdd:pfam00261 81 KVLENRALKDEEkmEILEAQLKEAKEIAEEadrKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 82524274 1000 -TKEKKALQ------EAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKK 1050
Cdd:pfam00261 161 eASEEKASEredkyeEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1260-1486 |
2.62e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1260 EDQVSELKTKEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHA 1339
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1340 LQSSRHDCDLLR--------EQYEEEQEAKAELQRAMSKANSEVAQWRTKYE---TDAIQRTEELEEAKKKLAQRLQDAE 1408
Cdd:COG3883 95 LYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEakkAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82524274 1409 EHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKESRSLST 1486
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1169-1580 |
2.66e-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: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1169 EMNKKREAEFQ-----------KMRRDLEEATLQHEATaaTLRKKHADSVAELGEQidnLQRVKQKLEKEKSEMKM---- 1233
Cdd:pfam15818 15 ELRMRREAETQyeeqigkiiveTQELKWQKETLQNQKE--TLAKQHKEAMAVFKKQ---LQMKMCALEEEKGKYQLatei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1234 ---EIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINE-------LTAQRGRLQTESGEYSRQLDEKDS 1303
Cdd:pfam15818 90 kekEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNEiekyyatITGQFGLVKENHGKLEQNVQEAIQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1304 LVSQLSRGKQAFTQQI----EELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEaKAELQRAMSKANSEvaqwr 1379
Cdd:pfam15818 170 LNKRLSALNKKQESEIcslkKELKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQELQE-RLNMELELNKKINE----- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1380 tkyETDAIQrtEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKI 1459
Cdd:pfam15818 244 ---EITHIQ--EEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1460 LAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQ 1539
Cdd:pfam15818 319 LGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNVPEVNNENSEMSTEKSENLIIQKYNSE 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 82524274 1540 IEQEK-------SELQAALEEAEASLEHEEGKILRIQLELNQVKSEID 1580
Cdd:pfam15818 399 QEIREentksfcSDTEYRETEKKKGPPVEEIIIEDLQVLEKSFKNEID 446
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1542-1914 |
2.84e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1542 QEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHI----------RVVESMQSTLDAE 1611
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEeleekykelsASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1612 IRSRNDAIRLKKKMEGDLNEMeiqlnhSNRMAAEALRNYRntqgiLKDTQLHLDDALRGQEDLKEQLamverRANLLQAE 1691
Cdd:pfam07888 121 LAQRAAHEARIRELEEDIKTL------TQRVLERETELER-----MKERAKKAGAQRKEEEAERKQL-----QAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1692 IEELRATLEQTERSRKIAEQElldaserVQLLHTQNTslINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAM 1771
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRD-------TQVLQLQDT--ITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1772 MAEELKK--EQDTSAHLERMKKNLEqtVKDLQHRLDEAeQLALKGGKKQ-IQKLEARVRELEGEVENEQKRNVEAIKglr 1848
Cdd:pfam07888 256 LGEELSSmaAQRDRTQAELHQARLQ--AAQLTLQLADA-SLALREGRARwAQERETLQQSAEADKDRIEKLSAELQR--- 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 1849 kherrvKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAE 1914
Cdd:pfam07888 330 ------LEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQE 389
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
848-1005 |
2.97e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 848 KSAETEKEMA--NMKEEFEKAKENLAK-AEAKRKELEEKMVALMQEKNDLQlqvqseaDSLADAEERCDQLIKTKIQLEA 924
Cdd:PRK12704 49 KEAEAIKKEAllEAKEEIHKLRNEFEKeLRERRNELQKLEKRLLQKEENLD-------RKLELLEKREEELEKKEKELEQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 925 KIKEVTERAEDEEEINAELtakKRKLEdECSELKKDiDDLELTLAKVEKE-KHATENKVKNLTEEmagldetiAKLTKEK 1003
Cdd:PRK12704 122 KQQELEKKEEELEELIEEQ---LQELE-RISGLTAE-EAKEILLEKVEEEaRHEAAVLIKEIEEE--------AKEEADK 188
|
..
