|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-770 |
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: 1360.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 420 VQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 500 EQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 579
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 580 FSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGGGGKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 660 NKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14915 561 NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 67189167 740 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14915 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-770 |
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: 1315.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEEATsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDS--KMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd14913 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 420 VQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14913 319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 500 EQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 579
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 580 FSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEgGGGKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADAD-SGKKKVAKKKGSSFQTVSALFRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 660 NKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14913 558 NKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 67189167 740 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14913 638 IDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
100-770 |
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: 1314.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEEatsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKES---GKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd01377 238 DILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 420 VQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd01377 318 KEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 500 EQEEYKKEGIDWEFIDFGMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPakGKAEA 578
Cdd:cd01377 398 EQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKP--KKSEA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 579 HFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSggqaAEAEGGGGKKGGKKKGSSFQTVSALFREN 658
Cdd:cd01377 476 HFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFK----DYEESGGGGGKKKKKGGSFRTVSQLHKEQ 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 659 LNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 738
Cdd:cd01377 552 LNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGF 631
|
650 660 670
....*....|....*....|....*....|..
gi 67189167 739 FiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd01377 632 D-DGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-770 |
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: 1280.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 420 VQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 500 EQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 579
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 580 FSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGGGGKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 660 NKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 67189167 740 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14910 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
100-770 |
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: 1246.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEEatSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEE--SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 420 VQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 500 EQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 579
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 580 FSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEgGGGKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEAD-SGAKKGAKKKGSSFQTVSALFRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 660 NKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14918 558 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 67189167 740 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14918 638 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-770 |
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: 1234.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEeATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKE-QQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14923 240 DILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 420 VQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 500 EQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 579
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 580 FSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEA-EGGGGKKGGKKKGSSFQTVSALFREN 658
Cdd:cd14923 480 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAgDSGGSKKGGKKKGSSFQTVSAVFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 659 LNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 738
Cdd:cd14923 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 67189167 739 FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14923 640 FIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-770 |
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: 1233.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 420 VQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 500 EQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 579
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 580 FSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGG--GGKKGGKKKGSSFQTVSALFRE 657
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAggGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 658 NLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 737
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 67189167 738 QFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
101-770 |
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 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 181 SGAGKTVNTKRVIQYFATIAVTGD--KKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDgpGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTA 338
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 339 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 419 TVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 499 LEQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKAE 577
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPdKKRKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 578 AHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSG--GQAAEAEGGGGKKGGKKKGSSFQTVSALF 655
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENyvGSDSTEDPKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 656 RENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 735
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 67189167 736 EGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14927 642 DDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-770 |
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: 1138.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIAVTGDK-KKEEATSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRsKKENPNANK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTA 338
Cdd:cd14916 159 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 339 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 419 TVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 499 LEQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEA 578
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 579 HFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGGGGKKGGKKKGSSFQTVSALFREN 658
Cdd:cd14916 479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHREN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 659 LNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 738
Cdd:cd14916 559 LNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQ 638
|
650 660 670
....*....|....*....|....*....|..
gi 67189167 739 FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14916 639 FIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-770 |
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: 1137.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd14917 159 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 420 VQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 500 EQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 579
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 580 FSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEgGGGKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAP-IEKGKGKAKKGSSFQTVSALHRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 660 NKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14917 558 NKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 67189167 740 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14917 638 IDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
100-770 |
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: 1032.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd14929 154 MLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14929 233 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 420 VQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14929 313 IEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 500 EQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 579
Cdd:cd14929 393 EQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 580 FSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAeGGGGKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14929 473 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDS-AIQFGEKKRKKGASFQTVASLHKENL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 660 NKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14929 552 NKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKF 631
|
650 660 670
....*....|....*....|....*....|.
gi 67189167 740 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14929 632 VSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
88-770 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1022.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 88 IEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFML 167
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 168 TDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEeatsgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV--------GRLEEQILQSNPILEAFGNAKTVRNNNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 248 GKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLItTNPYDFAYVSQ-GEITVPSI 326
Cdd:pfam00063 153 GKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTIDGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 327 DDQEELMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPR 406
Cdd:pfam00063 232 DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 407 VKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNTLEQLCINFTN 485
Cdd:pfam00063 312 IKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 486 EKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSN 564
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 565 NFQKPKPakgKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAE---AEGGGGKKGG 641
Cdd:pfam00063 470 HFQKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAEsaaANESGKSTPK 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 642 KKKGSSFQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 721
Cdd:pfam00063 547 RTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 67189167 722 FKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:pfam00063 627 FVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
81-782 |
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: 987.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 81 NPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISD 160
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 161 NAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKkeeatsgkmqGTLEDQIISANPLLEAFGNAKTVR 240
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV----------GSVEDQILESNPILEAFGNAKTLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 241 NDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTnPYDFAYVSQG- 319
Cdd:smart00242 151 NNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 320 EITVPSIDDQEELMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQA-EPDGTEVADKAAYLTSLNSADL 398
Cdd:smart00242 230 CLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 399 LKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQ 478
Cdd:smart00242 310 EKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 479 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYe 557
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 558 QHLGKSNNFQKPKPakgKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGqaaeaegggg 637
Cdd:smart00242 468 QHHKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG---------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 638 kKGGKKKGSSFQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRI 717
Cdd:smart00242 535 -VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRL 613
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67189167 718 LYADFKQRYKVLNASAIPEGQFiDSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGTLEEMRD 782
Cdd:smart00242 614 PFDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
101-770 |
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: 984.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 181 SGAGKTVNTKRVIQYFATIAVTGdkkkEEATSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTG----KQSSDGK--GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTAVD 340
Cdd:cd14934 156 LAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 341 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd14934 236 VLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 421 QQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14934 316 EQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 501 QEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGK-AEAH 579
Cdd:cd14934 396 QEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 580 FSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFsggqaaEAEGGGGKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14934 476 FELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLF------KEEEAPAGSKKQKRGSSFMTVSNFYREQL 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 660 NKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqF 739
Cdd:cd14934 550 NKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-F 628
|
650 660 670
....*....|....*....|....*....|.
gi 67189167 740 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14934 629 VDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-770 |
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: 968.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIAVTgdKKKEEATSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGAS--KKTDEAAKSK--GSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd14909 157 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 420 VQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14909 317 VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 500 EQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAK-GKAEA 578
Cdd:cd14909 397 EQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 579 HFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGGGGKKGGKKKGSSFQTVSALFREN 658
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQ 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 659 LNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 738
Cdd:cd14909 557 LNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE 636
|
650 660 670
....*....|....*....|....*....|..
gi 67189167 739 fiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14909 637 --DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
100-770 |
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: 833.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQ-EAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 179 GESGAGKTVNTKRVIQYFATIAvtgdkKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALS-----GSGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDF----AYVSQGEITVPSIDDQEELMA 334
Cdd:cd00124 156 GRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYylndYLNSSGCDRIDGVDDAEEFQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 335 TDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREE--QAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNE 412
Cdd:cd00124 236 LLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 413 YVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQ 490
Cdd:cd00124 316 TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 491 FFNHHMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKP 569
Cdd:cd00124 396 FFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 570 KpakgKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKsglktlaflfsggqaaeaeggggkkggkkkgssfq 649
Cdd:cd00124 475 R----KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS----------------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 650 tvSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 729
Cdd:cd00124 516 --GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRIL 593
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 67189167 730 NASAiPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd00124 594 APGA-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
30-1116 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 816.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 30 KPFDAKSSVFVVDAKESYVKATVqsreggKVTAKTEGGATVTVK--DDQVFSMNPPKYDKIEDMAMMTHLHEPAVLYNLK 107
Cdd:COG5022 14 IPDEEKGWIWAEIIKEAFNKGKV------TEEGKKEDGESVSVKkkVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 108 ERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTV 187
Cdd:COG5022 88 KRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 188 NTKRVIQYFATIavtgdkkkeEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIE 267
Cdd:COG5022 168 NAKRIMQYLASV---------TSSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 268 TYLLEKSRVTFQLKAERSYHIFYQIMSNKkPELIEMLLITTNPYDFAYVSQGE-ITVPSIDDQEELMATDTAVDILGFSA 346
Cdd:COG5022 239 TYLLEKSRVVHQNKNERNYHIFYQLLAGD-PEELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 347 DEKVAIYKLTGAVMHYGNMKFKqKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNS 426
Cdd:COG5022 318 EEQDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 427 VGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVLEQEEYKK 506
Cdd:COG5022 397 RDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 507 EGIDWEFIDFgMDLAACIELIEK--PMGIFSILEEECMFPKATDTSFKNKLYEQ-HLGKSNNFQKPKPAKGKaeahFSLV 583
Cdd:COG5022 477 EGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 584 HYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEaeggggkkggkkKGSSFQTVSALFRENLNKLM 663
Cdd:COG5022 552 HYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE------------SKGRFPTLGSRFKESLNSLM 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 664 TNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI--- 740
Cdd:COG5022 620 STLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwke 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 741 DSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGTLEEMRDEKLAQLITRTQAVCRGYLMRVEFKKMMERRESIFCIQY 820
Cdd:COG5022 700 DTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQH 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 821 NVRAFMNVKHWPWMKLYFKIKPLLKSAETEKEManmkEDFEKAKEDLAKSEAKRK---ELEEKMVALMQEKNDLQLQVQA 897
Cdd:COG5022 780 GFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEY----RSYLACIIKLQKTIKREKklrETEEVEFSLKAEVLIQKFGRSL 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 898 EADGLADAEERCDQLIKTKIQLEAKIKELTERAEDEEEINaELTAKKRKLEDECSELKKDID-----DLELTLAKVEKEK 972
Cdd:COG5022 856 KAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELESEIIELKKSLSsdlieNLEFKTELIARLK 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 973 HATEN-KVKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQekklRMD 1051
Cdd:COG5022 935 KLLNNiDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQ----YGA 1010
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67189167 1052 LERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKefEMSNLQSKIEDEQalgMQLQKKIKELQ 1116
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 ... |
101-770 |
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: 769.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 181 SGAGKTVNTKRVIQYFATIAVTGDKK-----KEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASKPKGsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 256 GATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITtNPYDFAYVSQGEITVPSIDDQEELMAT 335
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 336 DTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYV 414
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 415 TKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFN 493
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 494 HHMFVLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLgksnnfQKPKPAK 573
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 574 G--KAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQ---AAEAEGGGGKKGGKKKGSSF 648
Cdd:cd14911 474 TdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgMAQQALTDTQFGARTRKGMF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 649 QTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 67189167 729 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
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 ... |
101-770 |
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: 753.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 181 SGAGKTVNTKRVIQYFATIAVTGDKKKEeatsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVASSHKGRKD----HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFayVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd14920 158 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFNNYRF--LSNGYIPIPGQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 419 TVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14920 315 TKEQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 497 FVLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNFQKPKPAK 573
Cdd:cd14920 394 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 574 GKAEahFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFS-------GGQAAEAEGGGGKKGGKKKGS 646
Cdd:cd14920 473 DKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdvdrivgLDQVTGMTETAFGSAYKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 647 SFQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 726
Cdd:cd14920 551 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 67189167 727 KVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
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 ... |
101-770 |
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: 705.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 181 SGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFayVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLrSELCLEDYSKYRF--LSNGNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 419 TVQQVYNSVGALAKSMYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 498 VLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNFQKPKpaKG 574
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKV-VQEQGNNPKFQKPK--KL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 575 KAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFS------GGQAAEAEGGGGKKGGKKKGSSF 648
Cdd:cd14932 476 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKdvdrivGLDKVAGMGESLHGAFKTRKGMF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 649 QTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd14932 556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 67189167 729 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14932 636 LTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
101-770 |
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: 682.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 181 SGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASSHKGKKDTSITGE----LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITT-NPYDFayVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd14921 158 IVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGfNNYTF--LSNGFVPIPAAQDDEMFQETLEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14921 236 SIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 419 TVQQVYNSVGALAKSMYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14921 315 TKEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 498 VLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 574
Cdd:cd14921 395 ILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 575 KAEahFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSG-------GQAAEAEGGGGKKGGKKKGSS 647
Cdd:cd14921 474 KTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvdrivglDQMAKMTESSLPSASKTKKGM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 648 FQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14921 552 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 67189167 728 VLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14921 632 ILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-770 |
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: 677.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 179 GESGAGKTVNTKRVIQYFATiaVTGDKKKEEATsgkmqgtlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFAT--VGGSSSGETQV--------EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNK-KPELIEMLLitTNPYDFAYVSQGE-ITVPSIDDQEELMATD 336
Cdd:cd01380 151 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHL--GSAEDFFYTNQGGsPVIDGVDDAAEFEETR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 337 TAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd01380 229 KALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 417 GQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNH 494
Cdd:cd01380 309 PLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 495 HMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNN-FQKPKPAK 573
Cdd:cd01380 389 HVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFSN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 574 GKaeahFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSglktlaflfsggqaaeaeggggkkggkkkGSSFQTVSA 653
Cdd:cd01380 468 TA----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS-----------------------------KNRKKTVGS 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 654 LFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 733
Cdd:cd01380 515 QFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK 594
|
650 660 670
....*....|....*....|....*....|....*..
gi 67189167 734 ipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd01380 595 --EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-770 |
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: 662.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 181 SGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFayVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLrSELLLENYNNYRF--LSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 420 VQQVYNSVGALAKSMYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd15896 320 QEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 499 LEQEEYKKEGIDWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKpaKGK 575
Cdd:cd15896 400 LEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPK--KLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 576 AEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSG-----GQAAEAEGGGGKKGGKKKGSSFQT 650
Cdd:cd15896 477 DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDvdrivGLDKVSGMSEMPGAFKTRKGMFRT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 651 VSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 730
Cdd:cd15896 557 VGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 636
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 67189167 731 ASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd15896 637 PNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-770 |
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: 658.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 181 SGAGKTVNTKRVIQYFATIAVTGDKKKEeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLIttNPYD-FAYVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd14919 155 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 420 VQQVYNSVGALAKSMYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 499 LEQEEYKKEGIDWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGK 575
Cdd:cd14919 393 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 576 AEahFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSG-------GQAAEAEGGGGKKGGKKKGSSF 648
Cdd:cd14919 472 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGMSETALPGAFKTRKGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 649 QTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd14919 550 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 67189167 729 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
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 ... |
101-770 |
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: 645.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 181 SGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE----LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYdFAYVSQGEITVPSiDDQEELMATDTAVD 340
Cdd:cd14930 158 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 341 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14930 236 VLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 420 VQQVYNSVGALAKSMYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14930 315 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 498 VLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 574
Cdd:cd14930 394 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLRD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 575 KAEahFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSG-----GQAAEAEGGGGKKGGKKKGSSFQ 649
Cdd:cd14930 473 QAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSLGDGPPGGRPRRGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 650 TVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 729
Cdd:cd14930 551 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 67189167 730 NASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14930 631 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-770 |
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: 631.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRgkKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFAtiAVTGDKkkeeatsgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd01383 79 ESGAGKTETAKIAMQYLA--ALGGGS-----------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTnPYDFAYVSQGE-ITVPSIDDQEELMATDTA 338
Cdd:cd01383 146 KICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNcLTIDGVDDAKKFHELKEA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 339 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd01383 225 LDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 419 TVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDT-KQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd01383 305 TLQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 498 VLEQEEYKKEGIDWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNFqkpkpaKGKA 576
Cdd:cd01383 385 KLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGER 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 577 EAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKtLAFLFSGGQAAEAEGGGGKKGGKKKGSSFQTVSALFR 656
Cdd:cd01383 457 GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQ-LPQLFASKMLDASRKALPLTKASGSDSQKQSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 657 ENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 736
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSA 615
|
650 660 670
....*....|....*....|....*....|....
gi 67189167 737 GQFIDSkkASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd01383 616 SQDPLS--TSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
101-770 |
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: 617.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 181 SGAGKTVNTKRVIQYFAtiAVTGDkkkeeaTSGKMQGTlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd01378 82 SGAGKTEASKRIMQYIA--AVSGG------SESEVERV-KDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTnPYDFAYVSQGE-ITVPSIDDQEELMATDTAV 339
Cdd:cd01378 153 PVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQR-PEQYYYYSKSGcFDVDGIDDAADFKEVLNAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDgTEVADKAAYLTSLNSADLLKALCYPRVKVGNEY---VTK 416
Cdd:cd01378 232 KVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 417 GQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQ-YFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHh 495
Cdd:cd01378 311 PLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 496 mFVL--EQEEYKKEGIDWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNKLyEQHLGKSNNFQKPKP 571
Cdd:cd01378 390 -LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 572 AKGKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGGGGkkggkkkgssfqTV 651
Cdd:cd01378 467 HFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSKKRPP------------TA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 652 SALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 731
Cdd:cd01378 535 GTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSP 614
|
650 660 670
....*....|....*....|....*....|....*....
gi 67189167 732 SAIPEGQFIDsKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd01378 615 KTWPAWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
101-770 |
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: 612.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 181 SGAGKTVNTKRVIQYFATIavtgdkkkeeatSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd01381 82 SGAGKTESTKLILQYLAAI------------SGQ-HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTnPYDFAYVSQGE-ITVPSIDDQEELMATDTAV 339
Cdd:cd01381 149 IEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD-ASDYYYLTQGNcLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQRE--EQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 417
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 418 QTVQQVYNSVGALAKSMYEKMFLWMVTRIN----QQLDTKQPRQYfIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFN 493
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINsaiyKPRGTDSSRTS-IGVLDIFGFENFEVNSFEQLCINFANENLQQFFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 494 HHMFVLEQEEYKKEGIDWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPkpa 572
Cdd:cd01381 387 RHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 573 KGKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGGGGKkggkkkgssfQTVS 652
Cdd:cd01381 462 KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKS----------PTLS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 653 ALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnAS 732
Cdd:cd01381 532 SQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVL-VP 610
|
650 660 670
....*....|....*....|....*....|....*...
gi 67189167 733 AIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd01381 611 GIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
101-770 |
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: 602.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 181 SGAGKTVNTKRVIQYFAtiAVTGDkkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14883 82 SGAGKTETTKLILQYLC--AVTNN-----------HSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKK--PELIEmLLITTNPYDFAYVSQ-GEITVPSIDDQEELMATDT 337
Cdd:cd14883 149 IKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKE-KLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 338 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd14883 228 AMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 417 GQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14883 308 PLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 497 FVLEQEEYKKEGIDWEFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQkpKPAKGK 575
Cdd:cd14883 388 FKLEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYE--KPDRRR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 576 AEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFS----GGQAAEAEGGGGKKGGKKKGSSFQTV 651
Cdd:cd14883 464 WKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTypdlLALTGLSISLGGDTTSRGTSKGKPTV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 652 SALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 731
Cdd:cd14883 544 GDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDP 623
|
650 660 670
....*....|....*....|....*....|....*....
gi 67189167 732 SAIPEGQFIDsKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14883 624 RARSADHKET-CGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
100-770 |
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: 581.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 179 GESGAGKTVNTKRVIQYFATIAvtgdkkKEEATSGKmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG------GRAVTEGR---SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTnPYDFAYVSQGE-ITVPSIDDQEELMATDT 337
Cdd:cd01384 152 GRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKD-PKQFHYLNQSKcFELDGVDDAEEYRATRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 338 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKqkqreEQAEPDGTEVADKAAYLTSLNSADLL--------KALCYPRVKV 409
Cdd:cd01384 231 AMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEKSEFHLKAAAELLmcdekaleDALCKRVIVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 410 GNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQ 489
Cdd:cd01384 306 PDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 490 QFFNHHMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKSNNFQK 568
Cdd:cd01384 386 QHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 569 PKpakgKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAeggggkkggkKKGSSF 648
Cdd:cd01384 464 PK----LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGT----------SSSSKF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 649 QTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd01384 530 SSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGL 609
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 67189167 729 LnASAIPEGQFiDSKKASEKLLGSIDIDhtQYKFGHTKVFFK 770
Cdd:cd01384 610 L-APEVLKGSD-DEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
101-770 |
1.59e-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: 537.82 E-value: 1.59e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAY-QFM---LTDRENQSI 175
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtQLIqsgVLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 176 LITGESGAGKTVNTKRVIQYFATI----AVTGDKKKEEATSGKMQ--GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARItsgfAQGASGEGEAASEAIEQtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 250 FIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQgEITVPSIDDQ 329
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGE-CSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 330 EELMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGT-EVADKAAYLTSLNSADLLKALCYPRVK 408
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 409 VGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKL 488
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 489 QQFFNHHMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIE-----KPmGIFSILEEECMFPKA-TDTSFKNKLYEQHLGK 562
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgkvngKP-GIFITLDDCWRFKGEeANKKFVSQLHASFGRK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 563 SNNFQKPKPAKGK---------AEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGlktlaflfsggqaaeae 633
Cdd:cd14890 479 SGSGGTRRGSSQHphfvhpkfdADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR----------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 634 ggggkkggkkkgSSFQTVS--ALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRK 711
Cdd:cd14890 542 ------------RSIREVSvgAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQ 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 712 GFPSRILYADFKQRYKVLNASAipegqfiDSKKASEKLLGSI-DIDHTQYKFGHTKVFFK 770
Cdd:cd14890 610 GFALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKMlGLGKADWQIGSSKIFLK 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
850-1927 |
7.87e-168 |
|
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: 542.46 E-value: 7.87e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 850 EKEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIKELTER 929
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 930 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQ 1009
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1010 TLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEF 1089
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1090 EMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNK 1169
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1170 KREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNL 1249
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1250 EKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKA 1329
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1330 KNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDAEEHVE 1409
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1410 AVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQ---KY--EETQAELEASQKESRSLSte 1484
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAisaRYaeERDRAEAEAREKETRALS-- 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1485 lfkVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILR 1564
Cdd:pfam01576 641 ---LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLR 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1565 IQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAI 1644
Cdd:pfam01576 718 LEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1645 RNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQN 1724
Cdd:pfam01576 798 KQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGK 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1725 TSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEA 1804
Cdd:pfam01576 878 SALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1805 EQLALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKR 1884
Cdd:pfam01576 958 EGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKR 1037
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|...
gi 67189167 1885 QAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVK 1927
Cdd:pfam01576 1038 QLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
103-770 |
3.36e-167 |
|
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: 525.66 E-value: 3.36e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 182 GAGKTVNTKRVIQYFAtiavtgdkkkeeATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 261
Cdd:cd01382 84 GAGKTESTKYILRYLT------------ESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLittnpydfayvsqgeiTVPSIDDQEELMATDTAVDI 341
Cdd:cd01382 152 VGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 342 LGFSADEKVAIYKLTGAVMHYGNMKFkqkqrEEQAEPD--GTEVADK-------AAYLTSLNSADLLKALCYpRVKVGNE 412
Cdd:cd01382 216 IGLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSggGCNVKPKseqsleyAAELLGLDQDELRVSLTT-RVMQTTR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 413 YVTKGQ------TVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQpRQYFIGVLDIAGFEIFDFNTLEQLCINFTNE 486
Cdd:cd01382 290 GGAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 487 KLQQFFNHHMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLgksNN 565
Cdd:cd01382 369 KLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK---NH 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 566 FQKPKPAKGKAEAH--------FSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFsggqaAEAEGGGG 637
Cdd:cd01382 445 FRLSIPRKSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF-----ESSTNNNK 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 638 KKGGKKKGSSFQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRI 717
Cdd:cd01382 520 DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRT 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 718 LYADFKQRYKVLNASAIPEgqfIDSK---KASEKLLGSIDIDhtqYKFGHTKVFFK 770
Cdd:cd01382 600 SFHDLYNMYKKYLPPKLAR---LDPRlfcKALFKALGLNEND---FKFGLTKVFFR 649
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
100-770 |
6.87e-163 |
|
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: 514.63 E-value: 6.87e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRgKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 179 GESGAGKTVNTKRVIQYFATIAVTGDKKKEeatsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF--- 255
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS---------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFskl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 256 ------GATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMS-----------------------NKKPELIEMLL- 305
Cdd:cd14888 151 kskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 306 --ITTNPYDFAYvsqGEITVPSIDDQEELMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQA---EPDG 380
Cdd:cd14888 231 epHLKFRYLTKS---SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASC 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 381 TEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLD-TKQPRQYF 459
Cdd:cd14888 308 TDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 460 IGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGmDLAACIELI-EKPMGIFSILE 538
Cdd:cd14888 388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 539 EECMFPKATDTSFKNKLYEQHLGkSNNFQKPKpakgKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLK 618
Cdd:cd14888 467 EECFVPGGKDQGLCNKLCQKHKG-HKRFDVVK----TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNP 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 619 TLAFLFSGGQAAEAEGGGGKKGgkkkgssFQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLR 698
Cdd:cd14888 542 FISNLFSAYLRRGTDGNTKKKK-------FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLK 614
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67189167 699 CNGVLEGIRICRKGFPSRILYADFKQRYKVLnasAIPEGQfidskkasekllgsidIDHTQYKFGHTKVFFK 770
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRIL---LNGEGK----------------KQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
103-770 |
3.54e-162 |
|
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: 513.46 E-value: 3.54e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESG 182
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 183 AGKTVNTKRVIQYFAtiavtgdkkkeeATSGKMQGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 261
Cdd:cd01385 84 SGKTESTNFLLHHLT------------ALSQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTnPYDFAYVSQGE-ITVPSIDDQEELMATDTAVD 340
Cdd:cd01385 152 RGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDcYTLEGEDEKYEFERLKQAME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 341 ILGFSADEKVAIYKLTGAVMHYGNMKFKQK--QREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd01385 231 MVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 419 TVQQVYNSVGALAKSMYEKMFLWMVTRINQQL----DTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNH 494
Cdd:cd01385 311 KLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 495 HMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHlgKSNNF-QKPKpa 572
Cdd:cd01385 391 HIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAKFKQQH--KDNKYyEKPQ-- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 573 kgKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKS---------GLKTLA----------------FLFSGG 627
Cdd:cd01385 466 --VMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSssafvreliGIDPVAvfrwavlrafframaaFREAGR 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 628 QAAEAEGGGGKKGGKKKGSSF---------QTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLR 698
Cdd:cd01385 544 RRAQRTAGHSLTLHDRTTKSLlhlhkkkkpPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLR 623
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67189167 699 CNGVLEGIRICRKGFPSRILYADFKQRYKVLnasaIPEGQfIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd01385 624 YTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
100-770 |
6.44e-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: 511.63 E-value: 6.44e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 179 GESGAGKTVNTKRVIQYFATIAvtgdkkkeeatSGKMQGTLEdQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA-----------GGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIM-SNKKPELIEMLLITTNPYDFAYVSqgeITVPSIDDQEELMATDT 337
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLaSPDVEERLFLDSANECAYTGANKT---IKIEGMSDRKHFARTKE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 338 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE--PDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVT 415
Cdd:cd14903 226 ALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 416 KGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHH 495
Cdd:cd14903 306 VPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 496 MFVLEQEEYKKEGIDWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgk 575
Cdd:cd14903 386 VFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR-- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 576 aeAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGGGGKKGGKKKGS----SFQTV 651
Cdd:cd14903 463 --TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRggalTTTTV 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 652 SALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLna 731
Cdd:cd14903 541 GTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF-- 618
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 67189167 732 saIPEGQFIDSKKAS--EKLLGSIDIDH-TQYKFGHTKVFFK 770
Cdd:cd14903 619 --LPEGRNTDVPVAErcEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
100-770 |
1.23e-160 |
|
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: 507.78 E-value: 1.23e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIAvtgdkkkeEATSGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVA--------GSTNG-----VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSnkKPELIEMLLITTNPyDFAYVSQGE-ITVPSIDDQEELMATDTA 338
Cdd:cd14872 148 RICGASTENYLLEKSRVVYQIKGERNFHIFYQLLA--SPDPASRGGWGSSA-AYGYLSLSGcIEVEGVDDVADFEEVVLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 339 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGT---EVADKAAYLTSLNSADLLKALCYPRVKVgneyvt 415
Cdd:cd14872 225 MEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVanrDVLKEVATLLGVDAATLEEALTSRLMEI------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 416 KGQ-------TVQQVYNSVGALAKSMYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEK 487
Cdd:cd14872 299 KGCdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 488 LQQFFNHHMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSnnF 566
Cdd:cd14872 379 LQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS--T 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 567 QKPKPAKGkAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEaeggggkkggkkkGS 646
Cdd:cd14872 456 FVYAEVRT-SRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQ-------------KT 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 647 SFQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 726
Cdd:cd14872 522 SKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRY 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 67189167 727 KVLNaSAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14872 602 RFLV-KTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
100-768 |
6.74e-158 |
|
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: 500.47 E-value: 6.74e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAY------RGKKRQEAPPHIFSISDNAYQFMLTDRE-- 171
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 172 --NQSILITGESGAGKTVNTKRVIQYFATIAvTGDKKKEEATSgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVS-SATTHGQNATE---RENVRDRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 250 FIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPyDFAYV--SQGEITVPSID 327
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVE-EYKYLnsSQCYDRRDGVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 328 DQEELMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAY-LTSLNSADLLKALCYPR 406
Cdd:cd14901 236 DSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTRE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 407 VKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNTLEQLCINFT 484
Cdd:cd14901 316 IRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 485 NEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGMDlAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKS 563
Cdd:cd14901 396 NEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 564 NNFQKPKPAKGKAEahFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSglkTLAFLFSggqaaeaeggggkkggkk 643
Cdd:cd14901 474 ASFSVSKLQQGKRQ--FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTS---SNAFLSS------------------ 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 644 kgssfqTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFK 723
Cdd:cd14901 531 ------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFV 604
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 67189167 724 QRYKVLNAS------AIPEGQFIDSKKASEKLLGSIDIDHTQykFGHTKVF 768
Cdd:cd14901 605 HTYSCLAPDgasdtwKVNELAERLMSQLQHSELNIEHLPPFQ--VGKTKVF 653
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-770 |
4.84e-156 |
|
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: 494.49 E-value: 4.84e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIAVTGDKkkeeatsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVLGKANNR------------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIM----SNKKpeLIEMLLITTNPydFAYVSQGEITVPSIDDQ----EE 331
Cdd:cd01379 149 AVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKP--PRYLQNDGLTVQDIVNNsgnrEK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 332 LMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQ----AEPDGTEVADKAAYLTSLNSADLLKALCYPRV 407
Cdd:cd01379 225 FEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 408 KVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQP---RQYFIGVLDIAGFEIFDFNTLEQLCINFT 484
Cdd:cd01379 305 VTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSasdEPLSIGILDIFGFENFQKNSFEQLCINIA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 485 NEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFG-----MDLaacieLIEKPMGIFSILEEECMFPKATDTSFKNKLyEQH 559
Cdd:cd01379 385 NEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKF-HNN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 560 LgKSNNFQKPKpakgKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAflfsggqaaeaeggggkk 639
Cdd:cd01379 459 I-KSKYYWRPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 640 ggkkkgssfQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILY 719
Cdd:cd01379 516 ---------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILF 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 67189167 720 ADFKQRYKVL--NASAIPEGqfidSKKASEKLLGSIDIDHtqYKFGHTKVFFK 770
Cdd:cd01379 587 ADFLKRYYFLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
101-770 |
1.85e-155 |
|
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: 493.89 E-value: 1.85e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 181 SGAGKTVNTKRVIQYFATIAVTGDKKKEEatsgkmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgATGK 260
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVNQRRNNLVTE------------QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQI---MSNKKPELIEMLlittNPYDFAYVSQG-EITVPSIDDQEELMATD 336
Cdd:cd01387 149 IVGAITSQYLLEKSRIVTQAKNERNYHVFYELlagLPAQLRQKYGLQ----EAEKYFYLNQGgNCEIAGKSDADDFRRLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 337 TAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEpdGTEVADKA-----AYLTSLNSADLLKALCYPRVKVGN 411
Cdd:cd01387 225 AAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQE--GVSVGSDAeiqwvAHLLQISPEGLQKALTFKVTETRR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 412 EYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQF 491
Cdd:cd01387 303 ERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 492 FNHHMFVLEQEEYKKEGIDWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 570
Cdd:cd01387 383 FNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 571 paKGKAEahFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSG--GQAAEAEGGGGKKGGKKKGSSF 648
Cdd:cd01387 461 --MPLPE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSShrAQTDKAPPRLGKGRFVTMKPRT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 649 QTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd01387 537 PTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRC 616
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 67189167 729 LNASAIPEGQFIDSKKA-SEKLLGSIDIDhtQYKFGHTKVFFK 770
Cdd:cd01387 617 LVALKLPRPAPGDMCVSlLSRLCTVTPKD--MYRLGATKVFLR 657
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
101-770 |
4.14e-155 |
|
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: 492.77 E-value: 4.14e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIAvtgdKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVIS----QQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTnPYDFAYVSQ-GEITVPSIDDQEELMATDTA 338
Cdd:cd14873 158 NIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 339 VDILGFSADEKVAIYKLTGAVMHYGNMKFkqkqreeqAEPDGTEVADK-----AAYLTSLNSADLLKALCYPRVKVGNEY 413
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLRGEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 414 VTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQyFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFN 493
Cdd:cd14873 309 ILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 494 HHMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgkSNN--FQKPKp 571
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH---ANNhfYVKPR- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 572 akgKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGGGGKKGGKKKgssfQTV 651
Cdd:cd14873 463 ---VAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRR----PTV 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 652 SALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL-N 730
Cdd:cd14873 536 SSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLmR 615
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 67189167 731 ASAIPEgqfiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14873 616 NLALPE----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
106-770 |
4.39e-152 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 484.65 E-value: 4.39e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNpevVAAYRGKKRQEA-----PPHIFSISDNAYQFMLTDR----ENQSI 175
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYD---VPGFDSQRKEEAtasspPPHVFSIAERAYRAMKGVGkgqgTPQSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 176 LITGESGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14892 84 VVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 256 GATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpELIEMLLITTNPYDFAYVSQGE-ITVPSIDDQEELMA 334
Cdd:cd14892 164 NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGNcVEVDGVDDATEFKQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 335 TDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAD--KAAYLTSLNSADLLKALCYpRVKVGne 412
Cdd:cd14892 243 LRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFKLVT-QTTST-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 413 yvTKGQ------TVQQVYNSVGALAKSMYEKMFLWMVTRIN----QQL------DTKQPRQYFIGVLDIAGFEIFDFNTL 476
Cdd:cd14892 320 --ARGSvleiklTAREAKNALDALCKYLYGELFDWLISRINachkQQTsgvtggAASPTFSPFIGILDIFGFEIMPTNSF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIEK-PMGIFSILEEECMFP-KATDTSFKNK 554
Cdd:cd14892 398 EQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 555 LYEQHLGKSNNFQKPKpakgKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKsglktlaflfsggqaaeaeg 634
Cdd:cd14892 477 YHQTHLDKHPHYAKPR----FECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRS-------------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 635 gggkkggkkkgssfqtvSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 714
Cdd:cd14892 533 -----------------SSKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFP 595
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67189167 715 SRILYADFKQRYKVL-------NASAIPEGQFIDSKKASEKLLGSIDIDHTQykFGHTKVFFK 770
Cdd:cd14892 596 IRRQFEEFYEKFWPLarnkagvAASPDACDATTARKKCEEIVARALERENFQ--LGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-770 |
1.48e-144 |
|
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: 463.01 E-value: 1.48e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKK-RQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 181 SGAGKTVNTKRVIQYFATIavtgdkkkeeatSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 260
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKL------------SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLItTNPYDFAYVSQGEITVPSIDDQEEL-----MAT 335
Cdd:cd14897 151 LLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELeyyrqMFH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 336 DTaVDIL---GFSADEKVAIYKLTGAVMHYGNMKFkqkqrEEQAEPDGTEVADK-----AAYLTSLNSADLLKALCYPRV 407
Cdd:cd14897 230 DL-TNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 408 KVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYF-----IGVLDIAGFEIFDFNTLEQLCIN 482
Cdd:cd14897 304 TIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCIN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 483 FTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLyEQHLG 561
Cdd:cd14897 384 LSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 562 KSNNFQKPKpaKGKAEahFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFsggqaaeaeggggkkgg 641
Cdd:cd14897 462 ESPRYVASP--GNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF----------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 642 kkkgssfqtvSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 721
Cdd:cd14897 521 ----------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYED 590
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 67189167 722 FKQRYKVL-----NASAIPEGQFIDSKKasekllgsiDIDHTQYKFGHTKVFFK 770
Cdd:cd14897 591 FVKRYKEIcdfsnKVRSDDLGKCQKILK---------TAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
102-729 |
3.00e-144 |
|
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: 462.08 E-value: 3.00e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAY-----------RGKKRQEAPPHIFSISDNAYQFM--- 166
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 167 -LTDRENQSILITGESGAGKTVNTKRVIQYFATIavtGDKKKEEATS-GKMQGTLEDQIISANPLLEAFGNAKTVRNDNS 244
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQA---GDNNLAASVSmGKSTSGIAAKVLQTNILLESFGNARTLRNDNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 245 SRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMllittnpydfayvsqgeitvp 324
Cdd:cd14900 160 SRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR--------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 325 siDDQEELMAtdtAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA-------DKAAYLTSLNSAD 397
Cdd:cd14900 219 --DMYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 398 LLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQL-----DTKQPRQYFIGVLDIAGFEIFD 472
Cdd:cd14900 294 LEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 473 FNTLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSF 551
Cdd:cd14900 374 KNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 552 KNKLYEQhLGKSNNFQKPKPAKGKaeAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQksglktlaflfSGGQaae 631
Cdd:cd14900 453 ASKLYRA-CGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV-----------YGLQ--- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 632 aeggggkkggkkkgssfqtvsalFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRK 711
Cdd:cd14900 516 -----------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARA 572
|
650
....*....|....*...