gi 82524274 1004 KA 1005
Cdd:PRK12704 189 KA 190
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
866-1073 |
3.11e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 866 AKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTA 945
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 946 KKRKLEDECSELK-----KDIDDLeltLAKVEKEKHATENKvknlTEEMAGLDETIAKLTKEKKALQEAhQQTLDDLQAE 1020
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsESFSDF---LDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAK-LAELEALKAE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 82524274 1021 -EDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQEST 1073
Cdd:COG3883 166 lEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| EcCorA_ZntB-like |
cd12821 |
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily ... |
1302-1414 |
3.32e-03 |
|
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. Members of this family are found in all three kingdoms of life. It is a functionally diverse family, including the Mg2+ transporters Escherichia coli and Salmonella typhimurium CorAs (which can also transport Co2+, and Ni2+ ), and the Zn2+ transporter Salmonella typhimurium ZntB which mediates the efflux of Zn2+ (and Cd2+). It also includes two Saccharomyces cerevisiae members: the inner membrane Mg2+ transporters Mfm1p/Lpe10p, and Mrs2p, and a family of Arabidopsis thaliana members (AtMGTs) some of which are localized to distinct tissues, and not all of which can transport Mg2+. Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport.
Pssm-ID: 213355 [Multi-domain] Cd Length: 285 Bit Score: 41.53 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1302 DSLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSaLAHALqSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEvaQWRTK 1381
Cdd:cd12821 110 GAIIKALLTGIDQFEEKLEELEWDLLEGNNAIK-LDRIL-ELRRELLRLTNLIEPQQEVLMALQEAFAELLFS--EDEEE 185
|
90 100 110
....*....|....*....|....*....|...
gi 82524274 1382 YEtDAIQRTEELEEAKKKLAQRLQDAEEHVEAV 1414
Cdd:cd12821 186 LR-RTLDRIERLLQLIEEYEQELDTLQDIEEVV 217
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1142-1337 |
3.57e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1142 QRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVK 1221
Cdd:PHA02562 182 QIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLN 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1222 QKLEKEKSEMKM-------------------EIDDLASNMEVISKSKGNLEKMCRTLEDQVSELKTKEEEQQRLINELTA 1282
Cdd:PHA02562 262 TAAAKIKSKIEQfqkvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 82524274 1283 QRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAF---TQQIEELKRQLEEEIKAKSALA 1337
Cdd:PHA02562 342 LKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvdnAEELAKLQDELDKIVKTKSELV 399
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
955-1224 |
4.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 955 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKL 1034
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1035 EQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKKEFEMSNLQSKIED------EQALG 1108
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlseaeaEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1109 MQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEA 1188
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270
....*....|....*....|....*....|....*.
gi 82524274 1189 TLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKL 1224
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
861-1180 |
4.33e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 861 EEFEKAKENLAKAEAKRKELEEKMVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEIN 940
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 941 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKalqeahQQTLDDLQAE 1020
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA------EQALDELLKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1021 EDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDVENDKQQLDEKLKKKEFEMSNLQSK 1100
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1101 IEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQK 1180
Cdd:COG4372 272 DTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLL 351
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1313-1480 |
4.40e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1313 QAFTQQIEELKRQLEEEIKAKSALAHALQSsrhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKyetdaiqrtee 1392
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEAR----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1393 LEEAKKKLAQrLQDAEEhVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKYEETHA 1472
Cdd:COG1579 75 IKKYEEQLGN-VRNNKE-YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
....*...