gi 67189167 712 GFPSRILYADFKQRYKVL 729
Cdd:cd14900 573 GFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
100-770 |
2.06e-139 |
|
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: 449.39 E-value: 2.06e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 179 GESGAGKTVNTKRVIQYFATIAvtgdkkkeeatsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA------------GGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDT 337
Cdd:cd14904 149 GKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 338 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAdKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 417
Cdd:cd14904 229 SLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLS-QVAKMLGLPTTRIEEALCNRSVVTRNESVTVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 418 QTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQY-FIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14904 308 LAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 497 FVLEQEEYKKEGIDWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQH--LGKSNNFQKPKPAKg 574
Cdd:cd14904 388 FKTVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 575 kaeAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFsggQAAEAEGGGGKKGGKKKGSSFQTVSAL 654
Cdd:cd14904 466 ---TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF---GSSEAPSETKEGKSGKGTKAPKSLGSQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 655 FRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAI 734
Cdd:cd14904 540 FKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSM 619
|
650 660 670
....*....|....*....|....*....|....*..
gi 67189167 735 PEGqfiDSKKASEKLLGSIDIDHT-QYKFGHTKVFFK 770
Cdd:cd14904 620 HSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-770 |
2.29e-138 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 447.17 E-value: 2.29e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRG--KKRQEA------PPHIFSISDNAYQFMLTDREN 172
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiIQNGEYfdikkePPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 173 QSILITGESGAGKTVNTKRVIQYFATIA--------VTGDKKKEEATSgKMQGTLEDQIISANPLLEAFGNAKTVRNDNS 244
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSqqeqnseeVLTLTSSIRATS-KSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 245 SRFGKFIRIHFG-ATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDF--AYVSQGE- 320
Cdd:cd14907 162 SRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDryDYLKKSNc 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 321 ITVPSIDDQEELMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLTSLNSADL 398
Cdd:cd14907 242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 399 LKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQL--------DTKQPRQYFIGVLDIAGFEI 470
Cdd:cd14907 322 KEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 471 FDFNTLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEF--IDFgMDLAACIELIEK-PMGIFSILEEECMFPKAT 547
Cdd:cd14907 402 FQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 548 DTSFKNKLYEQHLGKSNNFQKPKPAKGKaeahFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGg 627
Cdd:cd14907 481 DEKLLNKIKKQHKNNSKLIFPNKINKDT----FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSG- 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 628 qaaeaEGGGGKKGGKKKGSSFQT---VSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLE 704
Cdd:cd14907 556 -----EDGSQQQNQSKQKKSQKKdkfLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLE 630
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 705 GIRICRKGFPSRILYADFKQRYKVLNasaipegqfidskkasekllgsididhTQYKFGHTKVFFK 770
Cdd:cd14907 631 SIRVRKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
19-829 |
8.60e-137 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 447.94 E-value: 8.60e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 19 KSEKERIEAQNKPFDAKSSVFVVDAKES----------------------YVKATVQ-SREGGKVTAK---TEGGATVTV 72
Cdd:PTZ00014 2 ARTKEKAKTANKLFRRNSNVEAFDKSGNvlkgfyvwtdkapavkedpdlmFAKCLVLpGSTGEKLTLKqidPPTNSTFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 73 KDDQVFSMNPP-KYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYR-GKKRQE 150
Cdd:PTZ00014 82 KPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRdAKDSDK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 151 APPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATiavtgdkkkeeATSGKMQGTLEDQIISANPLL 230
Cdd:PTZ00014 162 LPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS-----------SKSGNMDLKIQNAIMAANPVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 231 EAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLItTNP 310
Cdd:PTZ00014 231 EAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 311 YDFAYVSQGEITVPSIDDQEELMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-----PDGTEVAD 385
Cdd:PTZ00014 310 EEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDaaaisDESLEVFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 386 KAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDI 465
Cdd:PTZ00014 390 EACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 466 AGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPK 545
Cdd:PTZ00014 470 FGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPG 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 546 ATDTSFKNKLYEQhLGKSNNFqkpKPAKGKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFS 625
Cdd:PTZ00014 550 GTDEKFVSSCNTN-LKNNPKY---KPAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFE 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 626 GgqaAEAEGGGGKKGgkkkgssfQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEG 705
Cdd:PTZ00014 626 G---VEVEKGKLAKG--------QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEA 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 706 IRICRKGFPSRILYADFKQRYKVLNAsAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGTLEEMRDEKL 785
Cdd:PTZ00014 695 LQLRQLGFSYRRTFAEFLSQFKYLDL-AVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKL 773
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 67189167 786 AQ---LITRTQAVCRGYLMRvefKKMMERRESIFCIQYNVRAFMNVK 829
Cdd:PTZ00014 774 AAwepLVSVLEALILKIKKK---RKVRKNIKSLVRIQAHLRRHLVIA 817
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
102-770 |
7.83e-136 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 439.73 E-value: 7.83e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFML----TDRENQSILI 177
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 178 TGESGAGKTVNTKRVIQYFAtiavtgdkkkeEATSGKMQgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgA 257
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIM-----------ELCRGNSQ--LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-R 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 258 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQI---MSNKKPELIEMLlittNPYDFAYVSQGEitvpsidDQEELMA 334
Cdd:cd14889 149 NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNGA-------GCKREVQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 335 T--------DTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLTSLNSADLLKALCYP 405
Cdd:cd14889 218 YwkkkydevCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 406 RVKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLdtkQPRQYF------IGVLDIAGFEIFDFNTLEQL 479
Cdd:cd14889 298 VTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 480 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLyEQH 559
Cdd:cd14889 375 CINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKL-NIH 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 560 LGKSNNFQKPKPAKGKaeahFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGGGGKK 639
Cdd:cd14889 454 FKGNSYYGKSRSKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAK 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 640 GGKKKGSSF-----QTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 714
Cdd:cd14889 530 LPQAGSDNFnstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFS 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 715 SRILYADFKQRYKVLnasaIPEGQFIDSKKASEKLLGSIDIdhTQYKFGHTKVFFK 770
Cdd:cd14889 610 WRPSFAEFAERYKIL----LCEPALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
100-770 |
2.25e-135 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 437.94 E-value: 2.25e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAA--WMIYTYSGLFCVTVNPYKWLPvyNPEVvAAYRGKKRQEAPPHIFSISDNAYQFMLTDRE---NQS 174
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 175 ILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKMQG------TLEDQIISANPLLEAFGNAKTVRNDNSSRFG 248
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 249 KFIRIHFGATG-KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLItTNPYDFAYVSQ-GEITVPSI 326
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLL-LSPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 327 DDQEELMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREE----QAEPDGTEVADKAAYLTSLNSADLLKAL 402
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 403 CYPRVKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFD-FNTLEQLCI 481
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 482 NFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGmDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHl 560
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 561 GKSNNFQKPKPaKGKAEAhFSLVHYAGTVDYNIIGWLDKNKDPLNETVvglyqksglktlaflfsggqaaeaeggggkkg 640
Cdd:cd14891 475 KRHPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPEDF-------------------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 641 gkkkgSSFQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 720
Cdd:cd14891 521 -----EDLLASSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYA 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 721 DFKQRYKVLNASAI------PEGQFIdskkasEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14891 596 ELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
100-736 |
6.53e-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: 6.53e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYR--GKKRQ---EAP----PHIFSISDNAYQFMLTD- 169
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELG-KLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 250 FIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIM------SNKKPELIEMLLITTN-PYDFAYVSQGEI- 321
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDGITGGLQlPNEFHYTGQGGAp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 322 TVPSIDDQEELMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQRE---EQAEPDGTEVADKAAYLTSLNSADL 398
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDgaaEIAEEGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 399 LKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNTL 476
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNK 554
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 555 LYEQHLGKSN-----NFQKPKPAKGKAEAHFSLVHYAGTVDYNI-IGWLDKNKDPLNetvvglyqksglKTLAFLFSGGQ 628
Cdd:cd14908 479 LYETYLPEKNqthseNTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIP------------LTADSLFESGQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 629 AaeaeggggkkggkkkgssfqtvsalFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRI 708
Cdd:cd14908 547 Q-------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRV 601
|
650 660
....*....|....*....|....*...
gi 67189167 709 CRKGFPSRILYADFKQRYKVLnASAIPE 736
Cdd:cd14908 602 ARSGYPVRLPHKDFFKRYRML-LPLIPE 628
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
100-727 |
2.36e-128 |
|
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: 420.84 E-value: 2.36e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYR--------GKKRQEAPPHIFSISDNAYQFML-TD 169
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKMQGTledQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVEIGK---RILQTNPILESFGNAQTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 250 FIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEmLLITTNPYDFAYVSQGEIT-----VP 324
Cdd:cd14902 158 FIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD-LLGLQKGGKYELLNSYGPSfarkrAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 325 SIDDQEELMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKqkqrEEQAEPDGTEVA-------DKAAYLTSLNSAD 397
Cdd:cd14902 237 ADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFT----AENGQEDATAVTaasrfhlAKCAELMGVDVDK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 398 LLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLD-------TKQPRQYF--IGVLDIAGF 468
Cdd:cd14902 313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsISDEDEELatIGILDIFGF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 469 EIFDFNTLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKAT 547
Cdd:cd14902 393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 548 DTSFKNKLYEQHLGksnnfqkpkpakgkaEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFS-- 625
Cdd:cd14902 472 NQALSTKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGAde 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 626 --GGQAAEAEGGGGKKGGKKKGSSfqtVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVL 703
Cdd:cd14902 537 nrDSPGADNGAAGRRRYSMLRAPS---VSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVL 613
|
650 660
....*....|....*....|....
gi 67189167 704 EGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14902 614 EAVRIARHGYSVRLAHASFIELFS 637
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-770 |
4.10e-124 |
|
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: 408.57 E-value: 4.10e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNpevVAAYRGK--KRQEAPPHIFSISDNAYQFMLT-------D 169
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 170 RENQSILITGESGAGKTVNTKRVIQYFATIA----VTGDKKKEEATSGkmqgtleDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSkhttATSSSKRRRAISG-------SELLSANPILESFGNARTLRNDNSS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 246 RFGKFIRIHFG-----ATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPE-LIEMLLITTNPYDFAYVSQG 319
Cdd:cd14895 151 RFGKFVRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 320 EITV--PSIDDQEELMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA------------- 384
Cdd:cd14895 231 QCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspsslt 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 385 -----DKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQY- 458
Cdd:cd14895 311 vqqhlDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNp 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 459 ----------FIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGmDLAACIELIE 528
Cdd:cd14895 391 nkaankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 529 -KPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKpaKGKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNET 607
Cdd:cd14895 470 qRPSGIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 608 VVGLYQKSGLKTLAFLFSGGQAAE-AEGGGGKKGGKKKGSSFQTV--SALFRENLNKLMTNLKSTHPHFVRCLIPNETKT 684
Cdd:cd14895 547 LFSVLGKTSDAHLRELFEFFKASEsAELSLGQPKLRRRSSVLSSVgiGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESA 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 685 PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASaipegQFIDSKKASEkLLGSIDIDHTQykFGH 764
Cdd:cd14895 627 SDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAA-----KNASDATASA-LIETLKVDHAE--LGK 698
|
....*.
gi 67189167 765 TKVFFK 770
Cdd:cd14895 699 TRVFLR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
100-770 |
4.24e-123 |
|
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: 403.60 E-value: 4.24e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRG-KKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 179 GESGAGKTVNTKRVIQYFATiavtgdkkkeeATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 258
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS-----------AKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTnPYDFAYVSQGEITVPSIDDQEELMATDTA 338
Cdd:cd14876 150 GGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLG-LKEYKFLNPKCLDVPGIDDVADFEEVLES 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 339 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQ-----AEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEY 413
Cdd:cd14876 229 LKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 414 VTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFN 493
Cdd:cd14876 309 IEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 494 HHMFVLEQEEYKKEGIDWEFIDFgMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKSNnfqKPKPA 572
Cdd:cd14876 389 DIVFERESKLYKDEGIPTAELEY-TSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSNG---KFKPA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 573 KGKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSG-----GQAAEAeggggkkggkkkgss 647
Cdd:cd14876 464 KVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGvvvekGKIAKG--------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 648 fQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14876 529 -SLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFK 607
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 67189167 728 VLNAsAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14876 608 FLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
100-770 |
5.81e-120 |
|
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: 394.53 E-value: 5.81e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIavtgDKKKEEATSGKMQGTLedqiisanPLLEAFGNAKTVRNDNSSRFGKFIRIHFgATG 259
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----YQDQTEDRLRQPEDVL--------PILESFGHAKTILNANASRFGQVLRLHL-QHG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLItTNPYDFAYVSQGEI-TVPSIDDQEELMATDTA 338
Cdd:cd14896 148 VIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 339 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQ---AEPDGTEVADKAAYLtsLNSADLLKALCYPRVKVGN-EYV 414
Cdd:cd14896 227 LQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevaAVSSWAEIHTAARLL--QVPPERLEGAVTHRVTETPyGRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 415 TKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYF--IGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFF 492
Cdd:cd14896 305 SRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 493 NHHMFVLEQEEYKKEGIDWEFIDfGMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK- 570
Cdd:cd14896 385 SQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQl 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 571 --PAkgkaeahFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFsggQAAEAEGGGGKKGGkkkgssf 648
Cdd:cd14896 463 plPV-------FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF---QEAEPQYGLGQGKP------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 649 qTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd14896 526 -TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGA 604
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 67189167 729 LNASAIPEgqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14896 605 LGSERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-729 |
1.13e-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: 374.19 E-value: 1.13e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKR-QEAPPHIFSISDNAYQFMLTDRE--NQSILI 177
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 178 TGESGAGKTVNTKRVIQYFATIAVTgdkkKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 257
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAAS----PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 258 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPELIEMLLitTNPYDFAYVSQGEITVpsidDQEELMATD 336
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGaSADERLQWHL--PEGAAFSWLPNPERNL----EEDCFEVTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 337 TAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEy 413
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQ- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 414 vtkgqtvQQVYNSV----------GALAKSMYEKMFLWMVTRINQQLDTKQPR-QYFIGVLDIAGFEIFDFNTLEQLCIN 482
Cdd:cd14880 312 -------QQVFKKPcsraecdtrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCIN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 483 FTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLG 561
Cdd:cd14880 385 YANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 562 KSNNFQKPKPAKgkaEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFsggqAAEAEGGGGKKGG 641
Cdd:cd14880 464 GNPCLGHNKLSR---EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLF----PANPEEKTQEEPS 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 642 KKKGSSFQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 721
Cdd:cd14880 537 GQSRAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQN 616
|
....*...
gi 67189167 722 FKQRYKVL 729
Cdd:cd14880 617 FVERYKLL 624
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
106-770 |
1.62e-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: 361.90 E-value: 1.62e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQ-----EAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEEAtsgkmqgtledqIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTDVQSL------------ILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEML-LITTNPYDFAYVSQGeITVPSIDDQEELMATDTA 338
Cdd:cd14886 155 GLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLgFKSLESYNFLNASKC-YDAPGIDDQKEFAPVRSQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 339 VDILgFSADEKVAIYKLTGAVMHYGNMKFKQKQR---EEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVT 415
Cdd:cd14886 234 LEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETII 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 416 KGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHH 495
Cdd:cd14886 313 SPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 496 MFVLEQEEYKKEGIDWEFIDFgMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLyEQHLgKSNNFQkpkPAKG 574
Cdd:cd14886 393 VFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSFI---PGKG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 575 kAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGGGgkkggkkkgssfQTVSAL 654
Cdd:cd14886 467 -SQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKG------------KFLGST 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 655 FRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL---NA 731
Cdd:cd14886 534 FQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 67189167 732 SAIPEGQfiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14886 614 SSQNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-732 |
4.13e-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: 4.13e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKR-QEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYFatIAVTGDKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT- 258
Cdd:cd14906 83 ESGSGKTEASKTILQYL--INTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 259 GKLASADIETYLLEKSRVTFQL-KAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQ-------- 329
Cdd:cd14906 161 GKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFKSQssnknsnh 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 330 -------EELMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQ---REEQAEPDGTEVADKAAYLTSLNSADLL 399
Cdd:cd14906 241 nnktesiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 400 KALCYPRVKVGNE--YVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRIN----QQLDTKQPRQY-------FIGVLDIA 466
Cdd:cd14906 321 QALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINrkfnQNTQSNDLAGGsnkknnlFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 467 GFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPK 545
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 546 ATDTSFKNKlYEQHLGKSNNFQKPKPAKGKaeahFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFS 625
Cdd:cd14906 480 GSEQSLLEK-YNKQYHNTNQYYQRTLAKGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 626 ggqaaeaEGGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEG 705
Cdd:cd14906 555 -------QQITSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNT 627
|
650 660
....*....|....*....|....*..
gi 67189167 706 IRICRKGFPSRILYADFKQRYKVLNAS 732
Cdd:cd14906 628 IKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
101-727 |
2.00e-105 |
|
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: 355.17 E-value: 2.00e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAY----------RGKKRQEAPPHIFSISDNAYQFMLTD 169
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKM-----QGTLEDQIISANPLLEAFGNAKTVRNDNS 244
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPpaspsRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 245 SRFGKFIRIHF-GATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNK----KPELIEMLLITTNPYDFAYVSQG 319
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 320 EITV--PSIDDQEELMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQ--KQREEQAEPDGTEVA----------D 385
Cdd:cd14899 242 LCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 386 KAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQL--------------- 450
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 451 DTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGMDlAACIELIE-K 529
Cdd:cd14899 402 DDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 530 PMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVV 609
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 610 GLYQKSGLKTLAFLFSGGQAAEAEGGGGKKGGKKKGSSFQ-------TVSALFRENLNKLMTNLKSTHPHFVRCLIPNET 682
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAksaiaavSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 67189167 683 KTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-770 |
6.60e-102 |
|
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: 343.91 E-value: 6.60e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 182 GAGKTVNTKRVIQYFATIAVTGDKKkeeATSGKMQgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 261
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAGSVGGV---LSVEKLN--------AALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLL---ITTNPYDFAYVSQgeitvpSIDD----QEELMA 334
Cdd:cd01386 152 ASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHlnqLAESNSFGIVPLQ------KPEDkqkaAAAFSK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 335 TDTAVDILGFSADEKVAIYKLTGAVMHYGN---MKFKQKQREEQAEPdgtEVADKAAYLTSLNSADLLKALCYPRVKVGN 411
Cdd:cd01386 226 LQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 412 EYVTKGQTVQQVYNS------------VGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN----- 474
Cdd:cd01386 303 QQSTTSSGQESPARSssggpkltgveaLEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrg 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 475 -TLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGMDLAACIELIEK---------------PMGIFSILE 538
Cdd:cd01386 383 aTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 539 EECMFPKATDTSFKNKLYeQHLGKSNNFQKPKPAKgKAEA--HFSLVHYAGT--VDYNIIGWLDKNK-DPLNETVVGLYQ 613
Cdd:cd01386 463 EEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLR-RSEGplQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQ 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 614 KSGLKTlAFLFSGGQAAEAeggggkkggkkkgsSFQtvsalfrenLNKLMTNLKSTHPHFVRCLIPN------ETKTPGA 687
Cdd:cd01386 541 ESQKET-AAVKRKSPCLQI--------------KFQ---------VDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSP 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 688 MEHELVLH------QLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL----NASAIPEGQFIDSKKASEKLLGSIDIDH 757
Cdd:cd01386 597 AAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLapplTKKLGLNSEVADERKAVEELLEELDLEK 676
|
730
....*....|...
gi 67189167 758 TQYKFGHTKVFFK 770
Cdd:cd01386 677 SSYRIGLSQVFFR 689
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-770 |
1.91e-100 |
|
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: 339.09 E-value: 1.91e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 102 VLYNLKERYAAWMI-YTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEA-PPHIFSISDNAY-QFMLTDRENQSILIT 178
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 179 GESGAGKTVNTKRVIQYFAtiavtgdKKKEEATSGKMQGTLEDQIIS----ANPLLEAFGNAKTVRNDNSSRFGKFIRIH 254
Cdd:cd14875 83 GESGSGKTENAKMLIAYLG-------QLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 255 F-GATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAYVSQGEITV------PSID 327
Cdd:cd14875 156 FdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 328 DQEELMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQReeqaepDGTEVADKAAYLTSLNSADLLKAL---CY 404
Cdd:cd14875 236 DAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN------DKAQIADETPFLTACRLLQLDPAKlreCF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 405 pRVKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQ----QLDTKQPRqyFIGVLDIAGFEIFDFNTLEQLC 480
Cdd:cd14875 310 -LVKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNAsitpQGDCSGCK--YIGLLDIFGFENFTRNSFEQLC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 481 INFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQH 559
Cdd:cd14875 387 INYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQW 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 560 LGKSNNFQKPKPAkgkAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGgggkk 639
Cdd:cd14875 466 ANKSPYFVLPKST---IPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRK----- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 640 ggkkkgssfQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILY 719
Cdd:cd14875 538 ---------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPI 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 720 ADF-KQRYKVLNASAIPEGQFIDSKKASEKLLGS----IDIDHTQYKFGHTKVFFK 770
Cdd:cd14875 609 EQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
101-770 |
3.52e-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: 314.45 E-value: 3.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYR---GKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 177
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 178 TGESGAGKTVNTKRVIQYFAtiavtgdkkkeeATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 257
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLT------------CRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 258 TGK-LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITtNPYDFAYVSQGE----ITVPSIDDQEEL 332
Cdd:cd14878 150 RKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTMredvSTAERSLNREKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 333 MATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNE 412
Cdd:cd14878 229 AVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 413 YVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRIN----QQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKL 488
Cdd:cd14878 309 MIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclqSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 489 QQFFNHHMFVLEQEEYKKEGIDWEFI-DFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSNN-- 565
Cdd:cd14878 389 HHYINEVLFLQEQTECVQEGVTMETAySPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKL--QSLLESSNtn 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 566 --FQKPKPAKGKAE-----AHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFsggqaaeaeggggk 638
Cdd:cd14878 467 avYSPMKDGNGNVAlkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF-------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 639 kggkkkGSSFQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 718
Cdd:cd14878 533 ------QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLS 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 67189167 719 YADFKQRYKVLnASAIPEGQfidsKKASEKLLGSIDIDHTQ---YKFGHTKVFFK 770
Cdd:cd14878 607 FSDFLSRYKPL-ADTLLGEK----KKQSAEERCRLVLQQCKlqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-770 |
1.25e-88 |
|
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: 303.86 E-value: 1.25e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEvvaaYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 182 GAGKTVNTKRVIQYFatiaVTGDKKKEEATSgkmqgTLEDqiisANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 261
Cdd:cd14937 79 GSGKTEASKLVIKYY----LSGVKEDNEISN-----TLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPyDFAYVSQGEITVPSIDDQEELMATDTAVDI 341
Cdd:cd14937 146 VSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 342 LGFSaDEKVAIYKLTGAVMHYGNMKFKQ-----KQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd14937 225 MNMH-DMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 417 GQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 497 FVLEQEEYKKEGIDWEFIDFGMDlAACIELIEKPMGIFSILEEECMFPKATDTSfknkLYEQHLGKSNNFQKPKPAKGKA 576
Cdd:cd14937 384 YEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKYASTKKDI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 577 EAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGGGgkkggkkkgssfQTVSALFR 656
Cdd:cd14937 459 NKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK------------NLITFKYL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 657 ENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRIcRKGFPSRILYADFKQRYKVLNASAIPE 736
Cdd:cd14937 527 KNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKD 605
|
650 660 670
....*....|....*....|....*....|....
gi 67189167 737 GQFIDSKKASEKLLGSIDIDhtQYKFGHTKVFFK 770
Cdd:cd14937 606 SSLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
101-733 |
4.14e-88 |
|
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: 300.28 E-value: 4.14e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvynpEVVAAYRGKKRQE-----APPHIFSISDNAYQFMLTdRENQSI 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPY--------ETIYGAGAMKAYLknyshVEPHVYDVAEASVQDLLV-HGNQTI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 176 LITGESGAGKTVNTKRVIQYFatiaVTGDKKKEeatsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14898 73 VISGESGSGKTENAKLVIKYL----VERTASTT---------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 256 gaTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpeliemLLITTNPYDFAYVSQGEITVpsIDDQEELMAT 335
Cdd:cd14898 140 --DGKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 336 DTAVDILGFSADEkvAIYKLTGAVMHYGNMKFKQkqreeqaepDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVT 415
Cdd:cd14898 210 CSAMKSLGIANFK--SIEDCLLGILYLGSIQFVN---------DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 416 KGQTVQqVYNSV-------GALAKSMYEKMFLWMVTRINQQLDTKQPRQyfIGVLDIAGFEIFDFNTLEQLCINFTNEKL 488
Cdd:cd14898 279 KGETIE-VFNTLkqartirNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKI 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 489 QQFFNHHMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNfqk 568
Cdd:cd14898 356 QNDFIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIKKYLNGFINT--- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 569 pkpakgKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNetvVGLYQKSGLKTlaflfsggqaaeaeggggkkggkkkGSSF 648
Cdd:cd14898 432 ------KARDKIKVSHYAGDVEYDLRDFLDKNREKGQ---LLIFKNLLIND-------------------------EGSK 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 649 QTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd14898 478 EDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRI 557
|
....*
gi 67189167 729 LNASA 733
Cdd:cd14898 558 LGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
100-770 |
2.47e-87 |
|
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: 302.72 E-value: 2.47e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAA--------WMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRE 171
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 172 NQSILITGESGAGKTVNTKRVIQYFATIAvtgDKKKEEATSGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 251
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVS---DRRHGADSQG-----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKML 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 252 RIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLlittnpydfayvSQGEiTVPSIDDQEE 331
Cdd:cd14887 153 LLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKS------------SAGE-GDPESTDLRR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 332 LMATDTAVDILGfsaDEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADK---AAYLTSLNS----- 395
Cdd:cd14887 220 ITAAMKTVGIGG---GEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADrshSSEVKCLSSglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 396 -------ADLLKALCYPRVKVGNEYVTKGQTVQQV------YNSVGALA------KSMYEKMFLWMVTRINQQLDTKQPR 456
Cdd:cd14887 297 easrkhlKTVARLLGLPPGVEGEEMLRLALVSRSVretrsfFDLDGAAAardaacKNLYSRAFDAVVARINAGLQRSAKP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 457 QY--------------FIGVLDIAGFEIF---DFNTLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFI----D 515
Cdd:cd14887 377 SEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsafP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 516 FGMDLAAC--------IELIEKP--------------MGIFSILEEE-CMFPKATDTSFKNKLYEQHLGK----SNNFQK 568
Cdd:cd14887 457 FSFPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKN 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 569 PKPAKGKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNEtvvglyqksglkTLAFLFSGGQAAEAEGGGGKKGGKKKGSS- 647
Cdd:cd14887 537 ITPALSRENLEFTVSHFACDVTYDARDFCRANREATSD------------ELERLFLACSTYTRLVGSKKNSGVRAISSr 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 648 FQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14887 605 RSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYE 684
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 67189167 728 VLNASAIPEgqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14887 685 TKLPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
106-769 |
2.06e-86 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 297.54 E-value: 2.06e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 106 LKERYAAWMIYTY---SGLfcVTVNPYKWLPVYNPEVVAAYR-------GKKRQEAPPHIFSISDNAYQFMLTDRENQSI 175
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 176 LITGESGAGKTVNTKRVIQYFATIAVTGDKkkeeatsgkmqGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 254
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSSHSKK-----------GTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 255 FGATGKLASADIETYLLEKSRVTfQLKA-ERSYHIFYQIMSNKKPELIEMLLItTNPYDFA----YVSQGEITVPSIDDQ 329
Cdd:cd14879 157 FNERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGL-DDPSDYAllasYGCHPLPLGPGSDDA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 330 EELMATDTAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRV 407
Cdd:cd14879 235 EGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKTK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 408 KVGNEYVTkgqtvqqVY-NSVGA------LAKSMYEKMFLWMVTRINQQL-DTKQPRQYFIGVLDIAGFEIFD---FNTL 476
Cdd:cd14879 315 LVRKELCT-------VFlDPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSstgGNSL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFgMDLAACIELI-EKPMGIFSILEEEC-MFPKATDTSFKNK 554
Cdd:cd14879 388 DQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDEQMLEA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 555 LYEQHLGKSNNFQKPKPAKGKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNetvvglyqkSGLKTLafLFSGGQaaeaeg 634
Cdd:cd14879 467 LRKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLS---------PDFVNL--LRGATQ------ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 635 gggkkggkkkgssfqtvsalFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 714
Cdd:cd14879 530 --------------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYV 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 67189167 715 SRILYADFKQRYKvlnasaiPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFF 769
Cdd:cd14879 590 VSLEHAEFCERYK-------STLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
100-718 |
8.77e-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: 261.38 E-value: 8.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEA-------PPHIFSISDNAYQFMLTDRE 171
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 172 NQSILITGESGAGKTVNTKRVIQYFATIavTGDKKKEEatsgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 251
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI--QTDSQMTE---------RIDKLIYINNILESMSNATTIKNNNSSRCGRIN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 252 RIHF---------GATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPE------------LIEMLLITTNP 310
Cdd:cd14884 150 LLIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEdlarrnlvrncgVYGLLNPDESH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 311 YDFAYVSQGEITVPSIDDQEELMATDT--------AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQkqreeqaepdgte 382
Cdd:cd14884 230 QKRSVKGTLRLGSDSLDPSEEEKAKDEknfvallhGLHYIKYDERQINEFFDIIAGILHLGNRAYKA------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 383 vadkAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRIN---------QQLDTK 453
Cdd:cd14884 297 ----AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekDESDNE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 454 QPRQY---FIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDfgmdLAACIELIEKP 530
Cdd:cd14884 373 DIYSIneaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDV----APSYSDTLIFI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 531 MGIFSILEEECMFP----KATDTSFKNKLY----EQHLGKSNNFQK--PKPAKGKAEAH------FSLVHYAGTVDYNII 594
Cdd:cd14884 449 AKIFRRLDDITKLKnqgqKKTDDHFFRYLLnnerQQQLEGKVSYGFvlNHDADGTAKKQnikkniFFIRHYAGLVTYRIN 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 595 GWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQaaeaeggggkkggkkkGSSFQTVSALFRENLNKLMTNLKSTHPHFV 674
Cdd:cd14884 529 NWIDKNSDKIETSIETLISCSSNRFLREANNGGN----------------KGNFLSVSKKYIKELDNLFTQLQSTDMYYI 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 67189167 675 RCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 718
Cdd:cd14884 593 RCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
101-750 |
3.48e-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: 249.65 E-value: 3.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPvyNPEVVAAYRGKKRQeapPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 181 SGAGKTVNTKRVI-QYFAtiaVTGDKKKEEATSgkmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgATG 259
Cdd:cd14881 77 SGSGKTYASMLLLrQLFD---VAGGGPETDAFK---------HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKP-ELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTA 338
Cdd:cd14881 144 ALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQeERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 339 VDILGFSADEKVAIYkltGAVMHYGNMKFKQKQREEQAEPDGTEVaDKAAYLTSLNSADLLKALcYPRVKVgneyvTKGQ 418
Cdd:cd14881 224 LGILGIPFLDVVRVL---AAVLLLGNVQFIDGGGLEVDVKGETEL-KSVAALLGVSGAALFRGL-TTRTHN-----ARGQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 419 TVQQVyNSVG-------ALAKSMYEKMFLWMVTRINQQLD-----TKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNE 486
Cdd:cd14881 294 LVKSV-CDANmsnmtrdALAKALYCRTVATIVRRANSLKRlgstlGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 487 KLQQFFNHHMFVLEQEEYKKEGIDWEF-IDFgMDLAACIELIEK-PMGIFSILEEECMfPKATDTSFKNKLYEQHlgKSN 564
Cdd:cd14881 373 TMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQH--RQN 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 565 N-FQKPKPAKGKAeahFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKsglKTLAFlfsggqaaeaeggggkkggkk 643
Cdd:cd14881 449 PrLFEAKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK---QNCNF--------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 644 kgsSFQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFK 723
Cdd:cd14881 502 ---GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFN 578
|
650 660
....*....|....*....|....*..