gi 82524274 1473 ELEASQKE 1480
Cdd:COG1579 153 ELEAELEE 160
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1038-1519 |
4.45e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1038 VDDLEGSLeqeKKIRMDLE--RAKRKLEGDLK-LAQEST-------MDVENDKQQLDEKLKKKEFEMSNLQSKIEDEQAL 1107
Cdd:PRK04863 232 FQDMEAAL---RENRMTLEaiRVTQSDRDLFKhLITESTnyvaadyMRHANERRVHLEEALELRRELYTSRRQLAAEQYR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1108 GMQLQKKIKELQARIEELEEEIEAERASRAK---AEKQRSDLSR---ELEEISERLEEAGGATSAQIEMNKKREAEFqkm 1181
Cdd:PRK04863 309 LVEMARELAELNEAESDLEQDYQAASDHLNLvqtALRQQEKIERyqaDLEELEERLEEQNEVVEEADEQQEENEARA--- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1182 rrdlEEATLQHEATAATLrkkhADSVAELGEQ---IDNLQRVKQKLEKEKSemKMEIDDLAsnmeviskskgnLEKmcrt 1258
Cdd:PRK04863 386 ----EAAEEEVDELKSQL----ADYQQALDVQqtrAIQYQQAVQALERAKQ--LCGLPDLT------------ADN---- 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1259 LEDQVSELKTKEEEQQRLINELtAQRGRLqteSGEYSRQLDEKDSLVSQLSRG---KQAFtQQIEELKRQLEEEiKAKSA 1335
Cdd:PRK04863 440 AEDWLEEFQAKEQEATEELLSL-EQKLSV---AQAAHSQFEQAYQLVRKIAGEvsrSEAW-DVARELLRRLREQ-RHLAE 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1336 LAHALQSSRHDcdlLREQYEEEQEAKAELQRAMSKANSEVaqwrtkyetdaiQRTEELEEAKKKLAQRLQDAEEHVEAVN 1415
Cdd:PRK04863 514 QLQQLRMRLSE---LEQRLRQQQRAERLLAEFCKRLGKNL------------DDEDELEQLQEELEARLESLSESVSEAR 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1416 AKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDkkqrnfdkilaewkQKYEETHAELEASQKESRSLSTELFKIKNAY 1495
Cdd:PRK04863 579 ERRMALRQQLEQLQARIQRLAARAPAWLAAQDALA--------------RLREQSGEEFEDSQDVTEYMQQLLERERELT 644
|
490 500
....*....|....*....|....
gi 82524274 1496 EESlDHLETLKREnknLQQEISDL 1519
Cdd:PRK04863 645 VER-DELAARKQA---LDEEIERL 664
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1460-1741 |
4.60e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1460 LAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQ 1539
Cdd:COG4372 61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1540 IEQEKSELQAALEEAEASLEHEEGKILRIQLELNQvkseidRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAI 1619
Cdd:COG4372 141 LQSEIAEREEELKELEEQLESLQEELAALEQELQA------LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1620 RLKKKMEGDLNEMEIQLNhsnrmAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATL 1699
Cdd:COG4372 215 ELAEELLEAKDSLEAKLG-----LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 82524274 1700 EQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDI 1741
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
916-1184 |
4.73e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 916 IKTKIQLEaKIKEVTERAED--------EEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEkhatenkVKNLTE 987
Cdd:PRK05771 36 LKEELSNE-RLRKLRSLLTKlsealdklRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKE-------IKELEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 988 EMAGLDETIAKLTKEKKALQ--EAHQQTLDDLQAEED---KVNTLTKAKIKLEQQVDDLEGSLEqekkirmdlerAKRKL 1062
Cdd:PRK05771 108 EISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvFVGTVPEDKLEELKLESDVENVEY-----------ISTDK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1063 EGDLKLAqestMDVENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGmQLQKKIKELqarieeleeeieaerasrakaEKQ 1142
Cdd:PRK05771 177 GYVYVVV----VVLKELSDEVEEELKKLGFERLELEEEGTPSELIR-EIKEELEEI---------------------EKE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 82524274 1143 RSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRD 1184
Cdd:PRK05771 231 RESLLEELKELAKKYLEELLALYEYLEIELERAEALSKFLKT 272
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1584-1930 |
4.74e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 42.23 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1584 AEKDEEIDQLKR-----NHIRVVESMQStldaeiRSRNDAI-RLKKKMEGDL------NEMEIQLNHSNRMAAEAlrnYR 1651
Cdd:PLN03188 887 TKQASEITQLNRlvqqyKHERECNAIIG------QTREDKIiRLESLMDGVLskedflEEELASLMHEHKLLKEK---YE 957
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1652 NTQGILKdTQLHLDDALRGQEDLKEQLAMVERraNLLQAEIEELRATLEQTERSrkiaeqELLDASERVQLLHTQNTSLI 1731