gi 67189167 724 QRYKVLnASAIPEGQFIDSKKASEKLL 750
Cdd:cd14881 579 ARYRLL-APFRLLRRVEEKALEDCALI 604
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
106-713 |
2.75e-64 |
|
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: 233.06 E-value: 2.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 184
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 185 KTVNTKRVIQYFATIAVTGDKkkeeatsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASA 264
Cdd:cd14905 85 KSENTKIIIQYLLTTDLSRSK------------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 265 DIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPELIEMLLITTNPYDfaYVSQ-GEITVPSIDDQEELMATDTAVDIL 342
Cdd:cd14905 153 KLYSYFLDENRVTYQNKGERNFHIFYQFLKGiTDEEKAAYQLGDINSYH--YLNQgGSISVESIDDNRVFDRLKMSFVFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 343 GFSADEKVAIYKLTGAVMHYGNMKFKQKQREeqaepdgTEVADKaaylTSLNSadLLKALCYPRVKVGNEYVT-KGQTVQ 421
Cdd:cd14905 231 DFPSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDR----TLIES--LSHNITFDSTKLENILISdRSMPVN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 422 QVYNSVGALAKSMYEKMFLWMVTRINQQLdtkQPRQY--FIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14905 298 EAVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 500 EQEEYKKEGIDWEFIDFGMDLAACIELIEKpmgIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNFQKpKPAKgkaeah 579
Cdd:cd14905 375 EQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL-QNFLSRHHLFGK-KPNK------ 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 580 FSLVHYAGTVDYNIIGWLDKNKDP-------------------------LNETVVGLYQ---------KSGLKTLAFLFS 625
Cdd:cd14905 444 FGIEHYFGQFYYDVRGFIIKNRDEilqrtnvlhknsitkylfsrdgvfnINATVAELNQmfdakntakKSPLSIVKVLLS 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 626 GGQAAEAEGGGGKKG-------------GKKKGSSFQTVSAlfrenLNKLMTNlKSTHPHFVRCLIPNETKTPGAMEHEL 692
Cdd:cd14905 524 CGSNNPNNVNNPNNNsgggggggnsgggSGSGGSTYTTYSS-----TNKAINN-SNCDFHFIRCIKPNSKKTHLTFDVKS 597
|
650 660
....*....|....*....|.
gi 67189167 693 VLHQLRCNGVLEGIRICRKGF 713
Cdd:cd14905 598 VNEQIKSLCLLETTRIQRFGY 618
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
101-729 |
3.52e-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: 3.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYrgkkrqeappHIFSISDNAYQFMLTDREN-QSILITG 179
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 180 ESGAGKTVNTKRVIQYfatiaVTGDKKKEEATSgkmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 259
Cdd:cd14874 72 ESGSGKSYNAFQVFKY-----LTSQPKSKVTTK---------HSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITtNPYDFAYVSQGEITVPSIDDQEELMATDTAV 339
Cdd:cd14874 138 LTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLEDAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 340 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKqREEQAEPDGTEVADKA-----AYLTSLNSADLLKALCyPRVKVGNEYv 414
Cdd:cd14874 217 HVLGFSDDHCISIYKIISTILHIGNIYFRTK-RNPNVEQDVVEIGNMSevkwvAFLLEVDFDQLVNFLL-PKSEDGTTI- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 415 tkgqTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLdtKQPRQY-FIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFN 493
Cdd:cd14874 294 ----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHL--KCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 494 HHMFVLEQEEYKKEGIDwefIDFGM----DLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSnNFQK 568
Cdd:cd14874 368 KHSFHDQLVDYAKDGIS---VDYKVpnsiENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-SYGK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 569 pkpAKGKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGgggkkggkkkgssF 648
Cdd:cd14874 444 ---ARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDM-------------I 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 649 QTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd14874 508 VSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRC 587
|
.
gi 67189167 729 L 729
Cdd:cd14874 588 L 588
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
102-770 |
2.12e-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: 2.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 182 GAGKTVNTKRVIQYFATIavtgdkkkeeatsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 261
Cdd:cd14882 83 YSGKTTNARLLIKHLCYL-------------GDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMS--NKKPELIEMLLITTNPYDFAYVSQG-------------EITVPSI 326
Cdd:cd14882 150 SGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 327 DDQEELMAtdtavdILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREeqAEPDGTEVADKAAYLTSLNSADLLKALCYPR 406
Cdd:cd14882 230 KEFEEILK------DLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 407 VKVGNEYVTKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTkqPR-----QYFIGVLDIAGFEIFDFNTLEQLCI 481
Cdd:cd14882 302 LIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 482 NFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEecmfpkaTDTSFKNKLYEQHLG 561
Cdd:cd14882 380 NTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-------ASRSCQDQNYIMDRI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 562 KSNNFQKPKPAKGKaeaHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAaeaeggggkkgg 641
Cdd:cd14882 453 KEKHSQFVKKHSAH---EFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQV------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 642 kkkgSSFQTVSALFR----ENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRI 717
Cdd:cd14882 518 ----RNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRI 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 67189167 718 LYADFKQRYKVLnasAIPEGQFIDSKKASEKLLgSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14882 594 PFQEFLRRYQFL---AFDFDETVEMTKDNCRLL-LIRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
103-727 |
6.80e-63 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 230.63 E-value: 6.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQ----------EAPPHIFSISDNAYQFMLTDREN 172
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 173 QSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIR 252
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 253 IHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKK--PELIEMLLITTNPYDFAYVSQG--EITVPSID- 327
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFALDa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 328 -DQEELMATDTAVDIlgfSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDG--TEVADKAAYLTSLNSADLLKALC- 403
Cdd:cd14893 244 rDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGAnsTTVSDAQSCALKDPAQILLAAKLl 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 404 ---------YPRV-----KVGNEYVT--KGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQL----DTKQPRQYFIG-- 461
Cdd:cd14893 321 evepvvldnYFRTrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVINsq 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 462 ---VLDIAGFEIFD--FNTLEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEG--IDWEFIDFGMDLAACIELIE- 528
Cdd:cd14893 401 gvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFEd 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 529 KPMGIFSILEEECMFPKATDTSFKNKLY----------EQHLGKSNNFQKPKPAKgKAEAHFSLVHYAGTVDYNIIGWLD 598
Cdd:cd14893 481 KPFGIFDLLTENCKVRLPNDEDFVNKLFsgneavgglsRPNMGADTTNEYLAPSK-DWRLLFIVQHHCGKVTYNGKGLSS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 599 KNKDPLNETVVGLYQKSGLKTLAFLFSGGQAA--EAEGGGGKKGGKKKGSSFQTVSALFRENLN--------------KL 662
Cdd:cd14893 560 KNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAasSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadAL 639
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67189167 663 MTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14893 640 LHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
122-253 |
1.09e-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: 208.74 E-value: 1.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 122 FCVTVNPYKWLPVYNPEVV-AAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIA 200
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 201 VTGDKKKEEATS---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 ... |
100-768 |
1.49e-43 |
|
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: 171.17 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYR-GKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 179 GESGAGKTVNTKRVIQYFA-------------TIAVTGDKKKEEATsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAyqvkgsrrlptnlNDQEEDNIHNEENT--DYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 246 RFGKFIRIHFgATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITtNPYDFAYVSQGEITVPS 325
Cdd:cd14938 159 RFSKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK-NIENYSMLNNEKGFEKF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 326 IDDQEELMATDTAVDILGFSADEKVAIYKLTGAVMHYGN-------------MKFKQKQRE----------EQAEPDGTE 382
Cdd:cd14938 237 SDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 383 VADKAAYLTS-LNSADLLKALCYPRVK-VGNEYV-TKGQTVQQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYF 459
Cdd:cd14938 317 ENVKNLLLACkLLSFDIETFVKYFTTNyIFNDSIlIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 460 ---IGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPM--GIF 534
Cdd:cd14938 397 tnyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 535 SILEEECMfPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAhFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQK 614
Cdd:cd14938 477 SLLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 615 SGLKTLAFLF------SGGQAAEAEGGGGKKG-----GKKKGSSFQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETK 683
Cdd:cd14938 555 SENEYMRQFCmfynydNSGNIVEEKRRYSIQSalklfKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 684 TP-GAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAsaipegqfiDSKKASEKLLGSIDIDHTQYKF 762
Cdd:cd14938 635 RElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMI 705
|
....*.
gi 67189167 763 GHTKVF 768
Cdd:cd14938 706 GNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1177-1930 |
8.70e-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: 8.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1177 KMRRdlEEATLQHEATAAALrKKHADSVAELGEQIDNLQRVKQKLEK-----------EKSELKMEIDDLASNMETVSKA 1245
Cdd:TIGR02168 171 KERR--KETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1246 KGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEE 1325
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1326 ESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDAE 1405
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR-SKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1406 EHVEavnskcaSLEKTKQRLQNEVEDLmiDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTEL 1485
Cdd:TIGR02168 407 ARLE-------RLEDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1486 fkvkNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIdqekSELQASLEEAEASLEHEEGKILRI 1565
Cdd:TIGR02168 478 ----DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVL----SELISVDEGYEAAIEAALGGRLQA 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1566 QL--ELNQVKSEID----------RKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEI-- 1631
Cdd:TIGR02168 550 VVveNLNAAKKAIAflkqnelgrvTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvd 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1632 QLNHANRQAAEAIRNLRNTqgMLKDTQLHLDDALRGQDDlKEQLAMVERRAnlmqaEIEELRASLEQTERSRRVAEQELL 1711
Cdd:TIGR02168 630 DLDNALELAKKLRPGYRIV--TLDGDLVRPGGVITGGSA-KTNSSILERRR-----EIEELEEKIEELEEKIAELEKALA 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1712 DASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNME 1791
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1792 QTVKDLQHRLDEAEQlalkggkkQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDL 1871
Cdd:TIGR02168 782 AEIEELEAQIEQLKE--------ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 1872 VDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSRE 1930
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
861-1746 |
3.70e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 127.48 E-value: 3.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 861 EKAKEDLAKSEAKRKELEEKMvalmqekNDLQLQVQA--EADGLADAEERCDQ--LIKTKIQLEAKIKELTERAEDEEEI 936
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQL-------KSLERQAEKaeRYKELKAELRELELalLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 937 NAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQA 1016
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1017 EEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQS 1096
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1097 KIEDEQALGMQLQKKIKELQARIEELEEEIEAERasRAKAEKQRSDLSRELEEISERLEEAGGA---TSAQIEMNKKREA 1173
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEE--LEELQEELERLEEALEELREELEEAEQAldaAERELAQLQARLD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1174 EFQKMRRDLEEATlQHEATAAALRKKHADSVAELGEQIdnlqRVKQKLEKEKSEL------KMEIDDLASNMETVSKAKG 1247
Cdd:TIGR02168 493 SLERLQENLEGFS-EGVKALLKNQSGLSGILGVLSELI----SVDEGYEAAIEAAlggrlqAVVVENLNAAKKAIAFLKQ 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1248 NLEKMC----------RTLEDQLSEVKTKEEEQQRLINELSTQKARLH-TESGEFSR-----QLDEKDAMVSQLSRGKQA 1311
Cdd:TIGR02168 568 NELGRVtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkALSYLLGGvlvvdDLDNALELAKKLRPGYRI 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1312 FTQQIEELKRQlEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEvaqwrtkyetdaiqrTEELE 1391
Cdd:TIGR02168 648 VTLDGDLVRPG-GVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKE---------------LEELE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1392 EAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKqrnfdkvLAEWKQKYEETQAEL 1471
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER-------LEEAEEELAEAEAEI 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1472 EASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEA 1551
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1552 EASLEheegkilriqlelnqvksEIDRKIAEKDEEIDQLKRnHLRVVESMQSTLDAEIRSRNDAlriKKKMEGDLNEMEI 1631
Cdd:TIGR02168 865 EELIE------------------ELESELEALLNERASLEE-ALALLRSELEELSEELRELESK---RSELRRELEELRE 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1632 QLNHANRQAAEAIRNLRNTQGML-KDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEEL-RASLEqtersrrvAEQE 1709
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgPVNLA--------AIEE 994
|
890 900 910
....*....|....*....|....*....|....*..
gi 67189167 1710 LLDASERVQLLHTQNTSLINTKKKLETDISQIQGEME 1746
Cdd:TIGR02168 995 YEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAR 1031
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1149-1875 |
5.90e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 120.55 E-value: 5.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1149 EISERLEEAGGATSAqiemNKKREAEFQKMRRDLEEATLQHEataaalRKKHADSVAELGEQIDNLQRVKQKLEKEKSEL 1228
Cdd:TIGR02168 217 ELKAELRELELALLV----LRLEELREELEELQEELKEAEEE------LEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1229 KMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRG 1308
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1309 KQAFTQQIEELKRQLEEESKAKNALAHALQSAR----------HDCDLLREQYEEEQEA---------KAELQRAMSKAN 1369
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNneierlearlERLEDRRERLQQEIEEllkkleeaeLKELQAELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1370 SEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDL----------------- 1432
Cdd:TIGR02168 447 EELEELQEELE-RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVkallknqsglsgilgvl 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1433 -----------------------MIDVERSNAACAALDK-KQRNFDKV----LAEWK-QKYEETQAELEASQKESRSLST 1483
Cdd:TIGR02168 526 selisvdegyeaaieaalggrlqAVVVENLNAAKKAIAFlKQNELGRVtflpLDSIKgTEIQGNDREILKNIEGFLGVAK 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1484 ELFKVKNAYE-------------ESLDQLETLKRENK-------------------------------NLQQEISDLTEQ 1519
Cdd:TIGR02168 606 DLVKFDPKLRkalsyllggvlvvDDLDNALELAKKLRpgyrivtldgdlvrpggvitggsaktnssilERRREIEELEEK 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1520 IAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRkiaeKDEEIDQLKRNHLRVVE 1599
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEA 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1600 SMQSTLDAEIRSRNDALRIKKKMEgdlnEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVE 1679
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIE----ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1680 RRANLMQAEIEELRASLEQtersrrvAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKA 1759
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIES-------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1760 KKAItdaammaEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLAL-------KGGKKQIQKLEARVRELENEVEN 1832
Cdd:TIGR02168 911 SELR-------RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLeeaealeNKIEDDEEEARRRLKRLENKIKE 983
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 67189167 1833 EQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKL 1875
Cdd:TIGR02168 984 LGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1612 |
2.12e-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: 118.62 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 847 AETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIKEL 926
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 927 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQEA 1006
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1007 HQQTLDDLQAEEDKVNTLTKAKTKL-----EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLD 1081
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1082 EKLKKKEFEMSNLQSKIEDEQalgmQLQKKIKELqarieeleeeieAERASRAKAEKQR-SDLSRELEEISERLEEAGGA 1160
Cdd:TIGR02168 482 RELAQLQARLDSLERLQENLE----GFSEGVKAL------------LKNQSGLSGILGVlSELISVDEGYEAAIEAALGG 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1161 TSAQIEMNKKREAefqkmrRDLEEATLQHEATAAAL----RKKHADSVAELGEQIDNLQRVKQ---KLEKEKSELKMEI- 1232
Cdd:TIGR02168 546 RLQAVVVENLNAA------KKAIAFLKQNELGRVTFlpldSIKGTEIQGNDREILKNIEGFLGvakDLVKFDPKLRKALs 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1233 ---------DDLASNMETVSK-------------------------AKGNLEKMCRTLEdqLSEVKTKEEEQQRLINELS 1278
Cdd:TIGR02168 620 yllggvlvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsAKTNSSILERRRE--IEELEEKIEELEEKIAELE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1279 TQKARLhtesgefSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAK 1358
Cdd:TIGR02168 698 KALAEL-------RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1359 AELQRAMSKANSEVAQWRtkyetdaiQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVER 1438
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELE--------AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1439 SNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTE 1518
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1519 QIAEGGKHIHELE-KIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDR-------------KIAEKD 1584
Cdd:TIGR02168 923 KLAQLELRLEGLEvRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaieeyeELKERY 1002
|
810 820 830
....*....|....*....|....*....|.
gi 67189167 1585 EEIDQLKRNHLRVVESMQST---LDAEIRSR 1612
Cdd:TIGR02168 1003 DFLTAQKEDLTEAKETLEEAieeIDREARER 1033
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1593 |
3.65e-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: 117.86 E-value: 3.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 844 LKSAETEKEMANMKEDFEKAKEDLA----KSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQL 919
Cdd:TIGR02169 191 LIIDEKRQQLERLRREREKAERYQAllkeKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 920 EAKIKELTERAED--EEEINA------ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDE 991
Cdd:TIGR02169 271 EQLLEELNKKIKDlgEEEQLRvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 992 NIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTM 1071
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1072 DIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLS------- 1144
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEervrggr 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1145 -----------------RELEEISER----LEEAGGA------------TSAQIEMNKKREA------EFQKMRRDLEEA 1185
Cdd:TIGR02169 511 aveevlkasiqgvhgtvAQLGSVGERyataIEVAAGNrlnnvvveddavAKEAIELLKRRKAgratflPLNKMRDERRDL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1186 TLQHEATAAALrkkhADSVAELGEQIDNLQR-------VKQKLEKEKS--------ELKMEIDDLASNMETVSKAKGNLE 1250
Cdd:TIGR02169 591 SILSEDGVIGF----AVDLVEFDPKYEPAFKyvfgdtlVVEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGI 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1251 KMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAK 1330
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1331 NALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQDAEEHVEA 1410
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL---SKLEEEVSRIEARLREIEQKLNR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1411 VNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKN 1490
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1491 AYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHE----------LEKIKKQIDQEKSELQAsLEEAE--ASLEHE 1558
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRA-LEPVNmlAIQEYE 982
|
810 820 830
....*....|....*....|....*....|....*.
gi 67189167 1559 EGKILRIQLELNQVKSEIDRK-IAEKDEEIDQLKRN 1593
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKaILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1316-1935 |
2.09e-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: 115.54 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1316 IEELKRQLEE-ESKAKNALA-HALQSA--RHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETdAIQRTEELE 1391
Cdd:TIGR02168 195 LNELERQLKSlERQAEKAERyKELKAElrELELALLVLRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1392 EAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAEL 1471
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1472 EASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEA 1551
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1552 EASLEHEEGKILRIQLE--------LNQVKSEIDRKIAEKDEEIDQLKRNH------LRVVESMQSTLDAEIRSRNDALR 1617
Cdd:TIGR02168 434 ELKELQAELEELEEELEelqeelerLEEALEELREELEEAEQALDAAERELaqlqarLDSLERLQENLEGFSEGVKALLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1618 IKKKMEGDLN--------------EMEIQL-----------NHANRQAAEAIR--------------------------- 1645
Cdd:TIGR02168 514 NQSGLSGILGvlselisvdegyeaAIEAALggrlqavvvenLNAAKKAIAFLKqnelgrvtflpldsikgteiqgndrei 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1646 --NLRNTQGMLKD-----TQLH---------------LDDALRGQDDLKEQLAMV-----------------ERRANLMQ 1686
Cdd:TIGR02168 594 lkNIEGFLGVAKDlvkfdPKLRkalsyllggvlvvddLDNALELAKKLRPGYRIVtldgdlvrpggvitggsAKTNSSIL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1687 A---EIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAI 1763
Cdd:TIGR02168 674 ErrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1764 TDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKG 1843
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1844 LRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNK 1923
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
730
....*....|..
gi 67189167 1924 LRVKSREVHTKV 1935
Cdd:TIGR02168 913 LRRELEELREKL 924
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1314-1915 |
7.43e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.49 E-value: 7.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1314 QQIEELKRQ---------LEEESKAK--NALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVaqwrtkyetd 1382
Cdd:COG1196 200 RQLEPLERQaekaeryreLKEELKELeaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL---------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1383 aiqrtEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQ 1462
Cdd:COG1196 270 -----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1463 KYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKS 1542
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1543 ELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRsRNDALRIKKKM 1622
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-LLLLLEAEADY 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1623 EGDLNEMEIQLNHANRQ--------------AAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAmvERRANLMQAE 1688
Cdd:COG1196 504 EGFLEGVKAALLLAGLRglagavavligveaAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA--GRATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1689 IEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAM 1768
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1769 MAEELKKEQDTSahLERMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHE 1848
Cdd:COG1196 662 LTGGSRRELLAA--LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67189167 1849 RRVKELTYQTEEDRKNVLRLQDLvDKLQTKVKAYKRQAEEAEeqsNVNLAkfrKIQhELEEAEERAD 1915
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDL-EELERELERLEREIEALG---PVNLL---AIE-EYEELEERYD 798
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1257-1854 |
2.45e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.57 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1257 EDQLSEVKTKEEEQQRLINELSTQKARLHTESG------EFSRQLDEKDAMVSQLSRgkQAFTQQIEELKRQLEEESKAK 1330
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLERQAEkaeryrELKEELKELEAELLLLKL--RELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1331 NALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQDAEEHVEA 1410
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR--------LEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1411 VNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKN 1490
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1491 AYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELN 1570
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1571 QVKSEIDRKIAEKDE---EIDQLKRNHLRVVESMQSTLDAEIRSRNDALRikKKMEGDLNEMEIQLNHANRQAAEAIRNL 1647
Cdd:COG1196 488 EAAARLLLLLEAEADyegFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE--AALEAALAAALQNIVVEDDEVAAAAIEY 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1648 RNTQGMLKDTQLHLD--DALRGQDDLKEQLAMVERRANLMQAEIE--ELRASLEQTERSRRVAEQELLDASERVQLLHTQ 1723
Cdd:COG1196 566 LKAAKAGRATFLPLDkiRARAALAAALARGAIGAAVDLVASDLREadARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1724 NTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDE 1803
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 67189167 1804 AEQLALKGGKKQIQKLEARVRELENEVENEQKR--NIEAVKG-LRKHERRVKEL 1854
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEELPEppDLEELEReLERLEREIEAL 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1123-1913 |
2.13e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 108.62 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1123 EEEIEAERASRAKAEKQRSDLSRELEEISERLEEaggatsAQIEMNKKReaEFQKMRRDLEEAtlqhEATAAALRKKHAD 1202
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLER------LRREREKAE--RYQALLKEKREY----EGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1203 -SVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKakgnleKMCRTLEDQLSEVKTKeeeqqrlINELSTQK 1281
Cdd:TIGR02169 237 rQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK------KIKDLGEEEQLRVKEK-------IGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1282 ARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAEL 1361
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1362 QRamskansEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVErsna 1441
Cdd:TIGR02169 384 RD-------ELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK---- 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1442 acaALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTElfkvknayeesLDQLETLKRENKNLQQEISDLTEQIA 1521
Cdd:TIGR02169 452 ---KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE-----------LAEAEAQARASEERVRGGRAVEEVLK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1522 EGGKHIHELekiKKQIDQEKSELQASLEEAEAS------LEHEEGKILRIQ------------LELNQVKSE--IDRKIA 1581
Cdd:TIGR02169 518 ASIQGVHGT---VAQLGSVGERYATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrrkagratfLPLNKMRDErrDLSILS 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1582 EK------------DEEIDQLKRNHLR---VVESMQS-----------TLDAEI-----------RSRNDALRIKKKMEG 1624
Cdd:TIGR02169 595 EDgvigfavdlvefDPKYEPAFKYVFGdtlVVEDIEAarrlmgkyrmvTLEGELfeksgamtggsRAPRGGILFSRSEPA 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1625 DLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRR 1704
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1705 VAEQELLDASERVQLLHTQNTSLINTKKKLETDIS-----QIQGEMEDIVQE-------ARNAEEKAKKAITDAAMMAEE 1772
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEvsriearLREIEQKLNRLTLEKEYLEKE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1773 LKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQlalkggkkQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVK 1852
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 67189167 1853 ELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNvNLAKFRKIQHELEEAEER 1913
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLEDVQAELQRVEEE 966
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
223-715 |
4.01e-23 |
|
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: 107.52 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 223 IISANPLLEAFGNAKTVRNDNSSRFGKF--IRIHFGATG---KLASADIETYLLEKSRVTFQL------KAERSYHIFYQ 291
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 292 IMS--NKKPEL----IEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDT--------AVDILGFSADEKVAIYKLTG 357
Cdd:cd14894 329 MVAgvNAFPFMrllaKELHLDGIDCSALTYLGRSDHKLAGFVSKEDTWKKDVerwqqvidGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 358 AVMHYGNMKFKQKQREEQAEPDGT---EVADKAAYLTSLNSADLL-KALCYPRVKVGNEYVTKGQTVQ--QVYNSVGALA 431
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLeRMLMTKSVSLQSTSETFEVTLEkgQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 432 KSMYEKMFLWMVTRINQ--------------QLDTKQPRQYFIGVL---DIAGFEIFDFNTLEQLCINFTNEKLQQFFNH 494
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEatkmsalstdgnkhQMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINYLSEKLYAREEQ 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 495 HMFVLEQEEYKKEGIDWEfidfgmdlAACIELIEKPMGIFSILEEECMFPKATDTSF-----KNKLYEQHLGKSNNFQKP 569
Cdd:cd14894 569 VIAVAYSSRPHLTARDSE--------KDVLFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIYDRNSSRLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 570 KPAK--GKAEAH---------FSLVHYAGTVDYNIIGWLDKNKDPL-NETVVGLYQKSGLKTLAFLFSGGQAAEAEGGGG 637
Cdd:cd14894 641 EPPRvlSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLNESSQLGWSPNTNR 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 638 KK--GGKKKGSSFQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPS 715
Cdd:cd14894 721 SMlgSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNSSSS 800
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
837-1433 |
4.56e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.33 E-value: 4.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 837 YFKIKPLLKSAETE---KEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLI 913
Cdd:COG1196 215 YRELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 914 KTKIQLEAKIKELTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENI 993
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 994 AKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDI 1073
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1074 ENDKQQLDEKLKKKEFEMSNLQSKIEDEQALgmQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEIS-- 1151
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEE--LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgv 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1152 -ERLEEAGGATSAQIEMNKKREAEFQ-KMRRDLEEATLQHEATAAALRK----KHADSVAELGEQIDNLQRVKQKLEKEK 1225
Cdd:COG1196 533 eAAYEAALEAALAAALQNIVVEDDEVaAAAIEYLKAAKAGRATFLPLDKirarAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1226 SELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQL 1305
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1306 SRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAmskansevaqwrTKYETDAIQ 1385
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE------------ALEELPEPP 760
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 67189167 1386 RTEELEEAKKKLAQRLQD-------AEEHVEAVNSKCASLEKTKQRLQNEVEDLM 1433
Cdd:COG1196 761 DLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLE 815
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
921-1702 |
6.42e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 107.08 E-value: 6.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 921 AKIKELTERAEDEEEINAELTAKKRKLEDECSELKKdIDDLELTLAKVE-----KEKHATENKVKNLTEEMAGLDENIAK 995
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 996 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKaktkleqqvddlEGSLEQEKKLRmDLERAKRKLEGDLKLAQESTMDIEN 1075
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGE------------EEQLRVKEKIG-ELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1076 DKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLE 1155
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1156 EAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDL 1235
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1236 ASNMETVSKAKGNLEKMCRTLED------------------------QLSEVKTK--------------------EEEQQ 1271
Cdd:TIGR02169 482 EKELSKLQRELAEAEAQARASEErvrggraveevlkasiqgvhgtvaQLGSVGERyataievaagnrlnnvvvedDAVAK 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1272 RLINELSTQKA---------RLHTESGEFSR--------------QLDEKDAMVSQLSRGKQAFTQQIEELKRQ------ 1322
Cdd:TIGR02169 562 EAIELLKRRKAgratflplnKMRDERRDLSIlsedgvigfavdlvEFDPKYEPAFKYVFGDTLVVEDIEAARRLmgkyrm 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1323 ------LEEESKA----KNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKAN---SEVAQWRTKYEtDAIQRTEE 1389
Cdd:TIGR02169 642 vtlegeLFEKSGAmtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRrieNRLDELSQELS-DASRKIGE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1390 LEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEwkQKYEETQA 1469
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1470 ELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLE 1549
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1550 EAEASLEHEEGKILRIQLELnqvkSEIDRKIAEKDEEIDQlKRNHLRVVESMQSTLDAEIRSRNDAlrIKKKMEGDLNEM 1629
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQL----RELERKIEELEAQIEK-KRKRLSELKAKLEALEEELSEIEDP--KGEDEEIPEEEL 951
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67189167 1630 EIQLNHANRQAAEA-IRNLRNTQgMLKDTQlhLDDALRGQDDLKEQLAMVERRAnlmqAEIEELRASLEQTERS 1702
Cdd:TIGR02169 952 SLEDVQAELQRVEEeIRALEPVN-MLAIQE--YEEVLKRLDELKEKRAKLEEER----KAILERIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1139-1752 |
1.27e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.17 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1139 QRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHAdSVAELGEQIDNLQRVK 1218
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA-ELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1219 QKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEK 1298
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1299 DAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTK 1378
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1379 YETDA---IQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVE---------RSNAACAAL 1446
Cdd:COG1196 472 AALLEaalAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEaayeaaleaALAAALQNI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1447 DKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKH 1526
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1527 IHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLD 1606
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1607 AEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEairnlrntqgmlkdtqlhLDDALRGQDDLKEQLAMVERRANLMQ 1686
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEEL------------------LEEEALEELPEPPDLEELERELERLE 773
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 1687 AEIEELRAsleqtersrrV---AEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEA 1752
Cdd:COG1196 774 REIEALGP----------VnllAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLET 832
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1555 |
1.68e-22 |
|
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: 105.91 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 847 AETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKMvalmqekNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIKEL 926
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRL-------EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 927 TERAEDEEEINAELtaKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKE---KKAL 1003
Cdd:TIGR02168 413 EDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaqLQAR 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1004 QEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAkrkLEGDLklaQESTMDIENDKQQLDEK 1083
Cdd:TIGR02168 491 LDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA---LGGRL---QAVVVENLNAAKKAIAF 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1084 LKKKEFEMSNLqskIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSD-LSRELeeISERLEEA----- 1157
Cdd:TIGR02168 565 LKQNELGRVTF---LPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYlLGGVL--VVDDLDNAlelak 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1158 ------------------GGATSAQIEmnkKREAEFQKMRRDLEEATLQHEATAAALRKKHAdSVAELGEQIDNLQRVKQ 1219
Cdd:TIGR02168 640 klrpgyrivtldgdlvrpGGVITGGSA---KTNSSILERRREIEELEEKIEELEEKIAELEK-ALAELRKELEELEEELE 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1220 KLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDekd 1299
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE--- 792
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1300 amvsQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKY 1379
Cdd:TIGR02168 793 ----QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1380 ETdAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKK-QRNFDKVLA 1458
Cdd:TIGR02168 869 EE-LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRiDNLQERLSE 947
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1459 EWKQKYEETQAELEASQKESRSLSTELFKVKNAYEE-------SLDQLETLKRENKNLQQEISDLTEQIAeggkhihELE 1531
Cdd:TIGR02168 948 EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKE-------TLE 1020
|
730 740
....*....|....*....|....*
gi 67189167 1532 KIKKQIDQE-KSELQASLEEAEASL 1555
Cdd:TIGR02168 1021 EAIEEIDREaRERFKDTFDQVNENF 1045
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
982-1867 |
4.82e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 104.38 E-value: 4.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 982 LTEEMAGLDENIAKLTKEKKALQEAHQQtLDDLQAEEDKVNtltkaktkleQQVDDLEGslEQEKKLR-MDLERAKRKLE 1060
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEEN-IERLDLIIDEKR----------QQLERLRR--EREKAERyQALLKEKREYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1061 GDLKLAQESTMD-----IENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERAS-RA 1134
Cdd:TIGR02169 225 GYELLKEKEALErqkeaIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAeIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1135 KAEKQRSDLSRELEEISERL---EEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQI 1211
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLaklEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1212 DNLQRVKQKLEK---EKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTES 1288
Cdd:TIGR02169 385 DELKDYREKLEKlkrEINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1289 GEFSRQLDEKDAMVSQLSRgkqaftqQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYE------------EEQE 1356
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEK-------ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1357 AKAELQRAMSKANSEVaqwrTKYETDAIQRTEELEEAK---------KKLAQRLQDAEE-HVEAVNSKCASLEKTKQRLQ 1426
Cdd:TIGR02169 538 ATAIEVAAGNRLNNVV----VEDDAVAKEAIELLKRRKagratflplNKMRDERRDLSIlSEDGVIGFAVDLVEFDPKYE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1427 NEVEDLMID---VERSNAACAALDK----------------------KQRNFDKVLAEWKQKYEETQAELEASQKESRSL 1481
Cdd:TIGR02169 614 PAFKYVFGDtlvVEDIEAARRLMGKyrmvtlegelfeksgamtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1482 STELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGK 1561
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1562 ILRIQLELNQVKSEIDR-KIAEKDEEIDQLKRNHLRVVESMQSTldaeirsrndalrikkkmEGDLNEMeiqlnHANRQA 1640
Cdd:TIGR02169 774 LHKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRIEARLREI------------------EQKLNRL-----TLEKEY 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1641 AEAIRNlrntqgmlkdtqlhldDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELldaservqll 1720
Cdd:TIGR02169 831 LEKEIQ----------------ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL---------- 884
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1721 htqntslintkKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQtvkdlqhr 1800
Cdd:TIGR02169 885 -----------GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE-------- 945
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67189167 1801 lDEAEQLALKGGKKQIQKLEARVRELE-------NEVENEQKRNIEAVKGLRKHERR---VKELTYQTEEDRKNVLR 1867
Cdd:TIGR02169 946 -IPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEErkaILERIEEYEKKKREVFM 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
858-1600 |
6.55e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.45 E-value: 6.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 858 EDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIKELTERAEDEEEIN 937
Cdd:PTZ00121 1191 EELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 938 AELTAKKRKLED-ECSELKKDIDDLEltlaKVEKEKHATENKVKnlTEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQA 1016
Cdd:PTZ00121 1271 AIKAEEARKADElKKAEEKKKADEAK----KAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1017 EEdkvntltKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQS 1096
Cdd:PTZ00121 1345 AE-------AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1097 KIEDEQALGMQLQKKIKELQARIEELEeeieaerasRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEfq 1176
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEEAK---------KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-- 1486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1177 KMRRDLEEATLQ-HEATAAALRKKHADSVAELGEQidnlqrvKQKLEKEKSELKMEIDDlASNMETVSKAkgnlEKMCRT 1255
Cdd:PTZ00121 1487 EAKKKAEEAKKKaDEAKKAAEAKKKADEAKKAEEA-------KKADEAKKAEEAKKADE-AKKAEEKKKA----DELKKA 1554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1256 LEDQLSEVKTKEEEQQRlinelSTQKARLHTESGEFSRQLDEKdAMVSQLSRGKQAFTQQIEELKRqlEEESKAKNALAH 1335
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKK-----AEEDKNMALRKAEEAKKAEEA-RIEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELK 1626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1336 ALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAiQRTEEL---EEAKKKLAQRLQDAEEH---VE 1409
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaEEDEKKAAEALKKEAEEakkAE 1705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1410 AVNSKCASLEKTKQRLQNEVEDLMIDVERSnaacaaldKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVK 1489
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1490 NAY-EESLDQLETLKR-ENKNLQQEISDLTEQIAEGGKHIHE-LEKIKKQIDQEKSELQAS----LEEAEASLEHEEGKi 1562
Cdd:PTZ00121 1778 EAViEEELDEEDEKRRmEVDKKIKDIFDNFANIIEGGKEGNLvINDSKEMEDSAIKEVADSknmqLEEADAFEKHKFNK- 1856
|
730 740 750
....*....|....*....|....*....|....*...
gi 67189167 1563 lriqlelNQVKSEIDRKIAEKDEEIDQLKRNHLRVVES 1600
Cdd:PTZ00121 1857 -------NNENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
845-1432 |
1.08e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 103.21 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 845 KSAETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEA-------DGLADAEERCDQLIKTKI 917
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNneierleARLERLEDRRERLQQEIE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 918 QL-----EAKIKELTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV---KNLTEEMAGL 989
Cdd:TIGR02168 425 ELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQENLEGF 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 990 DENIAKLTKEKK-------------------------ALQEAHQQTL-DDLQAEEDKVNTLTKAKTKleqQVDDLEGSLE 1043
Cdd:TIGR02168 505 SEGVKALLKNQSglsgilgvlselisvdegyeaaieaALGGRLQAVVvENLNAAKKAIAFLKQNELG---RVTFLPLDSI 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1044 QEKKLRMDLERAKRKLEGDLKLAQE----------------STMDIENDKQQLDEKLKKKEFEMSN------------LQ 1095
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVAKDlvkfdpklrkalsyllGGVLVVDDLDNALELAKKLRPGYRIvtldgdlvrpggVI 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1096 SKIEDEQALGMQ-LQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAE 1174
Cdd:TIGR02168 662 TGGSAKTNSSILeRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL--------------SRQ 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1175 FQKMRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCR 1254
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1255 TLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALA 1334
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1335 HALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSK 1414
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDD 966
|
650
....*....|....*...
gi 67189167 1415 CASLEKTKQRLQNEVEDL 1432
Cdd:TIGR02168 967 EEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1145-1934 |
1.36e-21 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 102.84 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1145 RELEEISERLEEAggatsaQIEMNKKREaEFQKMRRDLEEAtlqhEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKE 1224
Cdd:TIGR02169 177 EELEEVEENIERL------DLIIDEKRQ-QLERLRREREKA----ERYQALLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1225 KSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQ-QRLINELSTQKARLHTESGEFSRQLDEKDAMVS 1303
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1304 QLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRamskansEVAQWRTKYEtDA 1383
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-------ELKDYREKLE-KL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1384 IQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVErsnaacaALDKKQRNFDKVLAEWKQK 1463
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK-------KQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1464 YEETQAELEASQKESRSLSTELfkvknayeeslDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELekiKKQIDQEKSE 1543
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQREL-----------AEAEAQARASEERVRGGRAVEEVLKASIQGVHGT---VAQLGSVGER 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1544 LQASLEEAEAS------LEHEEGKILRIQ------------LELNQVKSE-IDRKIAEKDEEIDQL-------KRNHLRV 1597
Cdd:TIGR02169 537 YATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrrkagratfLPLNKMRDErRDLSILSEDGVIGFAvdlvefdPKYEPAF 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1598 VESMQSTLDAEIRSRNDALRIKKKM---EGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQ 1674
Cdd:TIGR02169 617 KYVFGDTLVVEDIEAARRLMGKYRMvtlEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSE 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1675 LAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVqllhtqntslintkKKLETDISQIQGEMEdivqearN 1754
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL--------------EELEEDLSSLEQEIE-------N 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1755 AEEKAKKAITDAAMMAEELKKEQDTSAHLERMkknmeqtvkDLQHRLDEAEQLALKGgKKQIQKLEARVRELENEVENEQ 1834
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEAR---------LSHSRIPEIQAELSKL-EEEVSRIEARLREIEQKLNRLT 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1835 KRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERA 1914
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
810 820
....*....|....*....|
gi 67189167 1915 DIAESQVNKLRVKSREVHTK 1934
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAK 925
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
916-1544 |
1.41e-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: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 916 KIQLEAKIKELTERAEDEEEINAELTAKKRKLEdecsELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAK 995
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELE----ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 996 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIEN 1075
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1076 DKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLE 1155
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1156 EAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDL 1235
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1236 ASNMETVSKAkgnlekmcRTLEDQLSEVKTKEEEQQRLINELSTQKA------RLHTESGEFSRQLDEKDAMVSQLSRGK 1309
Cdd:COG1196 533 EAAYEAALEA--------ALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflPLDKIRARAALAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1310 QAFTQQIEELKRQLEEESKAKNALAHALQSARHdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEE 1389
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALR----RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1390 LEEAKKKLAQRLQDAEEHVEAvnskcasLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQA 1469
Cdd:COG1196 681 LEELAERLAEEELELEEALLA-------EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1470 ELEASQKESRSLSTELFKVKNAYEE-------SLDQLETLKRENKNLQQEISDLTEQIAeggkhihELEKIKKQIDQEKS 1542
Cdd:COG1196 754 EELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARE-------TLEEAIEEIDRETR 826
|
..
gi 67189167 1543 EL 1544
Cdd:COG1196 827 ER 828
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
844-1519 |
8.99e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 100.60 E-value: 8.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 844 LKSAETEKEMANMK--EDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQA-EADGLADAEERCDQLIKTKIQLE 920
Cdd:PTZ00121 1283 LKKAEEKKKADEAKkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAeEAKKAAEAAKAEAEAAADEAEAA 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 921 AKIKELTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLEltlAKVEKEKHATENKVKnlTEEMAGLDENIAKLTKEK 1000
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK---KKADELKKAAAAKKK--ADEAKKKAEEKKKADEAK 1437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1001 KALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKlrmdLERAKRKLEGDLKLAQESTMDIENDKQQL 1080
Cdd:PTZ00121 1438 KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK----ADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1081 DEKL---KKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSReleeiseRLEEA 1157
Cdd:PTZ00121 1514 EAKKaeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR-------KAEEA 1586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1158 GGATSAQIEMNKKREAEFQKMRRdlEEATLQHEATAAALRKKHADSVAELGEQIDNLQ----RVKQKLEKEKSELKMEID 1233
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKA--EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEaeekKKAEELKKAEEENKIKAA 1664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1234 DLASNMETvSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFT 1313
Cdd:PTZ00121 1665 EEAKKAEE-DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1314 QQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAM-------SKANSEVAQWRTKYETDAIQR 1386
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEvdkkikdIFDNFANIIEGGKEGNLVIND 1823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1387 TEELEEAKKKlaqrlqdaeehvEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNaacaaldkKQRNFDK---VLAEWKQK 1463
Cdd:PTZ00121 1824 SKEMEDSAIK------------EVADSKNMQLEEADAFEKHKFNKNNENGEDGN--------KEADFNKekdLKEDDEEE 1883
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 1464 YEETQAELEASQKE-SRSLSTELFKVKN--AYEESLDQLETLKRENKNLQQEISDLTEQ 1519
Cdd:PTZ00121 1884 IEEADEIEKIDKDDiEREIPNNNMAGKNndIIDDKLDKDEYIKRDAEETREEIIKISKK 1942
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1171-1915 |
5.47e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.82 E-value: 5.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1171 REAEFQKMRRDLEEATLQHEATAAALRKKHADSVAElgeqidnlqrvkqklEKEKSELKMEIDDLASNMETVSKAKG--N 1248
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAE---------------EARKAEEAKKKAEDARKAEEARKAEDarK 1141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1249 LEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARlhteSGEFSRQLDEkdamVSQLSRGKQAFTQQIEELKRQLEEESK 1328
Cdd:PTZ00121 1142 AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK----KAEAARKAEE----VRKAEELRKAEDARKAEAARKAEEERK 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1329 AKNALAHALQSARHDCDLLREQYEEEQEAK-AELQRAmskaNSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEH 1407
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKkAEEERN----NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK 1289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1408 VEAVNSKCASLEKTKQRLQNEVEDLMIDVErsnaacaaLDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELfk 1487
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKADE--------AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA-- 1359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1488 vkNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKilriql 1567
Cdd:PTZ00121 1360 --EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK------ 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1568 elnqvKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNL 1647
Cdd:PTZ00121 1432 -----KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1648 RNTQgmlKDTQLHLDDALRGQDDLKEqlAMVERRAN-LMQAEIEELRASLEQTERSRRVAEQELLDASERVQllHTQNTS 1726
Cdd:PTZ00121 1507 EAKK---KADEAKKAEEAKKADEAKK--AEEAKKADeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE--EDKNMA 1579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1727 LINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAiTDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQH-RLDEAE 1805
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElKKAEEE 1658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1806 QLALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQ 1885
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
730 740 750
....*....|....*....|....*....|...
gi 67189167 1886 AEEAE---EQSNVNLAKFRKIQHELEEAEERAD 1915
Cdd:PTZ00121 1739 AEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1074-1804 |
6.45e-19 |
|
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: 93.55 E-value: 6.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1074 ENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISER 1153
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1154 LEeaggatsAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQRVKQKLEKEKSELKMEID 1233
Cdd:TIGR04523 112 IK-------NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1234 DLASNMETVSKAKGNLEKMcrtledqLSEVKTKEEEQqrliNELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFT 1313
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELL-------LSNLKKKIQKN----KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1314 QQIEELKrqlEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEvaqWRTKYETDAIQRTEELEEA 1393
Cdd:TIGR04523 253 TQLNQLK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD---WNKELKSELKNQEKKLEEI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1394 KKKLAQrlqdAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEA 1473
Cdd:TIGR04523 327 QNQISQ----NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1474 SQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEA 1553
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1554 SLEHEEGKILRIQ---LELNQVKSEIDRKIAEKDEEIDQLKRNhLRVVESMQSTLDAEIRSRNDALrIKKKMEGDLNEME 1630
Cdd:TIGR04523 483 NLEQKQKELKSKEkelKKLNEEKKELEEKVKDLTKKISSLKEK-IEKLESEKKEKESKISDLEDEL-NKDDFELKKENLE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1631 IQLNHANRQaaeaIRNLRNTQGMLKDTQLHLDDALR----GQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVA 1706
Cdd:TIGR04523 561 KEIDEKNKE----IEELKQTQKSLKKKQEEKQELIDqkekEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1707 EQELLDASERVQLLHTQNTSLINTK-------KKLETDISQIQGEMEDIVQEARNAEEKA---KKAITDAAMMAEELKKE 1776
Cdd:TIGR04523 637 KSKKNKLKQEVKQIKETIKEIRNKWpeiikkiKESKTKIDDIIELMKDWLKELSLHYKKYitrMIRIKDLPKLEEKYKEI 716
|
730 740
....*....|....*....|....*...
gi 67189167 1777 QDTSAHLERMKKNMEQTVKDLQHRLDEA 1804
Cdd:TIGR04523 717 EKELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1077-1805 |
8.94e-19 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 93.64 E-value: 8.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1077 KQQLDEKLKKKEFEMSNLQSKIEDEQALGMQ----LQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISE 1152
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKqkfyLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1153 RLEeagGATSAQIEMNKKREAEFQKMRRDLeeatLQHEATAAALRKKHADSVAELGEQI---DNL------------QRV 1217
Cdd:pfam15921 153 ELE---AAKCLKEDMLEDSNTQIEQLRKMM----LSHEGVLQEIRSILVDFEEASGKKIyehDSMstmhfrslgsaiSKI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1218 KQKLEKEKSELKMEIDDLASNMETV-SKAKGNLEKMCRTLEDQLSEVKTKEE---------------EQQRLINELSTQK 1281
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALkSESQNKIELLLQQHQDRIEQLISEHEveitgltekassarsQANSIQSQLEIIQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1282 ARLHTESGEFSRQLDEKDAMVSQ----LSRGKQAFTQQIEELKRQLeeeskaknALAHA-LQSARHDcdllREQYEEE-- 1354
Cdd:pfam15921 306 EQARNQNSMYMRQLSDLESTVSQlrseLREAKRMYEDKIEELEKQL--------VLANSeLTEARTE----RDQFSQEsg 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1355 ------QEAKAELQRAMSKANSEVAQWRTKYETDA-------------------IQRTEELEEAKKKLAQ--------RL 1401
Cdd:pfam15921 374 nlddqlQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitidhlrrelddrnmeVQRLEALLKAMKSECQgqmerqmaAI 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1402 QDAEEHVEAVNSKCASLEKTKQRLQNEVEDLmidversNAACAALDKKQRNFDKVLAEWKQK---YEETQAELEASQKES 1478
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTVSDLTASLQEKeraIEATNAEITKLRSRV 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1479 RSLSTELFKVKNAyEESLDQLET------LKRENKN-----LQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQAS 1547
Cdd:pfam15921 527 DLKLQELQHLKNE-GDHLRNVQTecealkLQMAEKDkvieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1548 LEEAEASLEHEEGKILRIQ-----LELNQVK-----SEIDRKIAEKDEEIDQLkRNHLRVVESMQSTL--DAEIRSRNda 1615
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEarvsdLELEKVKlvnagSERLRAVKDIKQERDQL-LNEVKTSRNELNSLseDYEVLKRN-- 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1616 lrIKKKMEgdlnEMEIQLNHANRQAAEAIRNLRNTQGMLKdtqlhlddALRGQDDLKEQLAMVerranlMQAEIEELRAS 1695
Cdd:pfam15921 683 --FRNKSE----EMETTTNKLKMQLKSAQSELEQTRNTLK--------SMEGSDGHAMKVAMG------MQKQITAKRGQ 742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1696 LEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKakkaitdAAMMAEELKK 1775
Cdd:pfam15921 743 IDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEK-------VANMEVALDK 815
|
810 820 830
....*....|....*....|....*....|..
gi 67189167 1776 EQDTSAHLERMKKNMEQ-TVK-DLQHRLDEAE 1805
Cdd:pfam15921 816 ASLQFAECQDIIQRQEQeSVRlKLQHTLDVKE 847
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
853-1705 |
3.99e-18 |
|
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: 91.57 E-value: 3.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 853 MANMKEDFEKAKEDLA----KSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIKELTE 928
Cdd:pfam02463 147 IAMMKPERRLEIEEEAagsrLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 929 RAEDEEEINAE----LTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQ 1004
Cdd:pfam02463 227 LYLDYLKLNEEridlLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1005 EAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLE--QEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDE 1082
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKelEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1083 KLKKKEFEMSN-LQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGAT 1161
Cdd:pfam02463 387 SSAAKLKEEELeLKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1162 SAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMET 1241
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1242 VS-------------------KAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHteSGEFSRQLDEKDAMV 1302
Cdd:pfam02463 547 TAvivevsatadeveerqklvRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLD--KATLEADEDDKRAKV 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1303 SQLSRGKQAFTQQIEELKRqLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETD 1382
Cdd:pfam02463 625 VEGILKDTELTKLKESAKA-KESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1383 AIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVErsnaacaALDKKQRNFDKVLAEWKQ 1462
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK-------KEEKEEEKSELSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1463 KYEETQAELEASQKESRSLSTEL-FKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEK 1541
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQeEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEEL 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1542 SELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKR--NHLRVVESMQSTLDAEIRSRNDALRIK 1619
Cdd:pfam02463 857 ERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQklNLLEEKENEIEERIKEEAEILLKYEEE 936
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1620 KKMEGDLNEMEIQLNHANRQAAEaIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQT 1699
Cdd:pfam02463 937 PEELLLEEADEKEKEENNKEEEE-ERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEET 1015
|
....*.
gi 67189167 1700 ERSRRV 1705
Cdd:pfam02463 1016 CQRLKE 1021
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1028-1712 |
1.24e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 89.97 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1028 KTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLE--GDLKLAQESTMDIENDKQQLDEklkkkefemsnLQSKIEDEQAlg 1105
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEY-----------LRAALRLWFA-- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1106 mqlQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIE-----MNKKRE------AE 1174
Cdd:COG4913 287 ---QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEreierLERELEererrrAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1175 FQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQ-------RVKQKLEKEKSELKMEIDDLASNMETVSKakg 1247
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaeaeAALRDLRRELRELEAEIASLERRKSNIPA--- 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1248 NLEKMCRTLEDQLS-------------EVKTKEEEQQRLIN-ELSTQKARLHTESGEFSRQLdekdAMVSQLSRGKQAFT 1313
Cdd:COG4913 441 RLLALRDALAEALGldeaelpfvgeliEVRPEEERWRGAIErVLGGFALTLLVPPEHYAAAL----RWVNRLHLRGRLVY 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1314 QQIEELKRQLEEESKAKNALAHALQSARHDC-DLLREQYEEEQ-----EAKAELQRA--------MSKANSEVAQ----- 1374
Cdd:COG4913 517 ERVRTGLPDPERPRLDPDSLAGKLDFKPHPFrAWLEAELGRRFdyvcvDSPEELRRHpraitragQVKGNGTRHEkddrr 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1375 -WRTKYET--DAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQN--EVEDLMIDVERSNAACAALDKK 1449
Cdd:COG4913 597 rIRSRYVLgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1450 QRNFDK---VLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGgkh 1526
Cdd:COG4913 677 LERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE--- 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1527 IHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQV----KSEIDRKIAEKDE---EIDQLKRNHL---- 1595
Cdd:COG4913 754 RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwpaeTADLDADLESLPEylaLLDRLEEDGLpeye 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1596 ------------RVVESMQSTLDAEIRsrndalRIKKKMEgDLNEM----------EIQLNHANRQAAEairnlrntqgm 1653
Cdd:COG4913 834 erfkellnensiEFVADLLSKLRRAIR------EIKERID-PLNDSlkripfgpgrYLRLEARPRPDPE----------- 895
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 1654 LKDTQLHLDDALRGQDDLKEQLAmvERRANLMQAEIEELRASLEQTERSRRvaeQELLD 1712
Cdd:COG4913 896 VREFRQELRAVTSGASLFDEELS--EARFAALKRLIERLRSEEEESDRRWR---ARVLD 949
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
892-1429 |
2.43e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 88.56 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 892 QLQVQAEADGLADAEERCDQLIKTKIQLEAKIKELTER----AEDEEEINAELTAKKRKLEdECSELKKDIDDLELTLAK 967
Cdd:PRK02224 191 QLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQreqaRETRDEADEVLEEHEERRE-ELETLEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 968 VEKEKHATENKVKNLTEEMAGLDENIAKLTKEKkALQEAHQQTLDDLQAEedkvntltkaktkLEQQVDDLEGSLEQEkk 1047
Cdd:PRK02224 270 TEREREELAEEVRDLRERLEELEEERDDLLAEA-GLDDADAEAVEARREE-------------LEDRDEELRDRLEEC-- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1048 lRMDLERAKRKLEGdlklAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELqarieeleeeie 1127
Cdd:PRK02224 334 -RVAAQAHNEEAES----LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL------------ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1128 aerasrakaEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEA-TLQHEATAAALRKK-----HA 1201
Cdd:PRK02224 397 ---------RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAeALLEAGKCPECGQPvegspHV 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1202 DSVAELGEQIDnlqrvkqKLEKEKSELKMEIDDLASNMETVSKAKgNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQK 1281
Cdd:PRK02224 468 ETIEEDRERVE-------ELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERA 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1282 ARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAH------ALQSARHDCDLLREQYEEEQ 1355
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaAIADAEDEIERLREKREALA 619
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67189167 1356 EAKAELQRAMSKANSEVAQWRTKYETDAIqrteelEEAKkklaQRLQDAEEHVEAVNSKCASLEKTKQRLQNEV 1429
Cdd:PRK02224 620 ELNDERRERLAEKRERKRELEAEFDEARI------EEAR----EDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
845-1763 |
3.58e-17 |
|
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: 88.57 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 845 KSAETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKmvalmqekNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIK 924
Cdd:TIGR00606 201 KVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS--------REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 925 ELTERAEDEEEINAELTAKKRKLEDECSELKKDIDdleltlakvekekHATENKVKNLTEEMAGLDENIAKLTKEKKALQ 1004
Cdd:TIGR00606 273 ALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQRELEKLNKERRLLN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1005 EAH-----QQTLDDLQAEEDKVNTLTKAKTKLEQQ----VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIEN 1075
Cdd:TIGR00606 340 QEKtellvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1076 DKQQLDEKLKKKEFEMSNLQSKIEDEQALgmqLQKKIKELQARIEELEeeieaerasraKAEKQRSDLSRELEEISERLE 1155
Cdd:TIGR00606 420 KERLKQEQADEIRDEKKGLGRTIELKKEI---LEKKQEELKFVIKELQ-----------QLEGSSDRILELDQELRKAER 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1156 EAGGA-TSAQIEMNKKREAEFQKMRRDLEEaTLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDD 1234
Cdd:TIGR00606 486 ELSKAeKNSLTETLKKEVKSLQNEKADLDR-KLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTS 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1235 LASNMEtvskakgNLEKMCRTLEDQLSEVKTKEEEQQRLINELstqkARLHTESGEFSRQLDEKDAMVSQLSR------G 1308
Cdd:TIGR00606 565 LLGYFP-------NKKQLEDWLHSKSKEINQTRDRLAKLNKEL----ASLEQNKNHINNELESKEEQLSSYEDklfdvcG 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1309 KQAFTQQIEELKRQLEEESKAKNALAHAlqSARHDcDLLREQYEEEQEAKAELQRAMskansevaqwrtkyetdaiQRTE 1388
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSKQRAMLAGA--TAVYS-QFITQLTDENQSCCPVCQRVF-------------------QTEA 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1389 ELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQ 1468
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1469 AELE---ASQKESRSLSTELFKVKNAYEEsldqletLKRENKNLQQEISDLteQIAEGGKHIHELEKIKKQIDQEKSELQ 1545
Cdd:TIGR00606 772 TLLGtimPEEESAKVCLTDVTIMERFQME-------LKDVERKIAQQAAKL--QGSDLDRTVQQVNQEKQEKQHELDTVV 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1546 ASLEEAEASLEHEEGKILRIQLELNQVKSEiDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGD 1625
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHLKSKTNELKSE-KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKD 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1626 LNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRG-QDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRR 1704
Cdd:TIGR00606 922 QQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMR 1001
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67189167 1705 VAEQELLDASERVQLLHTQNTSLI--NTKKKLETDISQIQGEM-EDIVQEARNAEEKAKKAI 1763
Cdd:TIGR00606 1002 LMRQDIDTQKIQERWLQDNLTLRKreNELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENI 1063
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1137-1629 |
4.01e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 88.17 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1137 EKQRSDLSRELEEISERLEEAG---GATSAQIEMNKKREAEFQKMRRDLEEATlqhEATAAALRKKhadsvAELGEQIDN 1213
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARetrDEADEVLEEHEERREELETLEAEIEDLR---ETIAETERER-----EELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1214 LQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSR 1293
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1294 QLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVA 1373
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1374 QWRTKYE-------------TDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTK------QRLQNEVEDL-- 1432
Cdd:PRK02224 444 EAEALLEagkcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaedriERLEERREDLee 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1433 MID-----VERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEeSLDQLETLKRENK 1507
Cdd:PRK02224 524 LIAerretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERIRTLLAAIA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1508 NLQQEISDLTEQIaeggKHIHELEKIKKQIDQEKSELQASLEEA--EASLEHEEGKILRIQLELNQVKSEIDRKIAEKDE 1585
Cdd:PRK02224 603 DAEDEIERLREKR----EALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLDELREERDD 678
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67189167 1586 ----------EIDQL-----KRNHL--------------RVVESMQSTLDAEIRSRNDAlrikkKMEGDLNEM 1629
Cdd:PRK02224 679 lqaeigavenELEELeelreRREALenrvealealydeaEELESMYGDLRAELRQRNVE-----TLERMLNET 746
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1626-1927 |
9.65e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.91 E-value: 9.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1626 LNEMEIQLNHANRQAAEAIRnLRNTQGMLKDTQLHLddALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRV 1705
Cdd:COG1196 195 LGELERQLEPLERQAEKAER-YRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1706 AEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1785
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1786 MKKNMEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNV 1865
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEA-ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67189167 1866 LRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVK 1927
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
843-1581 |
3.03e-16 |
|
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: 85.41 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 843 LLKSAETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALmqekndlQLQVQAEADglaDAEERCDQLIKTKIQLEAK 922
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELL-------TLRSQLLTL---CTPCMPDTYHERKQVLEKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 923 IKELTERAEDEEEINAELTAK------KRKLEDECSELKKDIDDLELTLAKVEKEKHATE--NKVKNLTEEMAGLDE--- 991
Cdd:TIGR00618 228 LKHLREALQQTQQSHAYLTQKreaqeeQLKKQQLLKQLRARIEELRAQEAVLEETQERINraRKAAPLAAHIKAVTQieq 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 992 ---NIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQe 1068
Cdd:TIGR00618 308 qaqRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQ- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1069 stmDIENDKQQLdEKLKKKEFEMSNLQSKIE-------DEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRS 1141
Cdd:TIGR00618 387 ---QKTTLTQKL-QSLCKELDILQREQATIDtrtsafrDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1142 DLSRELEEISERLEEAGGATSAQIEMNKKREA---EFQKMRRDLEEATLQHEATAAALRKKHADS--VAELGEQIDNLQR 1216
Cdd:TIGR00618 463 ESAQSLKEREQQLQTKEQIHLQETRKKAVVLArllELQEEPCPLCGSCIHPNPARQDIDNPGPLTrrMQRGEQTYAQLET 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1217 VKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLD 1296
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQ 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1297 EKDAMVSqlsrgKQAFTQQIEElKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWR 1376
Cdd:TIGR00618 623 PEQDLQD-----VRLHLQQCSQ-ELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWK 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1377 TKYEtDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDlmidvERSNAACAALDKKQRNFDKV 1456
Cdd:TIGR00618 697 EMLA-QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH-----QARTVLKARTEAHFNNNEEV 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1457 LAEWK--QKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKR-ENKNLQQEISDLTEQIAEGGKHIHELEKI 1533
Cdd:TIGR00618 771 TAALQtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEEKSATLGEITHQ 850
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 67189167 1534 KKQiDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIA 1581
Cdd:TIGR00618 851 LLK-YEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFL 897
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
845-1459 |
3.38e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.12 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 845 KSAETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIK 924
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 925 ELTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEK---- 1000
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGerya 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1001 KALQEAHQQTLDDLQAEEDKVNT----LTKAK----------TKLEQQVDDLEGSLEQ------------EKKLR----- 1049
Cdd:TIGR02169 539 TAIEVAAGNRLNNVVVEDDAVAKeaieLLKRRkagratflplNKMRDERRDLSILSEDgvigfavdlvefDPKYEpafky 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1050 --------MDLERAKR--------KLEGDL--------------KLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIE 1099
Cdd:TIGR02169 619 vfgdtlvvEDIEAARRlmgkyrmvTLEGELfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELR 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1100 DEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAEFQKMR 1179
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV--------------KSELKELE 764
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1180 RDLEEatlqHEATAAALRKKHADSVAELG-EQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLED 1258
Cdd:TIGR02169 765 ARIEE----LEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1259 QLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEeskaknaLAHALQ 1338
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-------LEAQIE 913
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1339 SARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASL 1418
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE--ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDEL 991
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 67189167 1419 EKTKQRLQNEVEDL-----MIDVERSNAACAALDKKQRNFDKVLAE 1459
Cdd:TIGR02169 992 KEKRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
844-1729 |
1.28e-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: 83.30 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 844 LKSAETEKEmanmkedfekakedlakseakRKELEEKMvalmqekNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKI 923
Cdd:pfam01576 419 ARLSESERQ---------------------RAELAEKL-------SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 924 KELTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKAL 1003
Cdd:pfam01576 471 QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1004 QEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLegDLKLAQEstmdiendkqqldek 1083
Cdd:pfam01576 551 QRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKF--DQMLAEE--------------- 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1084 lkkkefemSNLQSKIEDEQalgmqlqkkikelqarieeleeeieaeraSRAKAEkqrsdlSREleeiserleeaggatsa 1163
Cdd:pfam01576 614 --------KAISARYAEER-----------------------------DRAEAE------ARE----------------- 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1164 qiemnkkREAEFQKMRRDLEEAtlqheataaalrkkhadsvaelgeqidnlQRVKQKLEKEKSELKMEIDDLASNMETVS 1243
Cdd:pfam01576 634 -------KETRALSLARALEEA-----------------------------LEAKEELERTNKQLRAEMEDLVSSKDDVG 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1244 KAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLhtesgEFSRQldekdAMVSQLSRGKQAFTQQIEELKRQL 1323
Cdd:pfam01576 678 KNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRL-----EVNMQ-----ALKAQFERDLQARDEQGEEKRRQL 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1324 EEEskaknalahalqsarhdcdlLRE-QYEEEQEAKaelQRAMSKAnsevaqwrtkyetdaiqrteeleeAKKKLAQRLQ 1402
Cdd:pfam01576 748 VKQ--------------------VRElEAELEDERK---QRAQAVA------------------------AKKKLELDLK 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1403 DAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAAcaaldkkqrnfdkvlaewkqkYEETQAELEASQKESRSLS 1482
Cdd:pfam01576 781 ELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARAS---------------------RDEILAQSKESEKKLKNLE 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1483 TELFKVKnayeeslDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKI 1562
Cdd:pfam01576 840 AELLQLQ-------EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1563 LRIQLELNQVKSEI--DRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALriKKKMEGDLNEMEIQLNHANRQA 1640
Cdd:pfam01576 913 RKSTLQVEQLTTELaaERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSS--IAALEAKIAQLEEQLEQESRER 990
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1641 AEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLL 1720
Cdd:pfam01576 991 QAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESM 1070
|
....*....