Cdd:PLN03188 958 NHPEVLR-TKIELKRVQDELEHYRNFYDMGER--EVLLEEIQDLRSQLQYYIDS------SLPSARKRNSLLKLTYSCEP 1028
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1732 NTKKKLETdISQIQGEM--EDIVQEARNAEEKAKKAITdaamMAEELKKEQDTSAHL-ERMKKNLEqTVKDLQHRLDEAE 1808
Cdd:PLN03188 1029 SQAPPLNT-IPESTDESpeKKLEQERLRWTEAESKWIS----LAEELRTELDASRALaEKQKHELD-TEKRCAEELKEAM 1102
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1809 QLALKGG-----------KKQIQKL------------------EARVRELEGEVENEQKRNVEAIKGLRKHERRvkeltY 1859
Cdd:PLN03188 1103 QMAMEGHarmleqyadleEKHIQLLarhrriqegiddvkkaaaRAGVRGAESKFINALAAEISALKVEREKERR-----Y 1177
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 82524274 1860 QTEEDRKNVLRLQDLVDKLQSKVKAYKRqAEEAEEQSNVnlakfrkIQHELEEAEERADIAESQVNKLRVK 1930
Cdd:PLN03188 1178 LRDENKSLQAQLRDTAEAVQAAGELLVR-LKEAEEALTV-------AQKRAMDAEQEAAEAYKQIDKLKRK 1240
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
936-1336 |
4.88e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 936 EEEINAEL-TAKKRKL-EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQT 1013
Cdd:PRK11281 38 EADVQAQLdALNKQKLlEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1014 LDDLQAEEdkvntltkakikLEQQVDDLEGSLEQEKK-----------IRMDLERAKRKLEGDLKLAQESTmdvendkQQ 1082
Cdd:PRK11281 118 LSTLSLRQ------------LESRLAQTLDQLQNAQNdlaeynsqlvsLQTQPERAQAALYANSQRLQQIR-------NL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1083 LDEKLKKKEFEMSNLQSKIEDEQA-LGMQLQKKIKELQARIEELEEeieaerasrakAEKQRSDLSrelEEISeRLEEAg 1161
Cdd:PRK11281 179 LKGGKVGGKALRPSQRVLLQAEQAlLNAQNDLQRKSLEGNTQLQDL-----------LQKQRDYLT---ARIQ-RLEHQ- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1162 gATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQI------------DNLqRVKQKLEkeks 1229
Cdd:PRK11281 243 -LQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLlkateklntltqQNL-RVKNWLD---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1230 emkmeiddlasnmeviskskgNLEKMCRTLEDQVSELKTK-------EEEQQRL-----INELTAQRGRLQTESGEYSRQ 1297
Cdd:PRK11281 317 ---------------------RLTQSERNIKEQISVLKGSlllsrilYQQQQALpsadlIEGLADRIADLRLEQFEINQQ 375
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 82524274 1298 LDE---KDSLVSQLSRG-KQAFTqqiEELKRQLEEEIKAKSAL 1336
Cdd:PRK11281 376 RDAlfqPDAYIDKLEAGhKSEVT---DEVRDALLQLLDERREL 415
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1393-1588 |
4.94e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1393 LEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALdkkqrnfdkilaewKQKYEETHA 1472
Cdd:PHA02562 204 IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKL--------------NTAAAKIKS 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1473 ELEASQKESRSLS--TELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRIHELEK-------IKKQIEQE 1543
Cdd:PHA02562 270 KIEQFQKVIKMYEkgGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEqskklleLKNKISTN 349
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 82524274 1544 KSEL----------QAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDE 1588
Cdd:PHA02562 350 KQSLitlvdkakkvKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYH 404
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1681-1920 |
5.10e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.06 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1681 VERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLhtqntslintKKKLETDISQIQGEMEDIVQEARNAEE 1760
Cdd:pfam00038 45 PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDF----------RQKYEDELNLRTSAENDLVGLRKDLDE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1761 kAKKAITDAAMMAEELKKEqdtsahLERMKKNLEQTVKDLQHRL-DEAEQLALKGGKKQiqKLEARVRELEGEVENEQKR 1839
Cdd:pfam00038 115 -ATLARVDLEAKIESLKEE------LAFLKKNHEEEVRELQAQVsDTQVNVEMDAARKL--DLTSALAEIRAQYEEIAAK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1840 NVEAIKglRKHERRVKELTYQTE--------------EDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNVNLAKFRK 1905
Cdd:pfam00038 186 NREEAE--EWYQSKLEELQQAAArngdalrsakeeitELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQE 263
|
250
....*....|....*..