gi 67189167 1721 HTQNTSLIN 1729
Cdd:pfam01576 1071 NREVSTLKS 1079
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1087-1864 |
1.54e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.27 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1087 KEFEMSNLQSKIEDEQAlgMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIE 1166
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEAT--EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1167 MNKKREAEFQKMR--RDLEEATLQHEA-TAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSElKMEIDDLASNMETVS 1243
Cdd:PTZ00121 1155 EIARKAEDARKAEeaRKAEDAKKAEAArKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1244 KAKGNLEKMCRTLEDQLSEVKTKEEEQQrlINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQL 1323
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEAR--MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1324 EEESKAKNALAHAlQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRteelEEAKKKLAQRLQD 1403
Cdd:PTZ00121 1312 EEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK----EEAKKKADAAKKK 1386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1404 AEEhveavNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAAldKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLST 1483
Cdd:PTZ00121 1387 AEE-----KKKADEAKKKAEEDKKKADELKKAAAAKKKADEA--KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA 1459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1484 ELFKVKNAYEESLDQLETlKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQA----SLEEAEASLEHEE 1559
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKK-KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAkkadEAKKAEEAKKADE 1538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1560 GKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQStldAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQ 1639
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK---AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1640 AAEAIRNlrntqgmlkdtqlhldDALRGQDDLKEQLAMVERRANLMQAEIEELRaslEQTERSRRVAEQELLDASERvql 1719
Cdd:PTZ00121 1616 EEAKIKA----------------EELKKAEEEKKKVEQLKKKEAEEKKKAEELK---KAEEENKIKAAEEAKKAEED--- 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1720 lhtqntslintKKKLEtDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQH 1799
Cdd:PTZ00121 1674 -----------KKKAE-EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 1800 RLDEAEQLAL-KGGKKQIQKLEARVRELENEVENEQKRNIEavKGLRKHERRVKELTYQTEEDRKN 1864
Cdd:PTZ00121 1742 DKKKAEEAKKdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVDKKIKDIFD 1805
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
839-1328 |
5.66e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 80.83 E-value: 5.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 839 KIKPLLKSAETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQ 918
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 919 LEAKIKELTERAEDEEEINAELT---AKKRKLEDECSELKKDIDDLELTLAKVE---------------------KEKHA 974
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISelkKQNNQLKDNIEKKQQEINEKTTEISNTQtqlnqlkdeqnkikkqlsekqKELEQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 975 TENKVKNLTEEMAGLDENIAKLTKEKKalQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLER 1054
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1055 AKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRA 1134
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1135 KAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQheataaalrkkhadsVAELGEQIDNL 1214
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE---------------LKSKEKELKKL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1215 QRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQL---------SEVKTKEEEQQRLINELSTQKARLH 1285
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLK 581
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 67189167 1286 TESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESK 1328
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1041-1938 |
7.82e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 80.86 E-value: 7.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1041 SLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKiEDEQALGMQLQKKIKELQARIE 1120
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY-ENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1121 ELEeeieAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREA-EFQKMRRDLEEATLQHEATAAALRKK 1199
Cdd:TIGR00606 266 KLD----NEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1200 HADSVAELGE-----QIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQ-------LSEVKTKE 1267
Cdd:TIGR00606 342 KTELLVEQGRlqlqaDRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEaktaaqlCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1268 EEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLL 1347
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1348 REQYeeEQEAKAELQRAMSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQDAE-EHVEAVNSKCA------SLEK 1420
Cdd:TIGR00606 502 EVKS--LQNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQIRKIKsRHSDELTSLLGyfpnkkQLED 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1421 TKQRLQNEVEDLMIDVERSNAACAALDKKQ---RNFDKVLAEWKQKYEETQAELEASQKEsrslSTELFKVKNAYEESLD 1497
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELASLEQNKnhiNNELESKEEQLSSYEDKLFDVCGSQDE----ESDLERLKEEIEKSSK 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1498 QLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQV----- 1572
Cdd:TIGR00606 654 QRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglap 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1573 --KSEIDRKIAEKDEEIDQLK---------RNHLRVVESMQSTLDAEIRSRNDALR-----IKKKMEGDLNEMEIQLNHA 1636
Cdd:TIGR00606 734 grQSIIDLKEKEIPELRNKLQkvnrdiqrlKNDIEEQETLLGTIMPEEESAKVCLTdvtimERFQMELKDVERKIAQQAA 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1637 NRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEEL---RASLEQTERSRRVAEQELLDA 1713
Cdd:TIGR00606 814 KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELkseKLQIGTNLQRRQQFEEQLVEL 893
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1714 SERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQearNAEEKAKKAITDAAMMAEELKK--------EQDTSAHLER 1785
Cdd:TIGR00606 894 STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS---SKETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDD 970
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1786 MKKNMEQTVKDLQHRLDEAEQlalkgGKKQIQKlEARVRELENEVENEQKRNIEAVKGLRKHERRVKEL-----TYQTEE 1860
Cdd:TIGR00606 971 YLKQKETELNTVNAQLEECEK-----HQEKINE-DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVeeelkQHLKEM 1044
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1861 DRKNVLRLQDLVDKLQTKVKAYKR-------QAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHT 1933
Cdd:TIGR00606 1045 GQMQVLQMKQEHQKLEENIDLIKRnhvlalgRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYY 1124
|
....*
gi 67189167 1934 KVISE 1938
Cdd:TIGR00606 1125 KTLDQ 1129
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1376-1925 |
8.46e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.49 E-value: 8.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1376 RTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNS-------KCASLEKTKQRLQ---NEVEDLMIDVERSNAACAA 1445
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSelpelreELEKLEKEVKELEelkEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1446 LDKKQRNFDKVLAEWKQKYEETQaELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGK 1525
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1526 HIHELEKIKKqidqEKSELQASLEEAEASLEHEEgKILRIQLELNQVKSEIdrkiaeKDEEIDQLKRnHLRVVESMQSTL 1605
Cdd:PRK03918 336 KEERLEELKK----KLKELEKRLEELEERHELYE-EAKAKKEELERLKKRL------TGLTPEKLEK-ELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1606 DAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRntqgmlkdtqlhlddalrgQDDLKEQLAMVERRANLM 1685
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT-------------------EEHRKELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1686 QAEIEELRASLEQTERSRRVAEQELLDASeRVQLLHTQNTSLINTKKKLEtdiSQIQGEMEDIVQEARNAEEKAKKAITD 1765
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKES-ELIKLKELAEQLKELEEKLK---KYNLEELEKKAEEYEKLKEKLIKLKGE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1766 AAMMAEELKKEQDtsahLERMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEnEVENEQKRNIEAVKGLR 1845
Cdd:PRK03918 541 IKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKELE 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1846 KHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQ--AEEAEEQSNVNLAKFRKI---QHELEEAEERADIAESQ 1920
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELREEYLELSRELaglRAELEELEKRREEIKKT 695
|
....*
gi 67189167 1921 VNKLR 1925
Cdd:PRK03918 696 LEKLK 700
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1212-1911 |
9.41e-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: 80.40 E-value: 9.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1212 DNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLiNELSTQKARLHTESGEF 1291
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1292 SRQLDEkdamvsqlsrgkqaFTQQIEELKRQLEEESKAKNALAHALQSARhdcdlLREQYEEEQEAKAELQRAMSKANSE 1371
Cdd:TIGR00618 266 RARIEE--------------LRAQEAVLEETQERINRARKAAPLAAHIKA-----VTQIEQQAQRIHTELQSKMRSRAKL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1372 VAQWRtkyetdAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTK-------QRLQNEVEDLMIDVERSNAACA 1444
Cdd:TIGR00618 327 LMKRA------AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIScqqhtltQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1445 ALDKKQRNFDKVLAEwKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGG 1524
Cdd:TIGR00618 401 ELDILQREQATIDTR-TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1525 KHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGK-------------ILRIQLELNQVKSEIDRKIAEKDEEIDQLK 1591
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPArqdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQRA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1592 RNHLRVVESMQSTLDAEI---RSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQ 1668
Cdd:TIGR00618 560 SLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1669 DDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDI 1748
Cdd:TIGR00618 640 ELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1749 VQEARNAEEKAKKAITD----AAMMAEELKKEQDTS-AHLERMKKNMEQTVKDLQHRLDEAEQLAlKGGKKQIQKLEARV 1823
Cdd:TIGR00618 720 FNEIENASSSLGSDLAAredaLNQSLKELMHQARTVlKARTEAHFNNNEEVTAALQTGAELSHLA-AEIQFFNRLREEDT 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1824 REL-ENEVENEQKrnieavkglRKHERRVKELT-YQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFR 1901
Cdd:TIGR00618 799 HLLkTLEAEIGQE---------IPSDEDILNLQcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
730
....*....|
gi 67189167 1902 KIQHELEEAE 1911
Cdd:TIGR00618 870 KIIQLSDKLN 879
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
920-1789 |
1.05e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 80.40 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 920 EAKIKELTERAEDEEEINAEL-TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHatenkvknlteemagLDENIAKLTK 998
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL---------------NEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 999 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQ 1078
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1079 QLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEag 1158
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE-- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1159 gatsaqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsvaELGEQIDNLQRvkqKLEKEKSELKMEIDDLASN 1238
Cdd:pfam02463 403 ----------EEKEAQLLLELARQLEDLLKEEKKEELEILE------EEEESIELKQG---KLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1239 METVSKAKGNLEkmcrtledqlSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEE 1318
Cdd:pfam02463 464 ELELKKSEDLLK----------ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1319 LKRQLEEESKAKNALAHALQSARHD-CDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKL 1397
Cdd:pfam02463 534 LGVAVENYKVAISTAVIVEVSATADeVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATL 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1398 AQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDV--ERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQ 1475
Cdd:pfam02463 614 EADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVslEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1476 KESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASL 1555
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1556 EHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNH--LRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQL 1633
Cdd:pfam02463 774 KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEeaELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1634 NHANRQAAEairNLRNTQGMLKDTQLHLDDALRgQDDLKEQLAMVERRANlmQAEIEELRASLEQTERSRRVAEQELLDA 1713
Cdd:pfam02463 854 EELERLEEE---ITKEELLQELLLKEEELEEQK-LKDELESKEEKEKEEK--KELEEESQKLNLLEEKENEIEERIKEEA 927
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 1714 SERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKN 1789
Cdd:pfam02463 928 EILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
844-1379 |
1.53e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.70 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 844 LKSAETEKEMAnmKEDFEKAKEDLAKSEAKRKELEEkmvaLMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKI 923
Cdd:PRK02224 222 IERYEEQREQA--RETRDEADEVLEEHEERREELET----LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEER 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 924 KELTERAEDEEeinaeltAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKAL 1003
Cdd:PRK02224 296 DDLLAEAGLDD-------ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAEL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1004 QEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEgsleqekklrMDLERAKRKLEgdlklaqestmDIENDKQQLDEK 1083
Cdd:PRK02224 369 ESELEEAREAVEDRREEIEELEEEIEELRERFGDAP----------VDLGNAEDFLE-----------ELREERDELRER 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1084 LKKKEFEMSNLQSKIEDEQALgmQLQKKIKEL--QARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGAT 1161
Cdd:PRK02224 428 EAELEATLRTARERVEEAEAL--LEAGKCPECgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1162 SAQIEMNKKREAefqkmRRDLEEATLQHEATAAALRKKHA---DSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASN 1238
Cdd:PRK02224 506 EAEDRIERLEER-----REDLEELIAERRETIEEKRERAEelrERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1239 METVSKAKGNLEKmcrtLEDQLSEVKTKEEEQQRL------INELSTQKARLHTESGEFSRQLDEK--DAMVSQLSRGKQ 1310
Cdd:PRK02224 581 LAELKERIESLER----IRTLLAAIADAEDEIERLrekreaLAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKE 656
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 1311 AFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREqYEEEQEAKAELQRAMSKANSEVAQWRTKY 1379
Cdd:PRK02224 657 RAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE-LRERREALENRVEALEALYDEAEELESMY 724
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1259-1925 |
1.94e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 79.45 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1259 QLSEVKTKEEEQQRL----------INELSTQKARLHTESGEFSRQLD-------EKDAMVSQLSRGKQAFTQQIEELKR 1321
Cdd:pfam01576 3 QEEEMQAKEEELQKVkerqqkaeseLKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1322 QLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTeELEEAKKKLAQRL 1401
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNS-KLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1402 QDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSL 1481
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1482 STELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGK 1561
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1562 ILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAA 1641
Cdd:pfam01576 322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1642 EAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMverranlMQAEIEELRASLEQTER-----SRRVA--EQELLDAS 1714
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK-------LQSELESVSSLLNEAEGkniklSKDVSslESQLQDTQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1715 ERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTV 1794
Cdd:pfam01576 475 ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1795 KDLQHRLDEAEQLALKggkkqIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELtyqTEEDRKNVLRLQDLVDK 1874
Cdd:pfam01576 555 EALTQQLEEKAAAYDK-----LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQM---LAEEKAISARYAEERDR 626
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 67189167 1875 lqtkvkaykrqaeeAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLR 1925
Cdd:pfam01576 627 --------------AEAEAREKETRALSLARALEEALEAKEELERTNKQLR 663
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
858-1538 |
2.68e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.95 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 858 EDFEKAKEDLAKSeakRKELEEKMVALmqekndlqlqvqaeaDGLADAEERCDQLIKTKIQ-LEAKIKELTERAEDEEEI 936
Cdd:PRK03918 158 DDYENAYKNLGEV---IKEIKRRIERL---------------EKFIKRTENIEELIKEKEKeLEEVLREINEISSELPEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 937 NAELtAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQA 1016
Cdd:PRK03918 220 REEL-EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1017 EEDKVNTLtKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIE--NDKQQLDEKLKKKEFEMSNL 1094
Cdd:PRK03918 299 SEFYEEYL-DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1095 QSKIEDEqalgmQLQKKIKELQarieeleeeieaerasraKAEKQRSDLSRELEEISER---LEEAGGATSAQIEMNKKR 1171
Cdd:PRK03918 378 KKRLTGL-----TPEKLEKELE------------------ELEKAKEEIEEEISKITARigeLKKEIKELKKAIEELKKA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1172 EAEFQKMRRDLEEatlQHEATaaaLRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIddlaSNMETVSKAKGNLEK 1251
Cdd:PRK03918 435 KGKCPVCGRELTE---EHRKE---LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL----KKESELIKLKELAEQ 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1252 McRTLEDQLSEVKTKEEEQQRliNELSTQKARLHTESGEfsrqldekdamvsqlsrgkqaftqqIEELKRQLEEESKAKN 1331
Cdd:PRK03918 505 L-KELEEKLKKYNLEELEKKA--EEYEKLKEKLIKLKGE-------------------------IKSLKKELEKLEELKK 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1332 ALAhalqsarhdcdLLREQYEEEQEAKAELQRAMSKANSEVaqwrtkyETDAIQRTEELEEAKKklaqrlqdaeEHVEAV 1411
Cdd:PRK03918 557 KLA-----------ELEKKLDELEEELAELLKELEELGFES-------VEELEERLKELEPFYN----------EYLELK 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1412 NSkcaslEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYeetqaeleaSQKESRSLSTELFKVKNA 1491
Cdd:PRK03918 609 DA-----EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY---------SEEEYEELREEYLELSRE 674
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 67189167 1492 YEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQID 1538
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
908-1590 |
4.28e-14 |
|
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: 78.09 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 908 RCDQLIKTKIQLEAKIKELTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAT----ENKVKNLT 983
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERkqvlEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 984 EEMAGLDENIAKLTKEKKALQEAH--QQTLDDLQAEEDKVNTLTKAKTKLEQqvddlegsleqekklRMDLERAKRKLEG 1061
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAVLEETQE---------------RINRARKAAPLAA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1062 DLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQlQKKIKELQARIEELEEEIEAERASRAKAEKQRS 1141
Cdd:TIGR00618 298 HIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-RRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1142 DLS--RELEEISERLEEAGGATSAQIE-----------------------MNKKREAEFQKMRRDLEEATLQHEATAAAL 1196
Cdd:TIGR00618 377 LTQhiHTLQQQKTTLTQKLQSLCKELDilqreqatidtrtsafrdlqgqlAHAKKQQELQQRYAELCAAAITCTAQCEKL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1197 RKKHADSVAE-LGEQIDNLQRVKQKLEKEK-------------SELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSE 1262
Cdd:TIGR00618 457 EKIHLQESAQsLKEREQQLQTKEQIHLQETrkkavvlarllelQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQT 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1263 VKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQA---FTQQIEELKRQLEEESKAKNALAhalqs 1339
Cdd:TIGR00618 537 YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDipnLQNITVRLQDLTEKLSEAEDMLA----- 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1340 arhdcDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLE 1419
Cdd:TIGR00618 612 -----CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1420 KTKQRLQNEVEDLmidvERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEA-------SQKESRSLSTELFKVK-NA 1491
Cdd:TIGR00618 687 SEKEQLTYWKEML----AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAredalnqSLKELMHQARTVLKARtEA 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1492 YEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQ 1571
Cdd:TIGR00618 763 HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSA 842
|
730
....*....|....*....
gi 67189167 1572 VKSEIDRKIAEKDEEIDQL 1590
Cdd:TIGR00618 843 TLGEITHQLLKYEECSKQL 861
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1073-1939 |
1.55e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 76.55 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1073 IENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEeieaeRASRAKAEKQRSDLSRELEEISE 1152
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEEL-----KLQELKLKEQAKKALEYYQLKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1153 RLEEAGGATSAQIEmnkKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEI 1232
Cdd:pfam02463 219 LELEEEYLLYLDYL---KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1233 ddlasnmETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAF 1312
Cdd:pfam02463 296 -------EELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1313 TQQIEELKRQLEEESKAKNA--------LAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAI 1384
Cdd:pfam02463 369 EQLEEELLAKKKLESERLSSaaklkeeeLELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1385 QRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTkqrlQNEVEDLMIDVERSNAACAALDKKQRNF----DKVLAEW 1460
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ----LELLLSRQKLEERSQKESKARSGLKVLLalikDGVGGRI 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1461 KQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKR-ENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQ 1539
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRaLTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1540 EKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIK 1619
Cdd:pfam02463 605 LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1620 KKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQT 1699
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1700 ERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKA----ITDAAMMAEELKK 1775
Cdd:pfam02463 765 EKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEekikEEELEELALELKE 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1776 EQDTSAHLE---RMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVK 1852
Cdd:pfam02463 845 EQKLEKLAEeelERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIK 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1853 ELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVH 1932
Cdd:pfam02463 925 EEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEK 1004
|
....*..
gi 67189167 1933 TKVISEE 1939
Cdd:pfam02463 1005 KKLIRAI 1011
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
835-1389 |
1.64e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.26 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 835 KLYFKIKPLLKSAETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQ----------VQAEADGLAD 904
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRlsrleeeingIEERIKELEE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 905 AEERCDQLIKTKIQLEAKIKELTERAEDEEEINAeLTAKKRKLEDECSELkkDIDDLELTLAKVEKEKHATENKVKNLTE 984
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYEEAKA-KKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 985 EMAGLDENIAKLTKEKKALQEAHQQ--TLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGD 1062
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1063 LKLAQESTM--DIENDKQQLD----EKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQarieeleeeieAERASRAKA 1136
Cdd:PRK03918 493 SELIKLKELaeQLKELEEKLKkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE-----------ELKKKLAEL 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1137 EKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATlqheataaalrkkhadsvaelgeqiDNLQR 1216
Cdd:PRK03918 562 EKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAE-------------------------KELER 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1217 VKQKLEKEKSELKMEIDDLAsnmetvsKAKGNLEKMCRTLEDQlsEVKTKEEEQQRLINELStqkarlhtesgEFSRQLD 1296
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELA-------ETEKRLEELRKELEEL--EKKYSEEEYEELREEYL-----------ELSRELA 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1297 EKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALaHALQSARHDCDLLREQY-----EEEQEAKAELQRAMSKANSE 1371
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL-EKLEKALERVEELREKVkkykaLLKERALSKVGEIASEIFEE 755
|
570
....*....|....*...
gi 67189167 1372 VAQwrTKYETDAIQRTEE 1389
Cdd:PRK03918 756 LTE--GKYSGVRVKAEEN 771
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
871-1450 |
1.67e-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: 76.31 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 871 EAKRKELEEKMVALMQEKNDLQLQV----QAEADGLAD-AEERCDQLIKTKIQLE-----------AKIKELTERAEDEE 934
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQDRIEQLisehEVEITGLTEkASSARSQANSIQSQLEiiqeqarnqnsMYMRQLSDLESTVS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 935 EINAELTAKKRKLEDECSELKKD--IDDLELTLAKVEKEKHATENkvKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLD 1012
Cdd:pfam15921 328 QLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKLLADLHKREKELSLEKEQNKRLWD 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1013 dlqaeEDKVNTLTkaktkleqqVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLkkkefemS 1092
Cdd:pfam15921 406 -----RDTGNSIT---------IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKV-------S 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1093 NLQSKIEDEQALgmqLQKKIKELqarieeleeeiEAERASRAKAEKQRSDLSRELEEISERLEeaggATSAQIEMNKKRE 1172
Cdd:pfam15921 465 SLTAQLESTKEM---LRKVVEEL-----------TAKKMTLESSERTVSDLTASLQEKERAIE----ATNAEITKLRSRV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1173 ----AEFQKMRRDLEE-ATLQHEATAAALRKKHADSVAE-LGEQIDNLQ-------RVKQKLEKEKSELKMEIDDLASNM 1239
Cdd:pfam15921 527 dlklQELQHLKNEGDHlRNVQTECEALKLQMAEKDKVIEiLRQQIENMTqlvgqhgRTAGAMQVEKAQLEKEINDRRLEL 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1240 ETVSKAKGNLEKMCRTLEDQLSEVktkEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSrgkqAFTQQIEEL 1319
Cdd:pfam15921 607 QEFKILKDKKDAKIRELEARVSDL---ELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELN----SLSEDYEVL 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1320 KRQL----EEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAE-------LQRAMSKANSEVAQWRTKYE------TD 1382
Cdd:pfam15921 680 KRNFrnksEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQITAKRGQIDALQSKIQfleeamTN 759
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 67189167 1383 AIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSN---AACAALDKKQ 1450
Cdd:pfam15921 760 ANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASlqfAECQDIIQRQ 830
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
33-77 |
1.80e-13 |
|
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: 66.30 E-value: 1.80e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 67189167 33 DAKSSVFVVDAKESYVKATVQSREGGKVTAKTEGGATVTVKDDQV 77
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1212-1889 |
1.84e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.87 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1212 DNLQRVKQKLEKEKSELKMEIddlasnmetvsKAKGNLEKMCRTLEDQLSEVKtkeeeqqRLINELSTQKarlhtesgef 1291
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFI-----------KRTENIEELIKEKEKELEEVL-------REINEISSEL---------- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1292 sRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKAN-- 1369
Cdd:PRK03918 217 -PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEey 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1370 SEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMidversnaacaaldkk 1449
Cdd:PRK03918 296 IKLSEFYEEYL----DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE---------------- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1450 qrnfdkVLAEWKQKYEETQAELEASQK-ESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIH 1528
Cdd:PRK03918 356 ------ELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1529 ELEKIKKQIDQEKSELqasleeaeaSLEHEEGKILRIQLELNQVKSEIdRKIAEKDEEIdqlkRNHLRVVESmqstldae 1608
Cdd:PRK03918 430 ELKKAKGKCPVCGREL---------TEEHRKELLEEYTAELKRIEKEL-KEIEEKERKL----RKELRELEK-------- 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1609 IRSRNDALRIKKKMEGDLNEMEIQLNHAN----RQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANl 1684
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKYNleelEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD- 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1685 mqaEIEELRASLEQTERSRRVAEQELLDasERVQLLHTQNTSLIntkkkletdisqiqgEMEDIVQEARNAEEKAKKAIT 1764
Cdd:PRK03918 567 ---ELEEELAELLKELEELGFESVEELE--ERLKELEPFYNEYL---------------ELKDAEKELEREEKELKKLEE 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1765 DAAMMAEELkkeQDTSAHLERMKKNMEQtvkdLQHRLDEAEQlalkggkkqiQKLEARVRELENEVENEQKRNIEAVKGL 1844
Cdd:PRK03918 627 ELDKAFEEL---AETEKRLEELRKELEE----LEKKYSEEEY----------EELREEYLELSRELAGLRAELEELEKRR 689
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 67189167 1845 RKHERRVKELTYQTEEDRKNVLRLQDL------VDKLQTKVKAYKRQAEEA 1889
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKKELEKLekalerVEELREKVKKYKALLKER 740
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1574-1892 |
2.85e-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: 75.49 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1574 SEIDRKIAEKDEEIDQLKRNHLR---VVESMQSTLDAEIRSRNDALR------IKKKMEG-----DLNEMEIQLNHANRQ 1639
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERyqallkEKREYEGyellkEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1640 AAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQL-AMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQ 1718
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1719 LLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSA----HLERMKKNMEQTV 1794
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyreKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1795 KDLQHRLDEAEQLALKGG--KKQIQKLEARVRELENEVENEQKRnieavkgLRKHERRVKELTYQTEEDRKNVLRLQDLV 1872
Cdd:TIGR02169 406 RELDRLQEELQRLSEELAdlNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340
....*....|....*....|
gi 67189167 1873 DKLQTKVKAYKRQAEEAEEQ 1892
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQ 498
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
914-1630 |
2.91e-13 |
|
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: 75.14 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 914 KTKIQLEAKIKELTERAEDEEEINAELTAkkRKLEDECSELKKDIddleltlakveKEKHATENKVKNLTEEMAGLDENI 993
Cdd:pfam05483 105 ENKLQENRKIIEAQRKAIQELQFENEKVS--LKLEEEIQENKDLI-----------KENNATRHLCNLLKETCARSAEKT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 994 AKLTKEKkalqEAHQQTLDDLQaeedkvNTLTKAKTKLEQ-QVDDLEGSLEQEKKLRMDLERAKRklegdlkLAQESTMD 1072
Cdd:pfam05483 172 KKYEYER----EETRQVYMDLN------NNIEKMILAFEElRVQAENARLEMHFKLKEDHEKIQH-------LEEEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1073 IENDKQQLDEKL---KKKEFEMSNLQSKIEDEQALGMQLQKKIKelqarieeleeeieAERASRAKAEKQRSDLSRELEE 1149
Cdd:pfam05483 235 INDKEKQVSLLLiqiTEKENKMKDLTFLLEESRDKANQLEEKTK--------------LQDENLKELIEKKDHLTKELED 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1150 ISERLEEaggATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAAlRKKHADSVAELGEQIDNLQRV----KQKLEKEK 1225
Cdd:pfam05483 301 IKMSLQR---SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA-KAAHSFVVTEFEATTCSLEELlrteQQRLEKNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1226 SELK---MEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKT---KEEEQQRLINELSTQKARLHTESGEFSRQLDEKD 1299
Cdd:pfam05483 377 DQLKiitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLE 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1300 AMVSQLSRGKQAFTQQIEELKRQLEEEsKAKNALAHAlqsarhDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRtKY 1379
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKE-KLKNIELTA------HCDKLLLENKELTQEASDMTLELKKHQEDIINCK-KQ 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1380 ETDAIQRTEELEEAKKKLAQRLQDAEEHV----EAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDK 1455
Cdd:pfam05483 529 EERMLKQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNK 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1456 VLAEWKQkyeETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDltEQIAEgGKHIHELEKIKK 1535
Cdd:pfam05483 609 NIEELHQ---ENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIED--KKISE-EKLLEEVEKAKA 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1536 QIDqEKSELQaslEEAEASLEHeegKILRIQLELNQVKSEIDRKIAEKDEEIDqLKRNHLRVVESMQSTLDAEIRS-RND 1614
Cdd:pfam05483 683 IAD-EAVKLQ---KEIDKRCQH---KIAEMVALMEKHKHQYDKIIEERDSELG-LYKNKEQEQSSAKAALEIELSNiKAE 754
|
730
....*....|....*.
gi 67189167 1615 ALRIKKKMEGDLNEME 1630
Cdd:pfam05483 755 LLSLKKQLEIEKEEKE 770
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
895-1521 |
3.27e-13 |
|
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: 75.26 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 895 VQAEADGLADAEERCDQLIKTKIQLEAKIKELTERAEDEEEINAELTAKKRkledecSELKKDIDDLELTLAKVEKEKHA 974
Cdd:pfam12128 239 IRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 975 TENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQAE-----------EDKVNTLTKAKTKL-----EQQVDDL 1038
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSElenleerlkalTGKHQDVTAKYNRRrskikEQNNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1039 EGSLEQEKKLRMDLERAKRKLEGDLKlAQESTMDIENDKQQLDEKLKKKEFE--MSNLQSKIEDEQA---LGMQLQKKIK 1113
Cdd:pfam12128 393 AGIKDKLAKIREARDRQLAVAEDDLQ-ALESELREQLEAGKLEFNEEEYRLKsrLGELKLRLNQATAtpeLLLQLENFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1114 EL---QARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRR----DLEEAT 1186
Cdd:pfam12128 472 RIeraREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRkeapDWEQSI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1187 LQHEATAAALRKK-HADSVAELGEQIDNL-------------------QRVKQKLEKEKSELKMEIDDLASNMETVSKAK 1246
Cdd:pfam12128 552 GKVISPELLHRTDlDPEVWDGSVGGELNLygvkldlkridvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQAN 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1247 GNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEK----DAMVSQLSRGKQAFTQQIeelKRQ 1322
Cdd:pfam12128 632 GELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERlnslEAQLKQLDKKHQAWLEEQ---KEQ 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1323 LEEESKAKNALAHALQSARHDcdllreqyeEEQEAKAELQRAMSKANSEVAQWRTKYETDAI------QRTEELEEAKKK 1396
Cdd:pfam12128 709 KREARTEKQAYWQVVEGALDA---------QLALLKAAIAARRSGAKAELKALETWYKRDLAslgvdpDVIAKLKREIRT 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1397 LAQRLQDAEEHVEAVNSKCASLEKT----KQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELE 1472
Cdd:pfam12128 780 LERKIERIAVRRQEVLRYFDWYQETwlqrRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLS 859
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67189167 1473 ASQKESRSLSTELFKVKNAYE---------ESLDQLETLKRENKNL----QQEISDLTEQIA 1521
Cdd:pfam12128 860 ENLRGLRCEMSKLATLKEDANseqaqgsigERLAQLEDLKLKRDYLsesvKKYVEHFKNVIA 921
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1388-1922 |
5.96e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.57 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1388 EELEEAKKKLAQrLQDAEEHveavnskCASLEKTKQRLQ-NEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEE 1466
Cdd:COG4913 242 EALEDAREQIEL-LEPIREL-------AERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1467 TQAELEASQKESRSLstelfkvKNAYEES-LDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKikkQIDQEKSELQ 1545
Cdd:COG4913 314 LEARLDALREELDEL-------EAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGL---PLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1546 ASLEEAEASLEHEEGKILRIQLELNQVKSEI---DRKIAEKDEEIDQLKRNHLRVVESMQSTLDA---EIRSRNDALRIK 1619
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALrdlRRELRELEAEIASLERRKSNIPARLLALRDAlaeALGLDEAELPFV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1620 kkmeGDLneMEIQLNHAN-RQAAE-AIRNLRNTqgMLKDTQlHLDDALRGQDDLKeqlamverranlmqaeieeLRASLe 1697
Cdd:COG4913 464 ----GEL--IEVRPEEERwRGAIErVLGGFALT--LLVPPE-HYAAALRWVNRLH-------------------LRGRL- 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1698 QTERSRRVAEQELLDASERVQLLHtqntslintkkKLETDISQIQGEMEDIVQE------ARNAEE--KAKKAITDAAMM 1769
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLEAELGRrfdyvcVDSPEElrRHPRAITRAGQV 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1770 AeelkkeQDTSAHlermkknmeqtVKDLQHRLDE--------AEQLALKggKKQIQKLEARVRELENEVE---------N 1832
Cdd:COG4913 584 K------GNGTRH-----------EKDDRRRIRSryvlgfdnRAKLAAL--EAELAELEEELAEAEERLEaleaeldalQ 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1833 EQKRNIEAVKGLRKHERRVKELTY---QTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEE 1909
Cdd:COG4913 645 ERREALQRLAEYSWDEIDVASAEReiaELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
570
....*....|...