gi 82524274 1906 IQHELEEA--EERADIA 1920
Cdd:pfam00038 264 LISELEAElqETRQEMA 280
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1112-1487 |
5.58e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1112 QKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATlq 1191
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEK-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1192 heataATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEmkmeiddlasnmeviskskgnLEKMCRTLEDQVSELKTKEE 1271
Cdd:pfam07888 118 -----DALLAQRAAHEARIRELEEDIKTLTQRVLERETE---------------------LERMKERAKKAGAQRKEEEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1272 EQQRLINELTAQRG---RLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKR---QLEEEIKAKSALAHALQSSRH 1345
Cdd:pfam07888 172 ERKQLQAKLQQTEEelrSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeaENEALLEELRSLQERLNASER 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1346 DCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAE---EHVEAVNAKCASLE 1422
Cdd:pfam07888 252 KVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEadkDRIEKLSAELQRLE 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 82524274 1423 KTKQRLQNEVEDLMIDVERtnaacaaldKKQRNFDKiLAEWKQKYEETHAELEASQKESRSLSTE 1487
Cdd:pfam07888 332 ERLQEERMEREKLEVELGR---------EKDCNRVQ-LSESRRELQELKASLRVAQKEKEQLQAE 386
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1385-1679 |
5.68e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1385 DAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNevedlmidvertnaACAALDKKQRNFDKILAEWK 1464
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQ--------------APAKLRQAQAELEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1465 QKYEETHAELEASQKESR--SLSTELFKIKNAYEESLDHLETLKRENKNLQQEISdlteqiaEGGKRIHELEKIKKQIEQ 1542
Cdd:PRK11281 112 EETRETLSTLSLRQLESRlaQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALY-------ANSQRLQQIRNLLKGGKV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1543 EKSEL---QAALEEAEASLeheegkiLRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAI 1619
Cdd:PRK11281 185 GGKALrpsQRVLLQAEQAL-------LNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRLTL 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 82524274 1620 RLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQL-------------HLDDALRGQEDLKEQLA 1679
Cdd:PRK11281 258 SEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKlntltqqnlrvknWLDRLTQSERNIKEQIS 330
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1232-1633 |
5.86e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1232 KMEIDDLASNMEVIskskgnlEKMCRTLEDQVSELKTKEEEQQRLINELTAQ----RGRLQTESGEYSRQLDEkdslvsq 1307
Cdd:PRK04778 104 KHEINEIESLLDLI-------EEDIEQILEELQELLESEEKNREEVEQLKDLyrelRKSLLANRFSFGPALDE------- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1308 lsrgkqaFTQQIEELKRQLEEEIKAKSALAHaLQSsrhdcdllREQYEEEQEAKAELQRAMSkansEVAQWRTKYETDAI 1387
Cdd:PRK04778 170 -------LEKQLENLEEEFSQFVELTESGDY-VEA--------REILDQLEEELAALEQIME----EIPELLKELQTELP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1388 QRTEELEEAkkklAQRLQDAEEHVEAVNakcasLEKTKQRLQNEVEDLMIDVERTNaacaaLDKKQRNFDKILAEWKQKY 1467
Cdd:PRK04778 230 DQLQELKAG----YRELVEEGYHLDHLD-----IEKEIQDLKEQIDENLALLEELD-----LDEAEEKNEEIQERIDQLY 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1468 EETHAELEASQKesrslstelfkIKNAYEESLDHLETLKRENKNLQQEISDLTE--QIAEggkriHELEKIKkQIEQEKS 1545
Cdd:PRK04778 296 DILEREVKARKY-----------VEKNSDTLPDFLEHAKEQNKELKEEIDRVKQsyTLNE-----SELESVR-QLEKQLE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1546 ELQAALEEAEASLEHEEgkilriqlelnQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKM 1625
Cdd:PRK04778 359 SLEKQYDEITERIAEQE-----------IAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKL 427
|
....*...
gi 82524274 1626 EGDLNEME 1633
Cdd:PRK04778 428 HEIKRYLE 435
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
896-1071 |
6.29e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 896 LQVQSEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAeltaKKRKLEDECSELKKDIDDLELTLAKVEKEK 975
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRE----RRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 976 HATENKVKNLTEEMAGLDetiakltKEKKALQEAHQQTLDDLQaeedKVNTLTKAKIKlEQQVDDLEGSLEQEKKIRMDL 1055
Cdd:PRK12704 110 EELEKKEKELEQKQQELE-------KKEEELEELIEEQLQELE----RISGLTAEEAK-EILLEKVEEEARHEAAVLIKE 177
|
170
....*....|....*.