gi 67189167 1910 AEERADIAESQVN 1922
Cdd:COG4913 725 AEEELDELQDRLE 737
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1418-1930 |
1.28e-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: 73.61 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1418 LEKTKQRLQNEVEDLMIDVERSNAacaaLDKKQRNF-DKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESL 1496
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNE----LHEKQKFYlRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1497 DQLETLKRENKNLQQEISDLTEQIaeggkhiHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLElnQVKSEI 1576
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSNTQIEQL-------RKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFR--SLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1577 DRKIAEKDEEIDQLKrNHLRVVESMQSTLDAEIRSRNDAL--RIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGML 1654
Cdd:pfam15921 223 SKILRELDTEISYLK-GRIFPVEDQLEALKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1655 KDTQlhlddalrgqDDLKEQLAMVERRANLMQAEIEELRASLEQterSRRVAEQELLDASERVQLLHTQntslintkkkl 1734
Cdd:pfam15921 302 EIIQ----------EQARNQNSMYMRQLSDLESTVSQLRSELRE---AKRMYEDKIEELEKQLVLANSE----------- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1735 etdISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQlalkggkk 1814
Cdd:pfam15921 358 ---LTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM-------- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1815 QIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDrKNVLR-------------------LQDLVDKL 1875
Cdd:pfam15921 427 EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEST-KEMLRkvveeltakkmtlessertVSDLTASL 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 1876 QTKVKAYK-RQAEEAEEQSNVNLaKFRKIQHeLEEAEERADIAESQVNKLRVKSRE 1930
Cdd:pfam15921 506 QEKERAIEaTNAEITKLRSRVDL-KLQELQH-LKNEGDHLRNVQTECEALKLQMAE 559
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
856-1633 |
2.22e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 72.77 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 856 MKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIKELTERAEDEEE 935
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRK 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 936 INAELTAKKRKLEDECseLKKDIDDLELTLAKVEKEKHAtenkvknlteemagLDENIAKLTKEKKALQEAHQQTLDDLQ 1015
Cdd:TIGR00606 483 AERELSKAEKNSLTET--LKKEVKSLQNEKADLDRKLRK--------------LDQEMEQLNHHTTTRTQMEMLTKDKMD 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1016 AEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRmDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQ 1095
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLH-SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYE 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1096 SKIED---EQALGMQLQKKIKELQarieeleeeieaerasraKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNK--- 1169
Cdd:TIGR00606 626 DKLFDvcgSQDEESDLERLKEEIE------------------KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQrvf 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1170 KREAEFQKMRRDLEEATL----QHEATAAALRKKHADSVAELG-------------EQIDNLQRVKQKLEKEKSELKMEI 1232
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGlapgrqsiidlkeKEIPELRNKLQKVNRDIQRLKNDI 767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1233 DDLASNMETVSkAKGNLEKMCRT-------LEDQLSEVKTKEEEQQRLIN--ELSTQKARLHTESGEFSRQLDEKDAMVS 1303
Cdd:TIGR00606 768 EEQETLLGTIM-PEEESAKVCLTdvtimerFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIE 846
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1304 QLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDa 1383
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ----FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKD- 921
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1384 IQRTEEL----EEAKKKLAQRLQDAEEHVEAVNSKCASLEKtkqRLQNEVEDLMIDVERS----NAACAALDKKQRNFDK 1455
Cdd:TIGR00606 922 QQEKEELisskETSNKKAQDKVNDIKEKVKNIHGYMKDIEN---KIQDGKDDYLKQKETElntvNAQLEECEKHQEKINE 998
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1456 VLAEWKQKYEeTQAELEASQKESRSLSTELFKVKNAYEE--------SLDQLETLKRENKNLQQEISDLTEQIAEGGKHI 1527
Cdd:TIGR00606 999 DMRLMRQDID-TQKIQERWLQDNLTLRKRENELKEVEEElkqhlkemGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQ 1077
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1528 HELEKIKKQIDQEKSELQ-----ASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQ 1602
Cdd:TIGR00606 1078 KGYEKEIKHFKKELREPQfrdaeEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDLWRSTYRGQ 1157
|
810 820 830
....*....|....*....|....*....|.
gi 67189167 1603 STLDAEIRSRNDALRIKKKMEGDLNEMEIQL 1633
Cdd:TIGR00606 1158 DIEYIEIRSDADENVSASDKRRNYNYRVVML 1188
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
861-1718 |
2.34e-12 |
|
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: 72.56 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 861 EKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLiktkiqleAKIKELTERAED-EEEINAE 939
Cdd:pfam12128 182 DKIAKAMHSKEGKFRDVKSMIVAILEDDGVVPPKSRLNRQQVEHWIRDIQAI--------AGIMKIRPEFTKlQQEFNTL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 940 LTAkkrklEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEM-AGLDENIAKLTKEKKALQEAHQQTLDDLQAEE 1018
Cdd:pfam12128 254 ESA-----ELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLdDQWKEKRDELNGELSAADAAVAKDRSELEALE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1019 DKvntltkAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKI 1098
Cdd:pfam12128 329 DQ------HGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1099 EDEQALGMQLQKKIKELQARIEeleeeieaerasRAKAEKQRSDLSRELEEISERLEEAGG------ATSAQIEMNKKRE 1172
Cdd:pfam12128 403 REARDRQLAVAEDDLQALESEL------------REQLEAGKLEFNEEEYRLKSRLGELKLrlnqatATPELLLQLENFD 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1173 AEFQKMRRDLEEATLQHEATAAALRKkhADSVAElgEQIDNLQRVKQKLEKEKSELkmeiddlASNMETVSKAKGNLEKM 1252
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQ--ARKRRD--QASEALRQASRRLEERQSAL-------DELELQLFPQAGTLLHF 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1253 CRTledqlsEVKTKEEEQQRLINELSTQKARLHTESGEFSrqldekdamvsqlSRGKQAFTQQIEELKRQLEEESKAKNa 1332
Cdd:pfam12128 540 LRK------EAPDWEQSIGKVISPELLHRTDLDPEVWDGS-------------VGGELNLYGVKLDLKRIDVPEWAASE- 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1333 lahalQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVaqwrtkyetDAIQRTEELEeakkklAQRLQDAEEhveavn 1412
Cdd:pfam12128 600 -----EELRERLDKAEEALQSAREKQAAAEEQLVQANGEL---------EKASREETFA------RTALKNARL------ 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1413 skcaslekTKQRLQNEVEDLMIDVERSNAAcaALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAY 1492
Cdd:pfam12128 654 --------DLRRLFDEKQSEKDKKNKALAE--RKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVV 723
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1493 EESLDQLETLkrenknLQQEISDLTEQIaeggkhihelekiKKQIDQEKSELQASLeeaeASLEHEEGKILRIQLELNQV 1572
Cdd:pfam12128 724 EGALDAQLAL------LKAAIAARRSGA-------------KAELKALETWYKRDL----ASLGVDPDVIAKLKREIRTL 780
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1573 KSEIDRkIAEKDEEIDQLKRnhlrvveSMQSTLDaeirSRNDALRIKK-KMEGDLNEMEIQLNHANRQAAEAIRNLRNTQ 1651
Cdd:pfam12128 781 ERKIER-IAVRRQEVLRYFD-------WYQETWL----QRRPRLATQLsNIERAISELQQQLARLIADTKLRRAKLEMER 848
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67189167 1652 GMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIeELRASLEQTERSRRVAEQELLDASERVQ 1718
Cdd:pfam12128 849 KASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQG-SIGERLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
845-1613 |
2.52e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 72.70 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 845 KSAETEKEMANMKEDFEKAKEDLAKSEAKRKElEEKMVALMQEKnDLQLQVQAEAD--GLADAEERCDQLIKTKIQLEAK 922
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKE-EEKEKKLQEEE-LKLLAKEEEELksELLKLERRKVDDEEKLKESEKE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 923 IKELTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTE----EMAGLDENIAKLTK 998
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESErlssAAKLKEEELELKSE 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 999 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKL---AQESTMDIEN 1075
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKsedLLKETQLVKL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1076 DKQQLDEKLKKKEFEMSNLQSKIEDEQA---LGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISE 1152
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKvllALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1153 RLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEI 1232
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAK 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1233 DDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQldEKDAMVSQLSRGKQAF 1312
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK--EQREKEELKKLKLEAE 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1313 TQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTK---YETDAIQRTEE 1389
Cdd:pfam02463 721 ELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLkveEEKEEKLKAQE 800
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1390 LEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLM---------IDVERSNAACAALDKKQRN-------- 1452
Cdd:pfam02463 801 EELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEeqkleklaeEELERLEEEITKEELLQELllkeeele 880
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1453 FDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKnaYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIH--EL 1530
Cdd:pfam02463 881 EQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN--EIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNkeEE 958
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1531 EKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIR 1610
Cdd:pfam02463 959 EERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFF 1038
|
...
gi 67189167 1611 SRN 1613
Cdd:pfam02463 1039 YLE 1041
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
851-1259 |
7.89e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 7.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 851 KEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEAD--GLADAEERCDQLIKTKIQLEAKIKELTE 928
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 929 RAEDEEEINAELTAKKRKLEDECSEL----KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQ 1004
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1005 EAHQ------------------QTLDDLQAEEDKV---------------NTLTKAKTKLEQQVDDLEGSLEQEKKLRMD 1051
Cdd:COG4717 241 LEERlkearlllliaaallallGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1052 LERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEfemsnlqskIEDEQALGMQLQKKIKELqarIEELEEEIEAERA 1131
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAE---------ELEEELQLEELEQEIAAL---LAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1132 SRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKR--EAEFQKMRRDLEEATLQHEataaALRKKHADSVAELG- 1208
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELE----ELREELAELEAELEq 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 67189167 1209 -EQIDNLQRVKQKLEKEKSELKMEIDDLASNMetvsKAKGNLEKMCRTLEDQ 1259
Cdd:COG4717 465 lEEDGELAELLQELEELKAELRELAEEWAALK----LALELLEEAREEYREE 512
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
989-1592 |
9.83e-12 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 70.32 E-value: 9.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 989 LDE--NIAKLTKEKKALQEahqqTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLA 1066
Cdd:PRK01156 155 LDEilEINSLERNYDKLKD----VIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1067 qestmdiENDKQQLDEklkkkefEMSNLQSKIEDEQALGMQLqkkikelqarieeleeeieaerasrAKAEKQRSDLSRE 1146
Cdd:PRK01156 231 -------MDDYNNLKS-------ALNELSSLEDMKNRYESEI-------------------------KTAESDLSMELEK 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1147 LEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKleKEKS 1226
Cdd:PRK01156 272 NNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKK--SRYD 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1227 ELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLS 1306
Cdd:PRK01156 350 DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLN 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1307 RGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEE----QEAKAELQRAMSKANSEVAQWRTKYETD 1382
Cdd:PRK01156 430 QRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKksrlEEKIREIEIEVKDIDEKIVDLKKRKEYL 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1383 AIQRTEELEEAKKKLAQ-------------RLQDAEEHVEAVNSKCASLEKTKQRLQNEvEDLMIDVERSNAACAALDKK 1449
Cdd:PRK01156 510 ESEEINKSINEYNKIESaradledikikinELKDKHDKYEEIKNRYKSLKLEDLDSKRT-SWLNALAVISLIDIETNRSR 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1450 QRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHE 1529
Cdd:PRK01156 589 SNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPD 668
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67189167 1530 LEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVkSEIDRKIAEKDEEIDQLKR 1592
Cdd:PRK01156 669 LKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRI-NELSDRINDINETLESMKK 730
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1207-1902 |
2.30e-11 |
|
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: 69.01 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1207 LGEQIDNLQRVKQKLEKEKSELKMEiddlasnMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELS-TQKARLH 1285
Cdd:pfam07111 61 LSQQAELISRQLQELRRLEEEVRLL-------RETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAgAEMVRKN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1286 TESGEfSRQLDEKDAM-VSQLSRGKQAFTQQIEELKRQLEEESKAKNAL-------AHALQSARHDCDLLREQY---EEE 1354
Cdd:pfam07111 134 LEEGS-QRELEEIQRLhQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLetkrageAKQLAEAQKEAELLRKQLsktQEE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1355 QEAKAELQRAMSKANSEVAQWRTKYETDAIQRtEELEEAKKKLAQRLQDAEEHVEAVNSKCASLektKQRLQNEVEDLMI 1434
Cdd:pfam07111 213 LEAQVTLVESLRKYVGEQVPPEVHSQTWELER-QELLDTMQHLQEDRADLQATVELLQVRVQSL---THMLALQEEELTR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1435 DVERSNAACAALDKKQRNfdkVLAEWKQKYEETQAELEASQKESRSlstelfkvknayeesldqletlkrENKNLQQEIS 1514
Cdd:pfam07111 289 KIQPSDSLEPEFPKKCRS---LLNRWREKVFALMVQLKAQDLEHRD------------------------SVKQLRGQVA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1515 DLTEQIAEGgkhihelekikkqiDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKrnh 1594
Cdd:pfam07111 342 ELQEQVTSQ--------------SQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLK--- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1595 lRVVESMQSTLDaeirsrndalRIKKKMeGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKdTQLHLDDALRGQDDLKEQ 1674
Cdd:pfam07111 405 -FVVNAMSSTQI----------WLETTM-TRVEQAVARIPSLSNRLSYAVRKVHTIKGLMA-RKVALAQLRQESCPPPPP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1675 LAMVERRANLMQAEIEELRASLE-QTERSRRVAEQELLDASERVQLLHTQntsLINTKKKLETDISQIQGEMEDIVQEAR 1753
Cdd:pfam07111 472 APPVDADLSLELEQLREERNRLDaELQLSAHLIQQEVGRAREQGEAERQQ---LSEVAQQLEQELQRAQESLASVGQQLE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1754 NAEEKAKKAITDAAMMAEELKKEQdtsahlERMKKNMEQTVKDLQHRLDEaeqlalkggkkQIQKLEARVreleNEVENE 1833
Cdd:pfam07111 549 VARQGQQESTEEAASLRQELTQQQ------EIYGQALQEKVAEVETRLRE-----------QLSDTKRRL----NEARRE 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 1834 QKRnieAVKGLRKHERRVKeltyQTEEDRKNVLRLQDLVDKLQTKVKAykRQAEEAEEQSNVNLAKFRK 1902
Cdd:pfam07111 608 QAK---AVVSLRQIQHRAT----QEKERNQELRRLQDEARKEEGQRLA--RRVQELERDKNLMLATLQQ 667
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1240-1931 |
2.38e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1240 ETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRgkqaftqQIEEl 1319
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIAR-------KAED- 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1320 KRQLEEESKAKNAlaHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDA-IQRTEELEEAKKkla 1398
Cdd:PTZ00121 1163 ARKAEEARKAEDA--KKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKkAEAVKKAEEAKK--- 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1399 qrlqDAEEhveavnSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQrnfdkvlAEWKQKYEETQAELEASQKES 1478
Cdd:PTZ00121 1238 ----DAEE------AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK-------ADELKKAEEKKKADEAKKAEE 1300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1479 RSLSTELfKVKNAYEESLDQLETLKRENKNLQQEISDLTEQiAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHE 1558
Cdd:PTZ00121 1301 KKKADEA-KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE-AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1559 EGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALriKKKMEGDLNEMEIQLNHANR 1638
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEA 1456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1639 QAAEAIRNlrntqgmlKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSrrvaeQELLDASErvq 1718
Cdd:PTZ00121 1457 KKAEEAKK--------KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA-----DEAKKAEE--- 1520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1719 llhtqntslintKKKLEtdisqiqgemedivqEARNAEEKAKkaiTDAAMMAEELKKEQDTSaHLERMKKNMEQTVKDLQ 1798
Cdd:PTZ00121 1521 ------------AKKAD---------------EAKKAEEAKK---ADEAKKAEEKKKADELK-KAEELKKAEEKKKAEEA 1569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1799 HRLDEAEQLALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKglRKHERRVK-ELTYQTEEDRKNVLRLQDLVDKLQT 1877
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 67189167 1878 KVKAYKRqAEEAEEQSNVNLAKF----RKIQHELEEAEERADIAESQVNKLRVKSREV 1931
Cdd:PTZ00121 1648 KAEELKK-AEEENKIKAAEEAKKaeedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1202-1805 |
3.98e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1202 DSVAELGEQIDNLQRVKQKLEKEKSELKM--EIDDLASNMETVSKAKGNLEKMCRTLEDQLSEvkTKEEEQQRLINELST 1279
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1280 QKARLHTESGEFSRQLDEKDAMVSQLSRGKQAF-TQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAK 1358
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1359 AELQRamskansEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTK---------------Q 1423
Cdd:COG4913 383 AALRA-------EAAALLEALE----EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniparllalrdalaE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1424 RLQNEVEDL-----MIDVERS-----NAACAAL---------DkkQRNFDKVLaEW-----------KQKYEETQAELEA 1473
Cdd:COG4913 452 ALGLDEAELpfvgeLIEVRPEeerwrGAIERVLggfaltllvP--PEHYAAAL-RWvnrlhlrgrlvYERVRTGLPDPER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1474 SQKESRSLSTELFKVKNAYEESLDQL-------------ETLKRENKNLQQE--ISDLTEQIAEGGKH------------ 1526
Cdd:COG4913 529 PRLDPDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRAITRAgqVKGNGTRHEKDDRRrirsryvlgfdn 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1527 ---IHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEID-----RKIAEKDEEIDQLKRNHlrvv 1598
Cdd:COG4913 609 rakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaeREIAELEAELERLDASS---- 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1599 esmqstldaeirsrndalrikkkmeGDLNEMEIQLNHANRQAAEAIRNLrntqgmlkdtqlhlddalrgqDDLKEQLAMV 1678
Cdd:COG4913 685 -------------------------DDLAALEEQLEELEAELEELEEEL---------------------DELKGEIGRL 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1679 ERRANLMQAEIEELRASLEQTERSRRVAEQELLDasERVQLLHTQNtSLINTKKKLETDISQIQGEMEDIVQEARNAEEK 1758
Cdd:COG4913 719 EKELEQAEEELDELQDRLEAAEDLARLELRALLE--ERFAAALGDA-VERELRENLEERIDALRARLNRAEEELERAMRA 795
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67189167 1759 AKK--------------AITDAAMMAEELkKEQDTSAHLERMK----KNMEQTVKDLQHRLDEAE 1805
Cdd:COG4913 796 FNRewpaetadldadleSLPEYLALLDRL-EEDGLPEYEERFKellnENSIEFVADLLSKLRRAI 859
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
847-1280 |
4.73e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.14 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 847 AETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKMvalmQEKNDLQLQVQAEADGLAD-----------AEERCDQLIKT 915
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELAEEV----RDLRERLEELEEERDDLLAeaglddadaeaVEARREELEDR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 916 KIQLEAKIKE--------------LTERAEDEEEINAELTAKKRKLEDEC--------------SELKKDIDDLELTLAK 967
Cdd:PRK02224 323 DEELRDRLEEcrvaaqahneeaesLREDADDLEERAEELREEAAELESELeeareavedrreeiEELEEEIEELRERFGD 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 968 VEKEKHATENKVKNLTEEMAGLDENIAKLT----------KEKKALQEA--------------HQQTLDDlqaEEDKVNT 1023
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEatlrtarervEEAEALLEAgkcpecgqpvegspHVETIEE---DRERVEE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1024 LTKAKTKLEQQVDDLEGSLEQEKKL-----RMDLERAKRKLEGDLKLAQESTmdIENDKQQLDEKLKKKEfemsNLQSKI 1098
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERAEDLveaedRIERLEERREDLEELIAERRET--IEEKRERAEELRERAA----ELEAEA 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1099 EDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSrELEEISERLEEAGGATSAQIEMNKKRE---AEF 1175
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDERRerlAEK 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1176 QKMRRDLEEATLQHEATAAALRKKHADS-VAELGEQIDNLQRVKQKLEKEKSELKMEIDDLasnmETVSKAKGNLEKMCR 1254
Cdd:PRK02224 633 RERKRELEAEFDEARIEEAREDKERAEEyLEQVEEKLDELREERDDLQAEIGAVENELEEL----EELRERREALENRVE 708
|
490 500
....*....|....*....|....*.
gi 67189167 1255 TLEDQLSEVKTKEEEQQRLINELSTQ 1280
Cdd:PRK02224 709 ALEALYDEAEELESMYGDLRAELRQR 734
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1315-1877 |
6.47e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.76 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1315 QIEELKRQLEE-ESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRtkyetdaiQRTEELEEA 1393
Cdd:PRK02224 188 SLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR--------EELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1394 KKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEA 1473
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1474 SQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEA 1553
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1554 SLE--HEEGKILRIQLElnqvksEIDRKIAEKDEEIDQLKrnhlrVVESMQSTLDAEIRSRNDALRIKK-KMEGDLNEME 1630
Cdd:PRK02224 420 ERDelREREAELEATLR------TARERVEEAEALLEAGK-----CPECGQPVEGSPHVETIEEDRERVeELEAELEDLE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1631 IQLNHANrQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQEL 1710
Cdd:PRK02224 489 EEVEEVE-ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1711 LDASERVQLLHTQNTSLINTKKKLEtDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmKKNM 1790
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELE--AEFD 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1791 EQTVKDLQHRLDEAEQLalkggkkqIQKLEARVRELENEVENEQKRnIEAVkglrkhERRVKELtyqtEEDRKNVLRLQD 1870
Cdd:PRK02224 645 EARIEEAREDKERAEEY--------LEQVEEKLDELREERDDLQAE-IGAV------ENELEEL----EELRERREALEN 705
|
....*..
gi 67189167 1871 LVDKLQT 1877
Cdd:PRK02224 706 RVEALEA 712
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
841-1522 |
1.04e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 67.05 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 841 KPLLKSAETEKEMANM-KEDFEKAKEDLAKSEAKRKELEEKMVALmqeKNDLQLQVQAEADGLADAEercdqliKTKIQL 919
Cdd:pfam05483 144 KDLIKENNATRHLCNLlKETCARSAEKTKKYEYEREETRQVYMDL---NNNIEKMILAFEELRVQAE-------NARLEM 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 920 EAKIKELTERAED-EEEINAELTAKKRK---LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAK 995
Cdd:pfam05483 214 HFKLKEDHEKIQHlEEEYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDH 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 996 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKL----EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTM 1071
Cdd:pfam05483 294 LTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1072 DIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEIS 1151
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIH 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1152 ERLEEAGGATSAQIEMNKkreaEFQKMRRDLEEATLQHeataaalrkkhadsvAELGEQIDNLQRVKQKLEKEKSELKME 1231
Cdd:pfam05483 454 DLEIQLTAIKTSEEHYLK----EVEDLKTELEKEKLKN---------------IELTAHCDKLLLENKELTQEASDMTLE 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1232 iddLASNMETVSKAKGNLEKMcrtledqLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQA 1311
Cdd:pfam05483 515 ---LKKHQEDIINCKKQEERM-------LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLK 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1312 FTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELE 1391
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIE 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1392 EAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMidversnaacAALDKKQRNFDKVLAEWKQKYEETQAEL 1471
Cdd:pfam05483 665 DKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMV----------ALMEKHKHQYDKIIEERDSELGLYKNKE 734
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 67189167 1472 EASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAE 1522
Cdd:pfam05483 735 QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
848-1276 |
1.30e-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: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 848 ETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEK-----NDLQLQVQAEADGLADAEERCDQLIKTKIQLEAK 922
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 923 I----KELTERAEDEEEINAELTAKKRKLEDecseLKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTK 998
Cdd:TIGR04523 344 IsqlkKELTNSESENSEKQRELEEKQNEIEK----LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 999 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLklaqestmdiENDKQ 1078
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL----------EQKQK 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1079 QLDEklKKKEFEMSNLQSKiedeqalgmQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEI-----SER 1153
Cdd:TIGR04523 490 ELKS--KEKELKKLNEEKK---------ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfelkKEN 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1154 LEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsVAELGEQIDNLQRVKQKLEKEKSELKMEID 1233
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE----IEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 67189167 1234 DLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINE 1276
Cdd:TIGR04523 635 NIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
862-1704 |
1.81e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.52 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 862 KAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKiQLEAKIKELTERAEDEEEINAELT 941
Cdd:PRK04863 297 TSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIE-RYQADLEELEERLEEQNEVVEEAD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 942 AKKRKLEDECSELKKDIDDLELTLAKVEKEkhatenkvKNLTEEMAGldeniaKLTKEKKALQEAHQQT-LDDLQAEEDK 1020
Cdd:PRK04863 376 EQQEENEARAEAAEEEVDELKSQLADYQQA--------LDVQQTRAI------QYQQAVQALERAKQLCgLPDLTADNAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1021 VnTLTKAKTKLEQQVDDLegsLEQEKKLRMDlERAKRKLEGDLKLAQESTMDIenDKQQLDEKLKKKEFEMSNLQSKIED 1100
Cdd:PRK04863 442 D-WLEEFQAKEQEATEEL---LSLEQKLSVA-QAAHSQFEQAYQLVRKIAGEV--SRSEAWDVARELLRRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1101 EQALGMQLqkkiKELQARIEELEEEIEAERASRAKAEKQRSDLSrELEEISERLEEAGGATSAQIEMNKKREAEFQKMRR 1180
Cdd:PRK04863 515 LQQLRMRL----SELEQRLRQQQRAERLLAEFCKRLGKNLDDED-ELEQLQEELEARLESLSESVSEARERRMALRQQLE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1181 DLEEATLQHEATAAALRKKHaDSVAELGEQ----IDNLQRV----KQKLEKEKsELKMEIDDLASN-------METVSKA 1245
Cdd:PRK04863 590 QLQARIQRLAARAPAWLAAQ-DALARLREQsgeeFEDSQDVteymQQLLERER-ELTVERDELAARkqaldeeIERLSQP 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1246 KGNLEKMCRTLEDQLSEVKTKE-------EE------------QQRLINELSTQKARLHTE------------------S 1288
Cdd:PRK04863 668 GGSEDPRLNALAERFGGVLLSEiyddvslEDapyfsalygparHAIVVPDLSDAAEQLAGLedcpedlyliegdpdsfdD 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1289 GEFSRQLDEKDAMV------SQLSR-------GKQAFTQQIEELKRQLEEESKAKNALAHALQsarhDCDLLREQYE--- 1352
Cdd:PRK04863 748 SVFSVEELEKAVVVkiadrqWRYSRfpevplfGRAAREKRIEQLRAEREELAERYATLSFDVQ----KLQRLHQAFSrfi 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1353 ----------EEQEAKAELQRAMSKANSEVAQwrtkyetdaiqrteeLEEAKKKLAQRLQDAEEHVEAVNsKCASLEKTK 1422
Cdd:PRK04863 824 gshlavafeaDPEAELRQLNRRRVELERALAD---------------HESQEQQQRSQLEQAKEGLSALN-RLLPRLNLL 887
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1423 QR--LQNEVEDLMIDVERSNAACAALDKKQRNFDKV-------------LAEWKQKYEETQAELEASQKESRSLsTELFK 1487
Cdd:PRK04863 888 ADetLADRVEEIREQLDEAEEAKRFVQQHGNALAQLepivsvlqsdpeqFEQLKQDYQQAQQTQRDAKQQAFAL-TEVVQ 966
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1488 VKN--AYEESLDQL-------ETLKRENKNLQQEISDLTEQIAEggkHIHELEKIKKQIDQEKSELQASLEE-AEASLEH 1557
Cdd:PRK04863 967 RRAhfSYEDAAEMLaknsdlnEKLRQRLEQAEQERTRAREQLRQ---AQAQLAQYNQVLASLKSSYDAKRQMlQELKQEL 1043
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1558 EEgkilriqLELNQVKSEIDRKIAEKDEEIDQLKRNHLRV--VESMQSTLDAEIRSRNDALRikkKMEGDLNEMEIQLNH 1635
Cdd:PRK04863 1044 QD-------LGVPADSGAEERARARRDELHARLSANRSRRnqLEKQLTFCEAEMDNLTKKLR---KLERDYHEMREQVVN 1113
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1636 ANRQAAEAIRNLRNTqGMLKdtQLHL-DDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRR 1704
Cdd:PRK04863 1114 AKAGWCAVLRLVKDN-GVER--RLHRrELAYLSADELRSMSDKALGALRLAVADNEHLRDVLRLSEDPKR 1180
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
835-1508 |
1.86e-10 |
|
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: 66.61 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 835 KLYFKIKPLLKSAETEKEMANMKEDFEKAKEDLAKSE--AKRKELEEKMVALMQEKNDLQLQVQAEADGLADAE------ 906
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttr 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 907 ERCDQLIKTKIQLEAKIKELTERAEDEEEINAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKV 979
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 980 KNLTEEMAGLDENIAKLTKekkalQEAHQQTLDDLQAEEDKVNT----LTKAKTKLEQQVDDLEGSLEQEKKLRMDLERA 1055
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCG-----SQDEESDLERLKEEIEKSSKqramLAGATAVYSQFITQLTDENQSCCPVCQRVFQT 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1056 KRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAK 1135
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1136 AEKQRSDLSRELEEISERLEEAGGATSAQIEMnKKREAEFQKMRRDLEEATLqhEATAAALRKKHADSVAEL---GEQID 1212
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVCLTDVTIMERFQMEL-KDVERKIAQQAAKLQGSDL--DRTVQQVNQEKQEKQHELdtvVSKIE 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1213 NLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVktkeeeqQRLINELSTQKARLHTESGEFS 1292
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV-------QSLIREIKDAKEQDSPLETFLE 919
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1293 RQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAK-AELQRAMSKANSE 1371
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQlEECEKHQEKINED 999
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1372 VAQWRTKYETDAIQ------------RTEELEEAKKKLAQRLQDAEEhveavnSKCASLEKTKQRLQNEVEDLMIDVERS 1439
Cdd:TIGR00606 1000 MRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELKQHLKEMGQ------MQVLQMKQEHQKLEENIDLIKRNHVLA 1073
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1440 NAACAALDKKQRNFDKVLAEWK-QKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKN 1508
Cdd:TIGR00606 1074 LGRQKGYEKEIKHFKKELREPQfRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEIN 1143
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1530-1934 |
1.98e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1530 LEKIKKQIDQEKS--------ELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKiAEKDEEIDQLKRNhlrvVESM 1601
Cdd:PRK02224 189 LDQLKAQIEEKEEkdlherlnGLESELAELDEEIERYEEQREQARETRDEADEVLEEH-EERREELETLEAE----IEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1602 QSTLDAEIRSRNDALRikkkmegdlnemEIQlnhANRQAAEAIRNLRNtqGMLKDTQLhlDDAlrGQDDLKEQLAMVERR 1681
Cdd:PRK02224 264 RETIAETEREREELAE------------EVR---DLRERLEELEEERD--DLLAEAGL--DDA--DAEAVEARREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1682 ANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKK 1761
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1762 AITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLaLKGGK---------------------KQIQKLE 1820
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-LEAGKcpecgqpvegsphvetieedrERVEELE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1821 ARVRELENEVENEQKRnIEAVKGLRKHERRVKELtyqtEEDRKNVlrlQDLVDKLQTKVKAYKRQAEEAEEQSNvnlakf 1900
Cdd:PRK02224 482 AELEDLEEEVEEVEER-LERAEDLVEAEDRIERL----EERREDL---EELIAERRETIEEKRERAEELRERAA------ 547
|
410 420 430
....*....|....*....|....*....|....
gi 67189167 1901 rKIQHELEEAEERADIAESQVNKLRVKSREVHTK 1934
Cdd:PRK02224 548 -ELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1191-1417 |
2.21e-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: 64.79 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1191 ATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQ 1270
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1271 QRLINELSTQKARLHTESGEFSRQLDEKDAM----VSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDL 1346
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 67189167 1347 LREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCAS 1417
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
910-1537 |
2.92e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 65.69 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 910 DQLIKTKIQLEAKIKELTERAEDEEEINAELtakkRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL 989
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRAEISNIDYLEEKL----KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 990 DE---NIAKLTKEKKALQEAHQQTLDDLQAEEDKVNtltkaktkleqqvdDLEGSLEQEKKLRMDLERAKRklegdlkla 1066
Cdd:PRK01156 238 KSalnELSSLEDMKNRYESEIKTAESDLSMELEKNN--------------YYKELEERHMKIINDPVYKNR--------- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1067 qESTMDIENDKQQLDEKLKKkefeMSNLQSKIEDEQAlgmqLQKKIKELQARIEELEeeieaerasraKAEKQRSDLSRE 1146
Cdd:PRK01156 295 -NYINDYFKYKNDIENKKQI----LSNIDAEINKYHA----IIKKLSVLQKDYNDYI-----------KKKSRYDDLNNQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1147 LEEISERLEEAGGATSAQIEMNKKREAEFQKMRR---DLEEATLQHEATAAALRKKHadsvAELGEQIDNLQRVKQKLEK 1223
Cdd:PRK01156 355 ILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERmsaFISEILKIQEIDPDAIKKEL----NEINVKLQDISSKVSSLNQ 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1224 EKSELKMEIDDLASNMETVSKAkgNLEKMCRTledqlsevKTKEEEQQRLINELSTQKARLHTESGEFSRQ---LDEK-- 1298
Cdd:PRK01156 431 RIRALRENLDELSRNMEMLNGQ--SVCPVCGT--------TLGEEKSNHIINHYNEKKSRLEEKIREIEIEvkdIDEKiv 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1299 --DAMVSQLSRGK----QAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAElqrAMSKANSEv 1372
Cdd:PRK01156 501 dlKKRKEYLESEEinksINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRT---SWLNALAV- 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1373 aqwRTKYETDAIQ-RTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQR 1451
Cdd:PRK01156 577 ---ISLIDIETNRsRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKID 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1452 NFDKVLAEwKQKYEETQAELEASQKESrslSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELE 1531
Cdd:PRK01156 654 NYKKQIAE-IDSIIPDLKEITSRINDI---EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK 729
|
....*.
gi 67189167 1532 KIKKQI 1537
Cdd:PRK01156 730 KIKKAI 735
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1210-1915 |
4.34e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.04 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1210 QIDNLQRVKQKLEKEKSELKMEIDDLASNMETV----SKAKGNLEKMCRTLEDQLSEVKTKEEeqqrLINELSTQKARLH 1285
Cdd:TIGR04523 55 ELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLndklKKNKDKINKLNSDLSKINSEIKNDKE----QKNKLEVELNKLE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1286 TESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAM 1365
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1366 SKANSEVAQWrtkyeTDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAA 1445
Cdd:TIGR04523 211 QKNKSLESQI-----SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1446 LDKKQRNFDKVLAEWKQKYE-----ETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQI 1520
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1521 AEGGKhihELEKIKKQIDQEKSELQasleeaeasleheegkilriqlELNQVKSEIDRKIaEKDEEIDQLKRNHLRVVES 1600
Cdd:TIGR04523 366 EEKQN---EIEKLKKENQSYKQEIK----------------------NLESQINDLESKI-QNQEKLNQQKDEQIKKLQQ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1601 MQSTLDAEIRsrndalrikkkmegDLNEMEIQLNhanrqaaEAIRNLRNTQGMLKDTQLHLDDAlrgQDDLKEQLAMVER 1680
Cdd:TIGR04523 420 EKELLEKEIE--------------RLKETIIKNN-------SEIKDLTNQDSVKELIIKNLDNT---RESLETQLKVLSR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1681 RANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIvqearnaEEKAK 1760
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL-------EDELN 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1761 KaitdaamMAEELKKEQdtsahLERMKKNMEQTVKDLQHrldeaeqlalkggkkQIQKLEARVRELENEVENEQKRNIEA 1840
Cdd:TIGR04523 549 K-------DDFELKKEN-----LEKEIDEKNKEIEELKQ---------------TQKSLKKKQEEKQELIDQKEKEKKDL 601
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67189167 1841 VKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERAD 1915
Cdd:TIGR04523 602 IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1681-1930 |
4.54e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1681 RANLMQAE--IEELRASLEQTERSRRVAEQ------------------ELLDASERVQLLHTQNTSLINTKKKLETDISQ 1740
Cdd:COG1196 185 EENLERLEdiLGELERQLEPLERQAEKAERyrelkeelkeleaellllKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1741 IQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQlalkggkkQIQKLE 1820
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE--------ELEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1821 ARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAkf 1900
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-- 414
|
250 260 270
....*....|....*....|....*....|
gi 67189167 1901 RKIQHELEEAEERADIAESQVNKLRVKSRE 1930
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEAL 444
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1237-1737 |
7.17e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.36 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1237 SNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKAR------LHTESGEFSRQLDEK----DAMVSQLS 1306
Cdd:pfam05483 209 ARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKmkdltfLLEESRDKANQLEEKtklqDENLKELI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1307 RGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEakaELQRAMSKANSEVAQWRTKyetdaiqr 1386
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQME---ELNKAKAAHSFVVTEFEAT-------- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1387 TEELEEAKKKLAQRLQDAEEHVEAVN---SKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQK 1463
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLKIITmelQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1464 YEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKR---------------------ENKNLQQEISDLTEQIAE 1522
Cdd:pfam05483 438 EQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTelekeklknieltahcdklllENKELTQEASDMTLELKK 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1523 GGKHI----HELEKIKKQID---QEKSELQASLEEAEASL--EHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRN 1593
Cdd:pfam05483 518 HQEDIinckKQEERMLKQIEnleEKEMNLRDELESVREEFiqKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1594 HLRVVESMQSTLDAEIRSRNDALRIKKKMEG--------DLNEMEIQLNHANRQAAEAIRNLR-----------NTQGML 1654
Cdd:pfam05483 598 NLKKQIENKNKNIEELHQENKALKKKGSAENkqlnayeiKVNKLELELASAKQKFEEIIDNYQkeiedkkiseeKLLEEV 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1655 KDTQLHLDDA--------LRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTErsRRVAEQELLDASERVQLLHTQNtS 1726
Cdd:pfam05483 678 EKAKAIADEAvklqkeidKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYK--NKEQEQSSAKAALEIELSNIKA-E 754
|
570
....*....|.
gi 67189167 1727 LINTKKKLETD 1737
Cdd:pfam05483 755 LLSLKKQLEIE 765
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
984-1857 |
8.52e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.21 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 984 EEMAGLDENIAKLTKEK---KALQEAHQQTLDDLQAEEDkvnTLTKAKTKLEQQVDDLEGSL----------EQEKKLRM 1050
Cdd:PRK04863 279 NERRVHLEEALELRRELytsRRQLAAEQYRLVEMARELA---ELNEAESDLEQDYQAASDHLnlvqtalrqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1051 DLERAKRKLEGDL---KLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQarieeleeeie 1127
Cdd:PRK04863 356 DLEELEERLEEQNevvEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE----------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1128 aerasRAKAEKQRSDLsrELEEISERLEEAggATSAQIEMNKKREAEfQKMRrDLEEATLQHEATAAALRKkhadsvaeL 1207
Cdd:PRK04863 425 -----RAKQLCGLPDL--TADNAEDWLEEF--QAKEQEATEELLSLE-QKLS-VAQAAHSQFEQAYQLVRK--------I 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1208 GEQID--NLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMcRTLEDQLSEVKTKEEEQQRLINELSTQKARLH 1285
Cdd:PRK04863 486 AGEVSrsEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQ-QRAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1286 TESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHaLQSARHDCDLLREQYEEEQEAKAELQRAM 1365
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALAR-LREQSGEEFEDSQDVTEYMQQLLEREREL 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1366 SKANSEVAQwrtkyetdaiqRTEELEEAKKKLAQ-------RLQDAEEHVEAV----------------------NSKCA 1416
Cdd:PRK04863 644 TVERDELAA-----------RKQALDEEIERLSQpggsedpRLNALAERFGGVllseiyddvsledapyfsalygPARHA 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1417 ----SLEKTKQRLQNEvEDLMIDVERSNAACAALDkkqrnfDKVLAEWKQKYEETQAELEASQKESRSLSTELFKvKNAY 1492
Cdd:PRK04863 713 ivvpDLSDAAEQLAGL-EDCPEDLYLIEGDPDSFD------DSVFSVEELEKAVVVKIADRQWRYSRFPEVPLFG-RAAR 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1493 EESLDQLetlkrenknlQQEISDLTEQIAEGGKHIHELEKIKKQIDQ----------------EKSELQASLEEAEASLE 1556
Cdd:PRK04863 785 EKRIEQL----------RAEREELAERYATLSFDVQKLQRLHQAFSRfigshlavafeadpeaELRQLNRRRVELERALA 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1557 HEEGKILRIQLELNQVKSEID--RKIAEkdeEIDQLKRNHL--RVVEsmqstLDAEIRSRNDALRIKKKMEGDLNEMEIQ 1632
Cdd:PRK04863 855 DHESQEQQQRSQLEQAKEGLSalNRLLP---RLNLLADETLadRVEE-----IREQLDEAEEAKRFVQQHGNALAQLEPI 926
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1633 LNhANRQAAEAIRNLRNTQGMLKDTQlhlDDALRGQDDLKEqlaMVERRANLMQAE-----------IEELRASLEQTER 1701
Cdd:PRK04863 927 VS-VLQSDPEQFEQLKQDYQQAQQTQ---RDAKQQAFALTE---VVQRRAHFSYEDaaemlaknsdlNEKLRQRLEQAEQ 999
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1702 SRRVAEQELLDASERvqllHTQNT-------SLINTKKKLETDISQiqgEMEDI-VQEARNAEEKakkaitdAAMMAEEL 1773
Cdd:PRK04863 1000 ERTRAREQLRQAQAQ----LAQYNqvlaslkSSYDAKRQMLQELKQ---ELQDLgVPADSGAEER-------ARARRDEL 1065
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1774 KKEQDTSahleRMKKN-MEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVRELENEVENEQKRNIEAVKGLRKH--ERR 1850
Cdd:PRK04863 1066 HARLSAN----RSRRNqLEKQLTFCEAEMDNLT--------KKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNgvERR 1133
|
....*....
gi 67189167 1851 V--KELTYQ 1857
Cdd:PRK04863 1134 LhrRELAYL 1142
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
918-1118 |
9.34e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 918 QLEAKIKELTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLT 997
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 998 KEKK----ALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDI 1073
Cdd:COG4942 104 EELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 67189167 1074 ENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQAR 1118
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
839-1320 |
1.07e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 839 KIKPLLKSAETEKEMANMK---EDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDlQLQVQAE-----ADGLADAEERCD 910
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKkkaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-EAKKKAEeakkkADEAKKAAEAKK 1510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 911 QLIKTKIQLEAKIKELTERAEDEEEINAELTAKKRKLEDE---------------CSELKKDIDDLELTLAKVEKEKHAT 975
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElkkaeelkkaeekkkAEEAKKAEEDKNMALRKAEEAKKAE 1590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 976 ENKVknltEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERA 1055
Cdd:PTZ00121 1591 EARI----EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1056 KRKLEGDLKLAQESTMDiENDKQQLDEKLKKKEFEmsnlqskiedeqalgmqlQKKIKELQARIEELEEEIEAERASRAK 1135
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKA-EEDEKKAAEALKKEAEE------------------AKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1136 AEKQRSDLSRELEEISERLEEAggatsaqiemnKKREAEFQKMRRDLEEatlqhEATAAALRKKHADSVAELGeqidnlq 1215
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEA-----------KKDEEEKKKIAHLKKE-----EEKKAEEIRKEKEAVIEEE------- 1784
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1216 rVKQKLEKEKSELKMEIDDLASNMETVSKA--KGNL--EKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEF 1291
Cdd:PTZ00121 1785 -LDEEDEKRRMEVDKKIKDIFDNFANIIEGgkEGNLviNDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGED 1863
|
490 500
....*....|....*....|....*....
gi 67189167 1292 SrqldEKDAMVSQLSRGKQAFTQQIEELK 1320
Cdd:PTZ00121 1864 G----NKEADFNKEKDLKEDDEEEIEEAD 1888
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1484-1930 |
1.13e-09 |
|
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: 63.66 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1484 ELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKIL 1563
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1564 RIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVesmqsTLDAEIRS-----------RNDALRIKKKMEGDLNEMEIQ 1632
Cdd:pfam01576 93 QLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKV-----TTEAKIKKleedillledqNSKLSKERKLLEERISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1633 LNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLD 1712
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1713 ASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDiVQEARNAEEKAKKaitdaammaeelkkeqDTSAHLERMKKNMEQ 1792
Cdd:pfam01576 248 ALARLEEETAQKNNALKKIRELEAQISELQEDLES-ERAARNKAEKQRR----------------DLGEELEALKTELED 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1793 TVKDlqhrldEAEQLALKGgkkqiqKLEARVRELENEVENEQKRNIEAVKGLR-KHERRVKELTYQTEEDRKNvlrlqdl 1871
Cdd:pfam01576 311 TLDT------TAAQQELRS------KREQEVTELKKALEEETRSHEAQLQEMRqKHTQALEELTEQLEQAKRN------- 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1872 vdklqtkvKAYKRQAEEAEEQSNVNL-AKFRKIQHELEEAEERADIAESQVNKLRVKSRE 1930
Cdd:pfam01576 372 --------KANLEKAKQALESENAELqAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE 423
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
848-1407 |
1.17e-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: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 848 ETEKEMANMKEDFEK---AKEDLAKSEAKRK---ELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKI-QLE 920
Cdd:COG4913 222 DTFEAADALVEHFDDlerAHEALEDAREQIEllePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELeELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 921 AKIKELTERAEDEEEINAELTAKKRKLEDECSELK-KDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKE 999
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1000 KKALQEAHQQTLDDLQAEEDKV-NTLTKAKTKLEQQVDDLEgSLEQEKKlrmDLERAKRKLEGDLKLAqestmdiendKQ 1078
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALeEALAEAEAALRDLRRELR-ELEAEIA---SLERRKSNIPARLLAL----------RD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1079 QLDEKLKKKEFEMSN----LQSKIEDE------------QALGM--------QLQKKIKELQARIEELEEEIEAERASRA 1134
Cdd:COG4913 448 ALAEALGLDEAELPFvgelIEVRPEEErwrgaiervlggFALTLlvppehyaAALRWVNRLHLRGRLVYERVRTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1135 KAEKQRSDLSRELE------------EISER--------LEEAGGATSA-----QIEMNKKReaeFQKMRRDLEEAT--L 1187
Cdd:COG4913 528 RPRLDPDSLAGKLDfkphpfrawleaELGRRfdyvcvdsPEELRRHPRAitragQVKGNGTR---HEKDDRRRIRSRyvL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1188 QHEATA--AALRKKHA---DSVAELGEQIDNLQRVKQKLEKEKSELKM----------------EIDDLASNMETVSKAK 1246
Cdd:COG4913 605 GFDNRAklAALEAELAeleEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvasaerEIAELEAELERLDASS 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1247 GNLekmcRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEE 1326
Cdd:COG4913 685 DDL----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1327 SKAKNALAHALQSARHDCDLLREQYEEeqeakaELQRAMSKANSE----VAQWRTKYET----DAI---QRTEELEEAKK 1395
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEE------ELERAMRAFNREwpaeTADLDADLESlpeyLALldrLEEDGLPEYEE 834
|
650
....*....|..
gi 67189167 1396 KLAQRLQDAEEH 1407
Cdd:COG4913 835 RFKELLNENSIE 846
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1317-1712 |
1.62e-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: 62.61 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1317 EELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEA----KAELQRAMSKANSEVAQWRtkyetdaiQRTEELEE 1392
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQwerqRRELESRVAELKEELRQSR--------EKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1393 AKKKLAQRlqdAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEE---TQA 1469
Cdd:pfam07888 102 KYKELSAS---SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAErkqLQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1470 ELEASQKESRSLSTELFKVKNAYEESLDQLETlkrenknLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLE 1549
Cdd:pfam07888 179 KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASER 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1550 EAEAsleheegkilriqlelnqVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEM 1629
Cdd:pfam07888 252 KVEG------------------LGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1630 EIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERranlmqaEIEELRASLE--QTERSRRVAE 1707
Cdd:pfam07888 314 EADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRR-------ELQELKASLRvaQKEKEQLQAE 386
|
....*.
gi 67189167 1708 -QELLD 1712
Cdd:pfam07888 387 kQELLE 392
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1078-1545 |
1.95e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1078 QQLDEKLKKKEFEMSNLQSKIEDEQALGMQ---LQKKIKELQARIEE--LEEEIEAERASRAKAEKQRSDLSRELEEISE 1152
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEEleeLEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1153 RLEEaggaTSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEI 1232
Cdd:COG4717 154 RLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1233 DDLASNMETVSKAKgNLEKMCRTLEdQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSrqldekdAMVSQLSRGKQAF 1312
Cdd:COG4717 230 EQLENELEAAALEE-RLKEARLLLL-IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLA-------LLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1313 TQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWrtkyetdaiqRTEELEE 1392
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL----------QLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1393 AKKKLAQRLQDAEEhvEAVNSKCASLEKtKQRLQNEVEDLMIDVERSNAACAALDKKQrnfdkVLAEWKQKYEETQAELE 1472
Cdd:COG4717 371 EIAALLAEAGVEDE--EELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEAL-----DEEELEEELEELEEELE 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67189167 1473 ASQKESRSLSTELFKVKNayeesldQLETLKRENK--NLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQ 1545
Cdd:COG4717 443 ELEEELEELREELAELEA-------ELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1230-1704 |
2.37e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1230 MEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGK 1309
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1310 QAFT--QQIEELKRQLEEESKAKNALAHALQSARHdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRT 1387
Cdd:COG4717 126 QLLPlyQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1388 EELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQ--NEVEDLMIDVERSNAACAALDKKQRNFDKV--------- 1456
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLIltiagvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1457 ------LAEWKQKYEETQAELEASQKESRSLSTELfkvknAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHEL 1530
Cdd:COG4717 282 vlgllaLLFLLLAREKASLGKEAEELQALPALEEL-----EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1531 EKIKKQIDQE--KSELQASLEEAEASLEHEegkiLRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQ-STLDA 1607
Cdd:COG4717 357 EELEEELQLEelEQEIAALLAEAGVEDEEE----LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeEELEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1608 EIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRnlrntqgmlkdtqlhLDDALRGQDDLKEQLAMVERRANLMQA 1687
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDGE---------------LAELLQELEELKAELRELAEEWAALKL 497
|
490
....*....|....*..
gi 67189167 1688 EIEELRASLEQTERSRR 1704
Cdd:COG4717 498 ALELLEEAREEYREERL 514
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
918-1246 |
2.68e-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: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 918 QLEAKIKELTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLT 997
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 998 KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDK 1077
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1078 QQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR------------ 1145
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrtqael 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1146 -----ELEEISERLEEA------GGATSAQ--------IEMNKKR----EAEFQKMRRDLEEATLQHEATAAAL------ 1196
Cdd:pfam07888 275 hqarlQAAQLTLQLADAslalreGRARWAQeretlqqsAEADKDRieklSAELQRLEERLQEERMEREKLEVELgrekdc 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 67189167 1197 -RKKHADSVAELGEQIDNL---QRVKQKLEKEKSELKMEIDDLASNMETVSKAK 1246
Cdd:pfam07888 355 nRVQLSESRRELQELKASLrvaQKEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1471-1918 |
2.93e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1471 LEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEe 1550
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1551 aeasleheegkilriQLELNQVKSEIDRKIAEKDEEIDQLKRnhlrvvesmqstldaEIRSRNDALRIKKKMEGDLNEME 1630
Cdd:COG4717 127 ---------------LLPLYQELEALEAELAELPERLEELEE---------------RLEELRELEEELEELEAELAELQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1631 IQLNHANRQAAEAIRNLrntqgmLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQEL 1710
Cdd:COG4717 177 EELEELLEQLSLATEEE------LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1711 LDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKK 1788
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1789 NMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENE---------VENEQK--RNIEAVKGLRKHERRVKELTYQ 1857
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaallaeagVEDEEElrAALEQAEEYQELKEELEELEEQ 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67189167 1858 TEEDRKNVLRLQDLVDK--LQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAE 1918
Cdd:COG4717 411 LEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
862-1672 |
3.52e-09 |
|
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: 62.28 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 862 KAKEDLAKSEAKRKELEEKMVALMQEkndLQLQVQAEADGLADAEERCD--QLIKTKIQLEAKIK-------ELTERAED 932
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARE---LEELSARESDLEQDYQAASDhlNLVQTALRQQEKIEryqedleELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 933 EEEINAELTAKkrkledecselkkdiddleltLAKVEKEKHATENKVKNLTEEMA----GLDENIAKLTKEKKALQ---E 1005
Cdd:COG3096 366 QEEVVEEAAEQ---------------------LAEAEARLEAAEEEVDSLKSQLAdyqqALDVQQTRAIQYQQAVQaleK 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1006 AHQQT-LDDLqAEEDKVNTLTKAKTKLEQQVDDLegsLEQEKKLRMDlERAKRKLEGDLKLAQesTMDIENDKQQLDEKL 1084
Cdd:COG3096 425 ARALCgLPDL-TPENAEDYLAAFRAKEQQATEEV---LELEQKLSVA-DAARRQFEKAYELVC--KIAGEVERSQAWQTA 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1085 KKKEFEMSNLQSKIEDEQALGMQLQKKIKELQarieeleeeieaeraSRAKAEKQRSDLSR----------ELEEISERL 1154
Cdd:COG3096 498 RELLRRYRSQQALAQRLQQLRAQLAELEQRLR---------------QQQNAERLLEEFCQrigqqldaaeELEELLAEL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1155 EeaggatsAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKK-----HADSVAE-----LGEQIDNLQRV----KQK 1220
Cdd:COG3096 563 E-------AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlAAQDALErlreqSGEALADSQEVtaamQQL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1221 LEKEKsELKMEIDDLA-------SNMETVSKAKGNLEKMCRTLEDQLSEVKTKE-------------------EEQQRLI 1274
Cdd:COG3096 636 LERER-EATVERDELAarkqaleSQIERLSQPGGAEDPRLLALAERLGGVLLSEiyddvtledapyfsalygpARHAIVV 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1275 NELSTQKARLHTE----------SGE--------FSRQlDEKDAMVSQLSR--------------GKQAFTQQIEELKRQ 1322
Cdd:COG3096 715 PDLSAVKEQLAGLedcpedlyliEGDpdsfddsvFDAE-ELEDAVVVKLSDrqwrysrfpevplfGRAAREKRLEELRAE 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1323 LEEESK--AKNA--------LAHALQS--ARHDCDLLREQYEEE----QEAKAELQRAMSKANSEVAQWRTKY------- 1379
Cdd:COG3096 794 RDELAEqyAKASfdvqklqrLHQAFSQfvGGHLAVAFAPDPEAElaalRQRRSELERELAQHRAQEQQLRQQLdqlkeql 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1380 --------------ETDAIQRTEELEEAkkklAQRLQDAEEHVEAVNSKCASLEKTKQRLQN---EVEDLMIDVERSNAA 1442
Cdd:COG3096 874 qllnkllpqanllaDETLADRLEELREE----LDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQ 949
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1443 CAALdkKQRNFdkVLAEWKQK-----YEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLT 1517
Cdd:COG3096 950 QRRL--KQQIF--ALSEVVQRrphfsYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLK 1025
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1518 -------EQIAEGGKhihELEKIKKQID--------QEKSELQASLEEAEASLEHEEGKILRIQLE---LNQVKSEIDRK 1579
Cdd:COG3096 1026 ssrdakqQTLQELEQ---ELEELGVQADaeaeerarIRRDELHEELSQNRSRRSQLEKQLTRCEAEmdsLQKRLRKAERD 1102
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1580 IAEKDEEIDQLKRNHLRVVEsmqstldaeiRSRNDALrikkkmEGDLNEMEIQLNHANRQAA---EAIRNLRNTQGMLKd 1656
Cdd:COG3096 1103 YKQEREQVVQAKAGWCAVLR----------LARDNDV------ERRLHRRELAYLSADELRSmsdKALGALRLAVADNE- 1165
|
970
....*....|....*.
gi 67189167 1657 tqlHLDDALRGQDDLK 1672
Cdd:COG3096 1166 ---HLRDALRLSEDPR 1178
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
973-1203 |
3.67e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 973 HATENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSL----EQEKKL 1048
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1049 RMDLERAKRKLEGDLKLAQEStmdieNDKQQLDEKLKKKEFE-----MSNLQSKIEDEQALGMQLQKKIKELQARIEELE 1123
Cdd:COG4942 96 RAELEAQKEELAELLRALYRL-----GRQPPLALLLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1124 EEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADS 1203
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARL----EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
871-1213 |
4.12e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 871 EAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLiktkiqleAKIKELTERAEDEEEINAELTAKKRKLEde 950
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL--------QRLAEYSWDEIDVASAEREIAELEAELE-- 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 951 csELKKDIDDLEltlaKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAktK 1030
Cdd:COG4913 679 --RLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--L 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1031 LEQQVDDLEGSlEQEKKLRMDLERAKRKLEGDLKLAQEstmDIENdkqQLDEKLKKKEFEMSNLQSKIED---------- 1100
Cdd:COG4913 751 LEERFAAALGD-AVERELRENLEERIDALRARLNRAEE---ELER---AMRAFNREWPAETADLDADLESlpeylalldr 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1101 --EQALgMQLQKKIKELqarieeleeeieaerasRAKAEKQ-----RSDLSRELEEISERLEEA---------GGATSAQ 1164
Cdd:COG4913 824 leEDGL-PEYEERFKEL-----------------LNENSIEfvadlLSKLRRAIREIKERIDPLndslkripfGPGRYLR 885
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 67189167 1165 IEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDN 1213
Cdd:COG4913 886 LEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1672-1935 |
5.44e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1672 KEQLAMVERRANLMQAEIEELRASLEQTERSRRVAE--QELLDASERVQLlhtqnTSLINTKKKLETDISQIQGEMEDIV 1749
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYEG-----YELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1750 QEARNAEEKAkkaitdaammaEELKKEqdtSAHLERMKKNMEQTVKDLqhrlDEAEQLALKGG----KKQIQKLEARVRE 1825
Cdd:TIGR02169 251 EELEKLTEEI-----------SELEKR---LEEIEQLLEELNKKIKDL----GEEEQLRVKEKigelEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1826 LENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQH 1905
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250 260 270
....*....|....*....|....*....|
gi 67189167 1906 ELEEAEERADIAESQVNKLRVKSREVHTKV 1935
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEEL 422
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1505-1720 |
5.75e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 5.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1505 ENKNLQQEISDLTEQIAEggkhiheLEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKD 1584
Cdd:COG4942 21 AAAEAEAELEQLQQEIAE-------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1585 EEIDQLKRNHLRVVESMQStldAEIRSRNDALRIKKKMEG--DLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLD 1662
Cdd:COG4942 94 ELRAELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 67189167 1663 DALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLL 1720
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
860-1432 |
6.50e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.51 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 860 FEKAKEDLAKSEaKRKELEEKMVALMQEKNDLQLQVQAEADG---LADAEERCDQLIKTKIQLEAKIKELTERAEDEEEI 936
Cdd:PRK04863 495 WDVARELLRRLR-EQRHLAEQLQQLRMRLSELEQRLRQQQRAerlLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 937 NAELTAKKRKLEDECSELKKDIDdlelTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTkekkalqEAHQQTLDDLQA 1016
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQ----RLAARAPAWLAAQDALARLREQSGEEFEDSQDVT-------EYMQQLLERERE 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1017 EEDKVNTLTKAKTKLEQQVDDLE----GSLEQEKKLR------------------------------------MDLERAK 1056
Cdd:PRK04863 643 LTVERDELAARKQALDEEIERLSqpggSEDPRLNALAerfggvllseiyddvsledapyfsalygparhaivvPDLSDAA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1057 RKLEG------DLKLaqestmdIENDKQQLDEK-LKKKEFE------MSNLQ---SKIEDEQALGmqlqkkikelqarie 1120
Cdd:PRK04863 723 EQLAGledcpeDLYL-------IEGDPDSFDDSvFSVEELEkavvvkIADRQwrySRFPEVPLFG--------------- 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1121 eleeeieaerasRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAEFQKMRR---DLEEATLQH-------- 1189
Cdd:PRK04863 781 ------------RAAREKRIEQLRAEREELAERYATL--------------SFDVQKLQRlhqAFSRFIGSHlavafead 834
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1190 -EATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMeIDDLASNMETVskAKGNLEKMCRTLEDQLSEVKTKE- 1267
Cdd:PRK04863 835 pEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSA-LNRLLPRLNLL--ADETLADRVEEIREQLDEAEEAKr 911
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1268 --EEQQRLINELSTQKARLHTESGEFS---RQLDEKDAMVSQLSRGKQAFTQQI--------EELKRQLEEESKAKNALA 1334
Cdd:PRK04863 912 fvQQHGNALAQLEPIVSVLQSDPEQFEqlkQDYQQAQQTQRDAKQQAFALTEVVqrrahfsyEDAAEMLAKNSDLNEKLR 991
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1335 HALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEvaqWRTKYET--DAIQRTEEL-----EEAKKKLAQRLQDAEEH 1407
Cdd:PRK04863 992 QRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSS---YDAKRQMlqELKQELQDLgvpadSGAEERARARRDELHAR 1068
|
650 660
....*....|....*....|....*
gi 67189167 1408 VEAVNSKCASLEKTKQRLQNEVEDL 1432
Cdd:PRK04863 1069 LSANRSRRNQLEKQLTFCEAEMDNL 1093
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
921-1164 |
6.67e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 6.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 921 AKIKELTERAEDEEEINAELTAKKRKLEdecsELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEK 1000
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELA----ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1001 KALQEahqqtldDLQAEEDKVNTLTKAKTKLEQQvDDLEGSLEQEKKLrmDLERAKRKLEGDLKLAQESTMDIENDKQQL 1080
Cdd:COG4942 93 AELRA-------ELEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFL--DAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1081 DEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGA 1160
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
....
gi 67189167 1161 TSAQ 1164
Cdd:COG4942 243 TPAA 246
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1166-1930 |
6.68e-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: 61.61 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1166 EMNKKREAEFQKMRrDLEEATLQ-HEATAAALRKKHADSVAEL-----GEQIDNLQRVKQKLEKEKSELKMEIDDLASNM 1239
Cdd:TIGR01612 700 DLKSKIDKEYDKIQ-NMETATVElHLSNIENKKNELLDIIVEIkkhihGEINKDLNKILEDFKNKEKELSNKINDYAKEK 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1240 ETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRlinelSTQKARLHTESgeFSRQLDEKDAMVSQLSRGKQAFTQQIEEL 1319
Cdd:TIGR01612 779 DELNKYKSKISEIKNHYNDQINIDNIKDEDAKQ-----NYDKSKEYIKT--ISIKEDEIFKIINEMKFMKDDFLNKVDKF 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1320 KrQLEEESKaknalahalqsarhdcdllrEQYEEEQEAKAELqraMSKANSEVAQWR-TKYETDAIQRTEELEEAKKKLA 1398
Cdd:TIGR01612 852 I-NFENNCK--------------------EKIDSEHEQFAEL---TNKIKAEISDDKlNDYEKKFNDSKSLINEINKSIE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1399 QRLQD------AEEHVEAVNSKCASLEK--TKQRLQNEVEDLMIDVERSNaacAALDKKQRN-FDKVLAEWKQKYEETQA 1469
Cdd:TIGR01612 908 EEYQNintlkkVDEYIKICENTKESIEKfhNKQNILKEILNKNIDTIKES---NLIEKSYKDkFDNTLIDKINELDKAFK 984
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1470 ELEASQKESRslSTELFKVKNAYEESL---------DQLETLKRENKNLQQEISDLTEQIAEGGKHIHE-----LEKIKK 1535
Cdd:TIGR01612 985 DASLNDYEAK--NNELIKYFNDLKANLgknkenmlyHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTsiyniIDEIEK 1062
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1536 QIDQEKSELQAS-LEEAEASLEHEEGkiLRIQLELNQVKSEIDRKIAEKDEEIDQLKRNhlrvVESMQSTLDAEIrsrND 1614
Cdd:TIGR01612 1063 EIGKNIELLNKEiLEEAEINITNFNE--IKEKLKHYNFDDFGKEENIKYADEINKIKDD----IKNLDQKIDHHI---KA 1133
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1615 ALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNlRNTQGMLKDTQ---LHLDDALRGQDDLKEQLAMVerranlmqAEIEE 1691
Cdd:TIGR01612 1134 LEEIKKKSENYIDEIKAQINDLEDVADKAISN-DDPEEIEKKIEnivTKIDKKKNIYDEIKKLLNEI--------AEIEK 1204
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1692 LRASLEQTersrrvaeqelldasERVQLLHTQNTSLI------NTKKKLETDISQIQGEMEDI--VQEARNAEEKAKKAI 1763
Cdd:TIGR01612 1205 DKTSLEEV---------------KGINLSYGKNLGKLflekidEEKKKSEHMIKAMEAYIEDLdeIKEKSPEIENEMGIE 1269
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1764 TDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRL-----DEAEQLALKGGKKQIQK--LEARVRELE-----NEVE 1831
Cdd:TIGR01612 1270 MDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSlkiieDFSEESDINDIKKELQKnlLDAQKHNSDinlylNEIA 1349
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1832 NeqKRNIEAVKGLRKHERRVKELTYQTEEDRKNVlrlQDLVDKLQTKVKAYKrqaeeaeEQSNVNLAKfRKIQHELEEAE 1911
Cdd:TIGR01612 1350 N--IYNILKLNKIKKIIDEVKEYTKEIEENNKNI---KDELDKSEKLIKKIK-------DDINLEECK-SKIESTLDDKD 1416
|
810
....*....|....*....
gi 67189167 1912 ERADIAESQVNKLRVKSRE 1930
Cdd:TIGR01612 1417 IDECIKKIKELKNHILSEE 1435
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
933-1364 |
8.10e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 933 EEEINAELTAKKRKLEDECSELKKDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKAL--QEAHQQT 1010
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1011 LDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgdlKLAQESTMDIENDKQQLDEKLKKKEFE 1090
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE---ELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1091 MSNLQSKIEdeqalgmQLQKKIKELQARIEELEEEIEAERASRAKAEKQRS--------DLSRELEEISERLEEAGGAT- 1161
Cdd:COG4717 208 LAELEEELE-------EAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallALLGLGGSLLSLILTIAGVLf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1162 ---------------SAQIEMNKKREAEFQKMRRDLEEATLQheATAAALRKKHADSVAELGEQIDNLQRVKQKL-EKEK 1225
Cdd:COG4717 281 lvlgllallflllarEKASLGKEAEELQALPALEELEEEELE--ELLAALGLPPDLSPEELLELLDRIEELQELLrEAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1226 SELKMEIDDLASNMETVskakgnLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAmvSQL 1305
Cdd:COG4717 359 LEEELQLEELEQEIAAL------LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EEL 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 1306 SRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDcDLLREQYEEEQEAKAELQRA 1364
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELREL 488
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1134-1341 |
1.15e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1134 AKAEKQRSDLSRELEEISERLEEaggaTSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDN 1213
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1214 LQRVKQKLEKEKSELKM---------------------EIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQR 1272
Cdd:COG4942 92 IAELRAELEAQKEELAEllralyrlgrqpplalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 1273 LINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSAR 1341
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1392-1619 |
1.77e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1392 EAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAEL 1471
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1472 E-----------ASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKkqidQE 1540
Cdd:COG4942 100 EaqkeelaellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER----AE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 1541 KSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIK 1619
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1625-1828 |
1.92e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1625 DLNEMEIQLNHANRQAaEAIRNLRNTQgmlkDTQLHLDDALRGQDDLKEQLAM--VERRANLMQAEIEELRASLEQTERS 1702
Cdd:COG4913 236 DLERAHEALEDAREQI-ELLEPIRELA----ERYAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1703 RRVAEQELLDASERVQLLHTQ-NTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQdtsA 1781
Cdd:COG4913 311 LERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR---A 387
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 67189167 1782 HLERMKKNMEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELEN 1828
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEA-ALRDLRRELRELEAEIASLER 433
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1463-1939 |
1.92e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1463 KYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKS 1542
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1543 ELQAS---LEEAEASLEHEEGKILRIQLELNQVKSEID--RKIAEKDEEIDQLKRNHLRVVESMQSTLDAEirsrNDALR 1617
Cdd:PRK03918 239 EIEELekeLESLEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDEL----REIEK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1618 IKKKMEGDLNEMEIQLNHANRQAAEaIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVER-RANLMQAEIEELRASL 1696
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEKEER-LEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1697 EQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETD-------------------ISQIQGEMEDIVQEARNAEE 1757
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelteehrkelLEEYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1758 KAKKAITDAAMMAEELKKEQDtsahLERMKKNMEQtVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENEVENeQKRN 1837
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESE----LIKLKELAEQ-LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS-LKKE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1838 IEAVKGLRKHERRVKELTYQTEEDRKNVLR---------LQDLVDKLQTKVKAYKR--QAEEAEEQSNVNLAKFRKIQHE 1906
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKeleelgfesVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEE 627
|
490 500 510
....*....|....*....|....*....|...