gi 82524274 1056 ERAKRKLEGDlKLAQE 1071
Cdd:PRK12704 178 IEEEAKEEAD-KKAKE 192
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
860-1576 |
7.75e-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: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 860 KEEFEKAKENLAKAEAKRKELEEK----MVALMQEKNDLQLQVQSEADSLADAEERCDQLIKTK--IQLEAKIKEVTERA 933
Cdd:TIGR01612 1103 KEENIKYADEINKIKDDIKNLDQKidhhIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDdpEEIEKKIENIVTKI 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 934 EDEEEINAELtakkRKLEDECSELKKDIDDLE---------------LTLAKVEKEKHATENKVKNLTEEMAGLDEtiak 998
Cdd:TIGR01612 1183 DKKKNIYDEI----KKLLNEIAEIEKDKTSLEevkginlsygknlgkLFLEKIDEEKKKSEHMIKAMEAYIEDLDE---- 1254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 999 lTKEKKALQEAHQQTLDDLQAEEDKVNT--------LTKAKIKLEQQVDDLEGSLE--QEKKIRMDLERAKRKLEGDLKL 1068
Cdd:TIGR01612 1255 -IKEKSPEIENEMGIEMDIKAEMETFNIshdddkdhHIISKKHDENISDIREKSLKiiEDFSEESDINDIKKELQKNLLD 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1069 AQESTMDVE---------------NDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKElqarieeleEEIEAER 1133
Cdd:TIGR01612 1334 AQKHNSDINlylneianiynilklNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD---------DINLEEC 1404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1134 ASRAKAEKQRSDLSRELEEISER-----LEEAGGAT--SAQIEMNKKREAEFQ--KMRRDLEEATLQHEATAATlrKKHA 1204
Cdd:TIGR01612 1405 KSKIESTLDDKDIDECIKKIKELknhilSEESNIDTyfKNADENNENVLLLFKniEMADNKSQHILKIKKDNAT--NDHD 1482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1205 DSVAELGEQIDNLQRVKQKLEKEKSEM----------KMEIDDLA---SNMEV---ISKSKGNLEKMCRTLEDQVSELKT 1268
Cdd:TIGR01612 1483 FNINELKEHIDKSKGCKDEADKNAKAIeknkelfeqyKKDVTELLnkySALAIknkFAKTKKDSEIIIKEIKDAHKKFIL 1562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1269 KEEEQQRLINELTAQRGRLQTESGEYSRQ-------------LDEK------------DSLVSQLSRGKQAFTQQIEELK 1323
Cdd:TIGR01612 1563 EAEKSEQKIKEIKKEKFRIEDDAAKNDKSnkaaidiqlslenFENKflkisdikkkinDCLKETESIEKKISSFSIDSQD 1642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1324 RQLEEEIKAKSALAHALQSsrhdcdlLREQYEEEQEAKAELQRAMSKANS---EVAQWRTKYETDAIQRTEELEEAKKKl 1400
Cdd:TIGR01612 1643 TELKENGDNLNSLQEFLES-------LKDQKKNIEDKKKELDELDSEIEKieiDVDQHKKNYEIGIIEKIKEIAIANKE- 1714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1401 aqrlqdaeehveavnakcaSLEKTKQRLQNEVEDLMI-----DVERTNAAcAALDKKQRNFDKILAEWKQKYEETHAELE 1475
Cdd:TIGR01612 1715 -------------------EIESIKELIEPTIENLISsfntnDLEGIDPN-EKLEEYNTEIGDIYEEFIELYNIIAGCLE 1774
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1476 ASQKESRSLSTELFKIKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKRihELEKIKKQIEQEKSELQAALEEAE 1555
Cdd:TIGR01612 1775 TVSKEPITYDEIKNTRINAQNEFLKIIEIEKKSKSYLDDIEAKEFDRIINHFKK--KLDHVNDKFTKEYSKINEGFDDIS 1852
|
810 820
....*....|....*....|....*.
gi 82524274 1556 ASLEH-----EEGKILRIqleLNQVK 1576
Cdd:TIGR01612 1853 KSIENvknstDENLLFDI---LNKTK 1875
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1086-1239 |
7.93e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1086 KLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEeieaerasRAKAEKQRSDLSRELEEISERLEEAGGATS 1165
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKL--------RNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1166 AQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELgEQIDNL----------QRVKQKLEKEKSEMKMEI 1235
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLtaeeakeillEKVEEEARHEAAVLIKEI 178
|
....
gi 82524274 1236 DDLA 1239
Cdd:PRK12704 179 EEEA 182
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1269-1599 |
8.21e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1269 KEEEQQRLINELTAQRGRLQTESGEYSRQLDEKDSLVSQLSRGKQAFTQQIEELKRQLEEEI-KAKSALAHALQSSRHDC 1347
Cdd:COG5185 230 NIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFeNTKEKIAEYTKSIDIKK 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1348 DLLR-EQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQ-----RLQDAEEHVEAVNAkcaSL 1421
Cdd:COG5185 310 ATESlEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENivgevELSKSSEELDSFKD---TI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1422 EKTKQRLQNEVEDLMidvERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESldh 1501
Cdd:COG5185 387 ESTKESLDEIPQNQR---GYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEE--- 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1502 letlkrENKNLQQEISDLTEQIAEggkrihELEKIKKQIEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDR 1581
Cdd:COG5185 461 ------SQSRLEEAYDEINRSVRS------KKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKD 528
|
330
....*....|....*...
gi 82524274 1582 KIAEKDEEIDQLKRNHIR 1599
Cdd:COG5185 529 FMRARGYAHILALENLIP 546
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1785-1906 |
8.61e-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: 41.26 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1785 HLERMKKNLEQTVKDLQHRLDEAEQLAlkggKKQIQKLEARVRELEGEVEnEQKRNVEAIKGLRKHERrvkeltyQTEED 1864
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELH----EKQKFYLRQSVIDLQTKLQ-EMQMERDAMADIRRRES-------QSQED 142
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 82524274 1865 RKNvlRLQDLVDKLQskvkAYKRQAEEAEEQSNVNLAKFRKI 1906
Cdd:pfam15921 143 LRN--QLQNTVHELE----AAKCLKEDMLEDSNTQIEQLRKM 178
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
857-1073 |
8.92e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.01 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 857 ANMKEEFEKAKENLAKAEakrkeleekmvalmQEKNDLQLQVQSEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDE 936
Cdd:PRK00106 24 IKMKSAKEAAELTLLNAE--------------QEAVNLRGKAERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 937 EEINA---ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEmaglDETIAKLTKEKkalqEAHQQT 1013
Cdd:PRK00106 90 QEFKSerqELKQIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDER----EEQVEKLEEQK----KAELER 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82524274 1014 LDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMD------LERAKRKLEGDLKLAQEST 1073
Cdd:PRK00106 162 VAALSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDkmakdlLAQAMQRLAGEYVTEQTIT 227
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1578-1928 |
9.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1578 EIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGIL 1657
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1658 KDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKL 1737
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1738 ETDISQIQGEMEDIvqEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKK 1817
Cdd:COG4372 163 QEELAALEQELQAL--SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1818 QIQKLEARVRELEGEVENEQKRNVEAI-KGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQS 1896
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAIlVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350
....*....|....*....|....*....|..
gi 82524274 1897 NVNLAKFRKIQHELEEAEERADIAESQVNKLR 1928
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1388-1609 |
9.87e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.13 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1388 QRTEELEEAKKKLAQRLQDA--EEHVEAVNAKCASLEKTKQR---LQNEVEDLMIDVERTNAACAALDKKQ--------- 1453
Cdd:pfam09787 14 QKAARILQSKEKLIASLKEGsgVEGLDSSTALTLELEELRQErdlLREEIQKLRGQIQQLRTELQELEAQQqeeaessre 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1454 --RNFDKILAEWKQKYEETHAELEASQKESRSLSTELFKIKNAYEESL----DHLETLKRENKNLQQeiSDLTEQIAEgg 1527
Cdd:pfam09787 94 qlQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIkdreAEIEKLRNQLTSKSQ--SSSSQSELE-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82524274 1528 KRIHELEK--IKKQ-----IEQEKSELQAALEEAEASLEHEEGKILR-IQLELNQVKSEID---RKIAEKDEEIDQLKRN 1596
Cdd:pfam09787 170 NRLHQLTEtlIQKQtmleaLSTEKNSLVLQLERMEQQIKELQGEGSNgTSINMEGISDGEGtrlRNVPGLFSESDSDRAG 249
|
250
....*....|...
gi 82524274 1597 HIRVVESMQSTLD 1609
Cdd:pfam09787 250 MYGKVRKAASVID 262
|
|
| |