gi 67189167 1907 LEEAEERADIAESQVNKLRVKSREVHTKVISEE 1939
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1005-1494 |
2.03e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1005 EAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgDLKLAQESTMDIENDKQQLdEKL 1084
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERL-EEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1085 KKKEFEMSNLQSKIEDEQALGMQLQKKIKEL-QARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatSA 1163
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL----EE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1164 QIEmNKKREAEFQKMRRDLEEATLQHEATAAALrkkhadSVAELGEQIDNLQRVKQKLekekseLKMEIDDLASNMETVS 1243
Cdd:COG4717 228 ELE-QLENELEAAALEERLKEARLLLLIAAALL------ALLGLGGSLLSLILTIAGV------LFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1244 KAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRG-KQAFTQQIEELKRQ 1322
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELeEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1323 LEEESKAKN--ALAHALQSArhdcdllrEQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAiqrteeleeakkkLAQR 1400
Cdd:COG4717 375 LLAEAGVEDeeELRAALEQA--------EEYQELKEELEELEEQLEELLGELEELLEALDEEE-------------LEEE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1401 LQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVErsnaacaaldkkqrnfdkvLAEWKQKYEETQAELEASQKESRS 1480
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELEQLEEDGE-------------------LAELLQELEELKAELRELAEEWAA 494
|
490
....*....|....
gi 67189167 1481 LSTELFKVKNAYEE 1494
Cdd:COG4717 495 LKLALELLEEAREE 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1462-1682 |
2.50e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1462 QKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEK 1541
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1542 SELQASLEEAEASLeHEEGKILRIQLELNQVKSEidrKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKK 1621
Cdd:COG4942 100 EAQKEELAELLRAL-YRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 67189167 1622 MEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRA 1682
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1198-1775 |
2.51e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.14 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1198 KKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDdlasnmeTVSKAKGNLEKMCRTLEDQLSEVKTKEEEqqrlINEL 1277
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYN-------NAMDDYNNLKSALNELSSLEDMKNRYESE----IKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1278 STQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSaRHDCDLLREQYEEEQEA 1357
Cdd:PRK01156 262 ESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINK-YHAIIKKLSVLQKDYND 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1358 KAELQRAMSKANSEVAQWRTkYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVE 1437
Cdd:PRK01156 341 YIKKKSRYDDLNNQILELEG-YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1438 RSNAACAALDKKQRNfdkvLAEWKQKYEETQAELEASQKE---SRSLSTE-LFKVKNAYEESLDQLETLKREnknLQQEI 1513
Cdd:PRK01156 420 DISSKVSSLNQRIRA----LRENLDELSRNMEMLNGQSVCpvcGTTLGEEkSNHIINHYNEKKSRLEEKIRE---IEIEV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1514 SDLTEQIAEGGKHIHELEKikKQIDQEKSELQaSLEEAEASLEHEEGKILRIQlELNQVKSEIDRKIAEKDEEIDQLKRN 1593
Cdd:PRK01156 493 KDIDEKIVDLKKRKEYLES--EEINKSINEYN-KIESARADLEDIKIKINELK-DKHDKYEEIKNRYKSLKLEDLDSKRT 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1594 HLRVVESMQSTLDAE-IRSRNDALRIK-KKMEGDLNEMEIQLNHAN-------RQAAEAIRNLRNTQGMLKDTQLHLDDA 1664
Cdd:PRK01156 569 SWLNALAVISLIDIEtNRSRSNEIKKQlNDLESRLQEIEIGFPDDKsyidksiREIENEANNLNNKYNEIQENKILIEKL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1665 LRGQDDLKEQLAMVERRanlmQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGE 1744
Cdd:PRK01156 649 RGKIDNYKKQIAEIDSI----IPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINET 724
|
570 580 590
....*....|....*....|....*....|.
gi 67189167 1745 MEDIvqearnaeEKAKKAITDAAMMAEELKK 1775
Cdd:PRK01156 725 LESM--------KKIKKAIGDLKRLREAFDK 747
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
857-1550 |
2.82e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 59.08 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 857 KEDFEKAKEDLAKSEAKRKELE--EKMVALMQEKndlQLQVQAEADGL-ADAEERCDQLIKTKIQLEAKIKELTER---- 929
Cdd:pfam12128 336 DADIETAAADQEQLPSWQSELEnlEERLKALTGK---HQDVTAKYNRRrSKIKEQNNRDIAGIKDKLAKIREARDRqlav 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 930 AED-----EEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENK------VKNLTEEMAGLDENIAKLTK 998
Cdd:pfam12128 413 AEDdlqalESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLenfderIERAREEQEAANAEVERLQS 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 999 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSL-EQEKKLRMDLERAKRKLeGDLKLAQESTMDIENDK 1077
Cdd:pfam12128 493 ELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlHFLRKEAPDWEQSIGKV-ISPELLHRTDLDPEVWD 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1078 QQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEeieaeraSRAKAEKQRSDLSRELEEISERLEEA 1157
Cdd:pfam12128 572 GSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSARE-------KQAAAEEQLVQANGELEKASREETFA 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1158 GGAtsaqiemnkkreaeFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLAS 1237
Cdd:pfam12128 645 RTA--------------LKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKR 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1238 NMETVSKAKgnLEKMCRTLEDQLSEVKTKEEEQQrlinelSTQKARLHTESGEFSRQLDEKDA---MVSQLSRGKQAFTQ 1314
Cdd:pfam12128 711 EARTEKQAY--WQVVEGALDAQLALLKAAIAARR------SGAKAELKALETWYKRDLASLGVdpdVIAKLKREIRTLER 782
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1315 QIEELKRQLEEESKAKNALAHALQSARhdcDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYET--DAIQRTE-ELE 1391
Cdd:pfam12128 783 KIERIAVRRQEVLRYFDWYQETWLQRR---PRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMerKASEKQQvRLS 859
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1392 EAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQneVEDLMIDVERsnaACAALDKKQRNFDKVLAewKQKYEETQAEL 1471
Cdd:pfam12128 860 ENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQ--LEDLKLKRDY---LSESVKKYVEHFKNVIA--DHSGSGLAETW 932
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1472 EASQKESRSLSTELFKVKNaYEESLDQLETLKreNKNLQQEISDLTEQIAEGGKHIHE----LEKIKKQIDQEKSELQAS 1547
Cdd:pfam12128 933 ESLREEDHYQNDKGIRLLD-YRKLVPYLEQWF--DVRVPQSIMVLREQVSILGVDLTEfydvLADFDRRIASFSRELQRE 1009
|
...
gi 67189167 1548 LEE 1550
Cdd:pfam12128 1010 VGE 1012
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
865-1320 |
2.93e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.96 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 865 EDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIqleAKIKELTERAEDEEEINAELTAKK 944
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIL---AEDEKLLDEKKQFEKIAEELKGKE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 945 RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAG-------LDENIAKLTKEKKALQEAHQQTLDDLQAE 1017
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeklknieLTAHCDKLLLENKELTQEASDMTLELKKH 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1018 EDKVNTLTKAKTKLEQQVDDLEgslEQEKKLRMDLERAKRKL--EGD-----LKLAQESTMDIENDKQQLDEKLKKKEFE 1090
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFiqKGDevkckLDKSEENARSIEYEVLKKEKQMKILENK 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1091 MSNLQSKIEDEQalgmqlqKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKK 1170
Cdd:pfam05483 596 CNNLKKQIENKN-------KNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKI 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1171 REaefQKMRRDLEEAtlqheataaalrKKHADSVAELGEQIDnlQRVKQKlekekselkmeIDDLASNMEtvsKAKGNLE 1250
Cdd:pfam05483 669 SE---EKLLEEVEKA------------KAIADEAVKLQKEID--KRCQHK-----------IAEMVALME---KHKHQYD 717
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1251 KMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELK 1320
Cdd:pfam05483 718 KIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1483-1913 |
3.79e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1483 TELFKVKNAYEESLDQLETLKRENKNLQQEISDlTEQIAEggkHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKI 1562
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKR-TENIEE---LIKEKEKELEEVLREINEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1563 LRIQlelnqvksEIDRKIAEKDEEIDQLKRnHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEME------IQLNHA 1636
Cdd:PRK03918 231 KELE--------ELKEEIEELEKELESLEG-SKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekaeeyIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1637 NRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQ----ELLD 1712
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1713 ASERVQLLHTQNTSLINTKKKLETDISQIQ---GEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEqdtsaHLERMKKN 1789
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITariGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE-----HRKELLEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1790 MEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVRELENEVENEQK--RNIEAVKGLRKHERRVKELTYQT-EEDRKNVL 1866
Cdd:PRK03918 457 YTAELKRIEKELKEIE--------EKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEElEKKAEEYE 528
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 67189167 1867 RLQDLVDKLQTKVKAYKRQAEEAEEQSNvnlaKFRKIQHELEEAEER 1913
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEE 571
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1360-1779 |
4.27e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1360 ELQRAMSKANSEVAQWRTKYET--DAIQRTEELEEAKKKLAQRLQDAEEHVEAvnskcASLEKTKQRLQNEVEDLMIDVE 1437
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEEleELEEELEELEAELEELREELEKLEKLLQL-----LPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1438 RSNAACAALDKKQRNfdkvLAEWKQKYEETQAEL-EASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDL 1516
Cdd:COG4717 150 ELEERLEELRELEEE----LEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1517 TEQIaEGGKHIHELEKIKKQIDQEKSELQA--------SLEEAEASLEHEEGKILRIQLEL-------NQVKSEIDRKIA 1581
Cdd:COG4717 226 EEEL-EQLENELEAAALEERLKEARLLLLIaaallallGLGGSLLSLILTIAGVLFLVLGLlallfllLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1582 EKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAiRNLRNTQGMLKDTQLHL 1661
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1662 DDALRGQDDLKEQLAMVERRANLMQAEIEELR---------ASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKK 1732
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLgeleelleaLDEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 67189167 1733 KLETD--ISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDT 1779
Cdd:COG4717 464 QLEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1066-1283 |
4.66e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1066 AQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR 1145
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1146 ELEEISERLEE-----------------AGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELG 1208
Cdd:COG4942 98 ELEAQKEELAEllralyrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67189167 1209 EQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKAR 1283
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
902-1878 |
4.77e-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: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 902 LADAEERCDQLIKTKIqlEAKIKELTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKE-------KHA 974
Cdd:TIGR01612 527 GFDIDQNIKAKLYKEI--EAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEiiyinklKLE 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 975 TENKVKNLTE---------EMAGLDEN----IAKLTKE-------------------KKALQEAHQQTLDDLQAE----- 1017
Cdd:TIGR01612 605 LKEKIKNISDkneyikkaiDLKKIIENnnayIDELAKIspyqvpehlknkdkiystiKSELSKIYEDDIDALYNElssiv 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1018 --------EDKVNtLTKAKTKLEQQVDDLEGSLEQEKKLRM-DLERAKRKLEGDL-KLAQESTMDIENDKQQLDEKLKKK 1087
Cdd:TIGR01612 685 kenaidntEDKAK-LDDLKSKIDKEYDKIQNMETATVELHLsNIENKKNELLDIIvEIKKHIHGEINKDLNKILEDFKNK 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1088 EFEMSNlqsKIEDEQALGMQLQK---KIKELQarieELEEEIEAERASRAKAEKQRSDLSRE-LEEISERLEEaggaTSA 1163
Cdd:TIGR01612 764 EKELSN---KINDYAKEKDELNKyksKISEIK----NHYNDQINIDNIKDEDAKQNYDKSKEyIKTISIKEDE----IFK 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1164 QIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQI--DNLQRVKQKLEKEKS---ELKMEIDDLASN 1238
Cdd:TIGR01612 833 IINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEIsdDKLNDYEKKFNDSKSlinEINKSIEEEYQN 912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1239 METVSKAKGNLeKMCRTLEDQLSEVKTKeeeqQRLINELSTQKARLHTESGEFSRQLDEK--DAMVSQLSRGKQAFTQ-Q 1315
Cdd:TIGR01612 913 INTLKKVDEYI-KICENTKESIEKFHNK----QNILKEILNKNIDTIKESNLIEKSYKDKfdNTLIDKINELDKAFKDaS 987
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1316 IEELKRQLEEESKAKNALAHALQSARHdcDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKK 1395
Cdd:TIGR01612 988 LNDYEAKNNELIKYFNDLKANLGKNKE--NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIG 1065
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1396 KLAQRLQdaEEHVEAVNSKCASLEKTKQRLQ----------------NEVEDLMIDVErsnaacaALDKKQRNFDKVLAE 1459
Cdd:TIGR01612 1066 KNIELLN--KEILEEAEINITNFNEIKEKLKhynfddfgkeenikyaDEINKIKDDIK-------NLDQKIDHHIKALEE 1136
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1460 WKQKYEETQAELEASQKESRSLSTELFKVKN--AYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIK--- 1534
Cdd:TIGR01612 1137 IKKKSENYIDEIKAQINDLEDVADKAISNDDpeEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKgin 1216
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1535 ------------KQIDQEKSELQASLEEAEA-------------SLEHEEGKILRIQLELN--QVKSEIDRK---IAEK- 1583
Cdd:TIGR01612 1217 lsygknlgklflEKIDEEKKKSEHMIKAMEAyiedldeikekspEIENEMGIEMDIKAEMEtfNISHDDDKDhhiISKKh 1296
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1584 DEEIDQLKRNHLRVVESMQSTLDAeirsrNDalrIKKKMEGDLNEMEIQLNHANRQAAEA-----IRNLRNTQGMLKDTQ 1658
Cdd:TIGR01612 1297 DENISDIREKSLKIIEDFSEESDI-----ND---IKKELQKNLLDAQKHNSDINLYLNEIaniynILKLNKIKKIIDEVK 1368
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1659 LHLDDALRGQDDLKEQLAMVERRANLMQAEI--EELRASLEQTERSRRVAE--QELLDASERVQLLHTQNTSLINTKKKL 1734
Cdd:TIGR01612 1369 EYTKEIEENNKNIKDELDKSEKLIKKIKDDInlEECKSKIESTLDDKDIDEciKKIKELKNHILSEESNIDTYFKNADEN 1448
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1735 ETDISQIQGEMEDIVQEARN-AEEKAKKAITDAAMMAEELKKEQDTS-----------AHLERMKKNMEQTVKDLQHRLD 1802
Cdd:TIGR01612 1449 NENVLLLFKNIEMADNKSQHiLKIKKDNATNDHDFNINELKEHIDKSkgckdeadknaKAIEKNKELFEQYKKDVTELLN 1528
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1803 EAEQLALKGG----KKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTK 1878
Cdd:TIGR01612 1529 KYSALAIKNKfaktKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENK 1608
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1673-1893 |
5.90e-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: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1673 EQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEA 1752
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1753 RNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNMEQTVKDLQHRLDE--AEQLALKGGKKQIQKLEARVREL 1826
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67189167 1827 ENEVENEQKRNIEAVKglrKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQS 1893
Cdd:COG4942 180 LAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1297-1720 |
6.48e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1297 EKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKnalaHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWr 1376
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1377 tkyetDAIQRTEELEEAKKKLAQRLQDAEEHVEAVnskcASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQrnfdkv 1456
Cdd:COG4717 129 -----PLYQELEALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEE------ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1457 LAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQE------------------ISDLTE 1518
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallglggsLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1519 QIAE------GGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKS------------EIDRKI 1580
Cdd:COG4717 274 TIAGvlflvlGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpeellelldrieELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1581 AEKDEEIDQLKRNHLR-----VVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLnhanrqaAEAIRNLRNTQGMLK 1655
Cdd:COG4717 354 REAEELEEELQLEELEqeiaaLLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQL-------EELLGELEELLEALD 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67189167 1656 DTQLHLDDAlrgqdDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAE--QELLDASERVQLL 1720
Cdd:COG4717 427 EEELEEELE-----ELEEELEELEEELEELREELAELEAELEQLEEDGELAEllQELEELKAELREL 488
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1201-1445 |
7.74e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1201 ADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVktkEEEQQRLINELSTQ 1280
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1281 KARLHTESGEFSRQLDeKDAMVSQLSRGKQAFTQQ-IEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKA 1359
Cdd:COG4942 96 RAELEAQKEELAELLR-ALYRLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1360 ELQRAmskansevaqwrtkyETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERS 1439
Cdd:COG4942 175 ELEAL---------------LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
....*.
gi 67189167 1440 NAACAA 1445
Cdd:COG4942 240 AERTPA 245
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
856-1328 |
8.38e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 57.52 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 856 MKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLiktkiqlEAKIKELTERAEDEEE 935
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL-------QTEVDALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 936 INAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQ------ 1009
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalt 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1010 TLDDLQAEEDKV-NTLTKAKTKLEQQVDDlegSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKE 1088
Cdd:pfam10174 440 TLEEALSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1089 FEMS----NLQSKIEDEQALGMQLqKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEIsERLEEAGGATSAQ 1164
Cdd:pfam10174 517 SKLKsleiAVEQKKEECSKLENQL-KKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEV-ERLLGILREVENE 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1165 IEMNKKREAEFQKMR----RDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQK---------LEKEKSELKME 1231
Cdd:pfam10174 595 KNDKDKKIAELESLTlrqmKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQlqleelmgaLEKTRQELDAT 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1232 IDDLASNMETVSKAKGNLEKMCRTLEDQLSEV-KTKEEEQQRLINELSTQKARLHTESGEFSRQLDEkdamVSQLSRGKQ 1310
Cdd:pfam10174 675 KARLSSTQQSLAEKDGHLTNLRAERRKQLEEIlEMKQEALLAAISEKDANIALLELSSSKKKKTQEE----VMALKREKD 750
|
490
....*....|....*...
gi 67189167 1311 AFTQQieeLKRQLEEESK 1328
Cdd:pfam10174 751 RLVHQ---LKQQTQNRMK 765
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1132-1710 |
9.12e-08 |
|
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: 57.06 E-value: 9.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1132 SRAKAEKQRSDLSRELEEISerLEEAGGATSAQIEMNKKREAEFQKMRRDLEEatlQHEATAAALRkkhadsvaelgEQI 1211
Cdd:pfam05557 12 SQLQNEKKQMELEHKRARIE--LEKKASALKRQLDRESDRNQELQKRIRLLEK---REAEAEEALR-----------EQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1212 DNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLinelstqkarlhtesgef 1291
Cdd:pfam05557 76 ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL------------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1292 SRQLDEKDAMVSQLSRGKQAFTQQIEELKrqlEEESKAKNaLAHALQSARHDCDLLREQyEEEQEAKAELQRAMSKANSE 1371
Cdd:pfam05557 138 QERLDLLKAKASEAEQLRQNLEKQQSSLA---EAEQRIKE-LEFEIQSQEQDSEIVKNS-KSELARIPELEKELERLREH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1372 VAQWRTKYETDAIQRtEELEEAKKKLaqrlqdaeEHVEAVNSKCASLEKTKQRLQNEvedlmidversnaacaaldkkqr 1451
Cdd:pfam05557 213 NKHLNENIENKLLLK-EEVEDLKRKL--------EREEKYREEAATLELEKEKLEQE----------------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1452 nfdkvLAEWKQKYEETQAELEASQKESRslstelfkvknayeesldQLETLKRENKNLQQEISDLTEQiaeggkhIHELE 1531
Cdd:pfam05557 261 -----LQSWVKLAQDTGLNLRSPEDLSR------------------RIEQLQQREIVLKEENSSLTSS-------ARQLE 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1532 KIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQlelnqvkseidRKIAEKDEEIDQLKRNhlrvVESMQSTLDAEIRS 1611
Cdd:pfam05557 311 KARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-----------RRVLLLTKERDGYRAI----LESYDKELTMSNYS 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1612 RNDALRIK------KKMEGDLNEMEIQLNHANRqaaeairnlrnTQGMLKDTQLHLD---DALRGQDDLKEQLAMVERRA 1682
Cdd:pfam05557 376 PQLLERIEeaedmtQKMQAHNEEMEAQLSVAEE-----------ELGGYKQQAQTLErelQALRQQESLADPSYSKEEVD 444
|
570 580
....*....|....*....|....*...
gi 67189167 1683 NLMQaEIEELRASLEQTERSRRVAEQEL 1710
Cdd:pfam05557 445 SLRR-KLETLELERQRLREQKNELEMEL 471
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1576-1919 |
1.05e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 57.22 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1576 IDRKIAEKDEEIDQLKRNHLRVVESM--QSTLDAEIRSRNDALRIKKKMEGDLnemEIQLNHANRQAAEAIRnLRNTQGM 1653
Cdd:PLN02939 61 SNSKLQSNTDENGQLENTSLRTVMELpqKSTSSDDDHNRASMQRDEAIAAIDN---EQQTNSKDGEQLSDFQ-LEDLVGM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1654 LKDTQ---LHLDDA-LRGQDDLKEQLAmvERRAnlMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLIN 1729
Cdd:PLN02939 137 IQNAEkniLLLNQArLQALEDLEKILT--EKEA--LQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1730 TKKKLETDISQIQGEMEDIVQEarNAEEKAkkaitDAAMMAEELKKEQDTS---AHLERMKKNMEQTVKDLQHRLDEAEQ 1806
Cdd:PLN02939 213 RGATEGLCVHSLSKELDVLKEE--NMLLKD-----DIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1807 LALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKH---ERRVKELTYQTEEdrKNVLRLQ-DLVDKLQTKVKAY 1882
Cdd:PLN02939 286 DVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNqdlRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLL 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 67189167 1883 KR--QAEEAEEQSNVNL-----AKFRKIQHELEEAEERADIAES 1919
Cdd:PLN02939 364 EErlQASDHEIHSYIQLyqesiKEFQDTLSKLKEESKKRSLEHP 407
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
850-1613 |
1.10e-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: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 850 EKEMANMKEDFEKAKEDLAKS--EAKRKELEEKMVALMQ-----EKNDLQLQVQAEADGLADAEERCDQLIKT----KIQ 918
Cdd:TIGR01612 969 DNTLIDKINELDKAFKDASLNdyEAKNNELIKYFNDLKAnlgknKENMLYHQFDEKEKATNDIEQKIEDANKNipniEIA 1048
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 919 LEAKIKELTERAEDEEEINAELTAKK--RKLEDECSELKKDIDDLEL----TLAKVEKEKHATE-NKVKNlteEMAGLDE 991
Cdd:TIGR01612 1049 IHTSIYNIIDEIEKEIGKNIELLNKEilEEAEINITNFNEIKEKLKHynfdDFGKEENIKYADEiNKIKD---DIKNLDQ 1125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 992 NIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTkleqQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTm 1071
Cdd:TIGR01612 1126 KIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAI----SNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIA- 1200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1072 DIENDK----------------------QQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELqARIEELEEEIEAE 1129
Cdd:TIGR01612 1201 EIEKDKtsleevkginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEM-GIEMDIKAEMETF 1279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1130 RASRAKAEKQRSDLSRELEEISERLEEaggatSAQIEMNKKREAEFQKMRRDLEEATLQHEataaalrkKHADSVAELGE 1209
Cdd:TIGR01612 1280 NISHDDDKDHHIISKKHDENISDIREK-----SLKIIEDFSEESDINDIKKELQKNLLDAQ--------KHNSDINLYLN 1346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1210 QIDNLQRVKQ--KLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLED--QLSEVKTKEE---------EQQRLINE 1276
Cdd:TIGR01612 1347 EIANIYNILKlnKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDdiNLEECKSKIEstlddkdidECIKKIKE 1426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1277 LSTQKARLHTESGEFSRQLDEKDAMVSQLSRgkqafTQQIEELKRQLEEESKAKNAlahalqSARHDCDLlreqyeeeqe 1356
Cdd:TIGR01612 1427 LKNHILSEESNIDTYFKNADENNENVLLLFK-----NIEMADNKSQHILKIKKDNA------TNDHDFNI---------- 1485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1357 akAELQRAMSKANsevaqwrtKYETDAIQRTEELEEAKKKLAQRLQDAEEHVE-----AVNSKCASLEKTKQRLQNEVED 1431
Cdd:TIGR01612 1486 --NELKEHIDKSK--------GCKDEADKNAKAIEKNKELFEQYKKDVTELLNkysalAIKNKFAKTKKDSEIIIKEIKD 1555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1432 L----MIDVERSNAACAALDKKQRNFDKVLAewkqKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLetlkRENK 1507
Cdd:TIGR01612 1556 AhkkfILEAEKSEQKIKEIKKEKFRIEDDAA----KNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCL----KETE 1627
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1508 NLQQEISDLT-----EQIAEGGKHIHELEKIKKQIDQEKSelqaSLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAE 1582
Cdd:TIGR01612 1628 SIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQKK----NIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIE 1703
|
810 820 830
....*....|....*....|....*....|..
gi 67189167 1583 KDEEIDQLKRNHLRVV-ESMQSTLDAEIRSRN 1613
Cdd:TIGR01612 1704 KIKEIAIANKEEIESIkELIEPTIENLISSFN 1735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1066-1283 |
1.28e-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: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1066 AQESTMDIENDKQQLDE---KLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSD 1142
Cdd:COG4942 15 AAAQADAAAEAEAELEQlqqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1143 LSRELEEISERLEE-------AGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsVAELGEQIDNLQ 1215
Cdd:COG4942 95 LRAELEAQKEELAEllralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67189167 1216 RVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKAR 1283
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1249-1522 |
1.47e-07 |
|
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: 56.40 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1249 LEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESK 1328
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1329 AKNALAHALQSARHdcdllREQYEEEQEAKAELQRAMSKANSevaqwrtkyeTDAI-QRTEELEEAKKKLAQRLQDAEEH 1407
Cdd:pfam09726 480 ARASAEKQLAEEKK-----RKKEEEATAARAVALAAASRGEC----------TESLkQRKRELESEIKKLTHDIKLKEEQ 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1408 VEAVNSKCASLEKTKQRlQNEVEDLMidversnAACAALDKKQRNFDKVLAewkqkyEETQAELeasqkesrslstELFk 1487
Cdd:pfam09726 545 IRELEIKVQELRKYKES-EKDTEVLM-------SALSAMQDKNQHLENSLS------AETRIKL------------DLF- 597
|
250 260 270
....*....|....*....|....*....|....*
gi 67189167 1488 vkNAYEESLDQLETLKRENKNLQQEISDLTEQIAE 1522
Cdd:pfam09726 598 --SALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAE 630
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1254-1495 |
1.78e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1254 RTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNAL 1333
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1334 AHALQsarhdcDLLREQYEEEQEAKAELqrAMSKANSEVAQWRTKYETDAIQ----RTEELEEAKKKLAQRLQDAEEHVE 1409
Cdd:COG4942 103 KEELA------ELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAParreQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1410 AVNSKCASLEKTKQRLQNEvedlmidversnaacaaldKKQRNfdKVLAEWKQKYEETQAELEASQKESRSLSTELFKVK 1489
Cdd:COG4942 175 ELEALLAELEEERAALEAL-------------------KAERQ--KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*.
gi 67189167 1490 NAYEES 1495
Cdd:COG4942 234 AEAAAA 239
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1490-1933 |
1.86e-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: 56.37 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1490 NAYEESLDQL-ETL--KRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLE-EAEASLEHEEGKILRI 1565
Cdd:pfam10174 154 GARDESIKKLlEMLqsKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHrRNQLQPDPAKTKALQT 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1566 QLELNQVK-SEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKME---GDLNEMEIQLnhanrQAA 1641
Cdd:pfam10174 234 VIEMKDTKiSSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDqlkQELSKKESEL-----LAL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1642 EAIRNLRNTQGmlKDTQLHLDDalrgqddLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLH 1721
Cdd:pfam10174 309 QTKLETLTNQN--SDCKQHIEV-------LKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1722 TQNTSLINTKKKLETDISQIQGEMEDIVQEARNAE-------EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM-EQT 1793
Cdd:pfam10174 380 GEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDkqlaglkERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQR 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1794 VKDLQHRLDEAEQL--ALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDL 1871
Cdd:pfam10174 460 EREDRERLEELESLkkENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQ 539
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67189167 1872 VDKLQtkvkaykrQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHT 1933
Cdd:pfam10174 540 LKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVEN 593
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1668-1904 |
2.12e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1668 QDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRV--AEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEM 1745
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1746 EDIvQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNMEQTVKDLQHRLDEAEQLALKGGKKQ 1815
Cdd:COG3206 243 AAL-RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1816 IQKLEARVRELENEVENEQKRnieaVKGLRKHERRVKELTYQTEEDRKNvlrLQDLVDKLQtkvkaykrqaeEAEEQSNV 1895
Cdd:COG3206 322 LEALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVAREL---YESLLQRLE-----------EARLAEAL 383
|
....*....
gi 67189167 1896 NLAKFRKIQ 1904
Cdd:COG3206 384 TVGNVRVID 392
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1053-1866 |
2.50e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1053 ERAKRKLEGDLKLAQE--STMDIENDKQQLDEKLKKKEFEMSNLQSKIEDE-QAL---------GMQLQKKIKELQARIE 1120
Cdd:COG3096 278 NERRELSERALELRRElfGARRQLAEEQYRLVEMARELEELSARESDLEQDyQAAsdhlnlvqtALRQQEKIERYQEDLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1121 ELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGG--ATSAQ-IEMNKKREAEFQKMRRDLEEATLQHEA---TAA 1194
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSqlADYQQaLDVQQTRAIQYQQAVQALEKARALCGLpdlTPE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1195 ALRKKHADSVAELGEQIDNLQRVKQKL--------EKEKS-ELKMEIDDLASNMETVSKAKgnlEKMCR----------- 1254
Cdd:COG3096 438 NAEDYLAAFRAKEQQATEEVLELEQKLsvadaarrQFEKAyELVCKIAGEVERSQAWQTAR---ELLRRyrsqqalaqrl 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1255 -TLEDQLSEVKTKEEEQQ---RLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEE----- 1325
Cdd:COG3096 515 qQLRAQLAELEQRLRQQQnaeRLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQlrari 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1326 -ESKAKNALAHALQSARHDcdlLREQYEEEQEAKAELQRAMSK-ANSEVAQWRTKYEtdAIQRTEELEEAKKKLAQ---- 1399
Cdd:COG3096 595 kELAARAPAWLAAQDALER---LREQSGEALADSQEVTAAMQQlLEREREATVERDE--LAARKQALESQIERLSQpgga 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1400 ---RLQDAEEHVEAV----------------------NSKCA----SLEKTKQRLQNeVEDLMIDV-------------- 1436
Cdd:COG3096 670 edpRLLALAERLGGVllseiyddvtledapyfsalygPARHAivvpDLSAVKEQLAG-LEDCPEDLyliegdpdsfddsv 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1437 ----ERSNAACAALDKKQRNFDKV-------LAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYeESLDQLETLKRE 1505
Cdd:COG3096 749 fdaeELEDAVVVKLSDRQWRYSRFpevplfgRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLH-QAFSQFVGGHLA 827
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1506 ---NKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEE-----AEASLEHEEGKILRIQlelnQVKSEID 1577
Cdd:COG3096 828 vafAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLlnkllPQANLLADETLADRLE----ELREELD 903
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1578 rkIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSrNDALRIkkkmegDLNEMEIQLNHAnRQAAEAIrnlrnTQGMLKDT 1657
Cdd:COG3096 904 --AAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQ-FEQLQA------DYLQAKEQQRRL-KQQIFAL-----SEVVQRRP 968
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1658 QLHLDDAlrgQDDLKEQLAMVERranlmqaeieeLRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKK-KLET 1736
Cdd:COG3096 969 HFSYEDA---VGLLGENSDLNEK-----------LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDaKQQT 1034
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1737 dISQIQGEMEDI-VQEARNAEEKAKkaitdaammaeELKKEQDTSAHLERMKKNmeQTVKDLQHRLDEAEQLAlkggkKQ 1815
Cdd:COG3096 1035 -LQELEQELEELgVQADAEAEERAR-----------IRRDELHEELSQNRSRRS--QLEKQLTRCEAEMDSLQ-----KR 1095
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 1816 IQKLEARVRELENEVENeQKRNIEAVKGLRKH---ERRV--KELTYQTEEDRKNVL 1866
Cdd:COG3096 1096 LRKAERDYKQEREQVVQ-AKAGWCAVLRLARDndvERRLhrRELAYLSADELRSMS 1150
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
843-1070 |
2.98e-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: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 843 LLKSAETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAK 922
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 923 IKELTERAEDEEEINAELTAKKRKLEDEcSELK-----KDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLT 997
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQ-PPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67189167 998 KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQEST 1070
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1457-1913 |
3.08e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1457 LAEWKQKYEETQAELEASQKESRSLSTELfkvknAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQ 1536
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1537 IDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQstlDAEIRSRNDAL 1616
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE---AAALEERLKEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1617 RIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASL 1696
Cdd:COG4717 249 RLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1697 eqtERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLEtdISQIQGEMEDIVQEARNAEEKakkaitDAAMMAEELKKE 1776
Cdd:COG4717 329 ---GLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEE------ELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1777 QDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALkggKKQIQKLEARVRELENEVENEQKRnieavkgLRKHERRVKELty 1856
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEEL---EEELEELEEELEELEEELEELREE-------LAELEAELEQL-- 465
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 67189167 1857 qtEEDrknvlrlqDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEER 1913
Cdd:COG4717 466 --EED--------GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
984-1758 |
3.56e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.73 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 984 EEMAGLDENIAKLTKEKKALQEAHQQTLDDLQAEED---KVNTLTKAKTKLEQQVDDLEgsleqekklrmDLERAKRKLE 1060
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlnLVQTALRQQEKIERYQEDLE-----------ELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1061 GDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQarieeleeeieaerasRAKAEKQR 1140
Cdd:COG3096 368 EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALE----------------KARALCGL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1141 SDLSreLEEISERLEEAGGATSAQIEmnKKREAEfQKMRrDLEEATLQHEATAAALRK-------KHADSVA-ELGEQID 1212
Cdd:COG3096 432 PDLT--PENAEDYLAAFRAKEQQATE--EVLELE-QKLS-VADAARRQFEKAYELVCKiageverSQAWQTArELLRRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1213 NLQRVKQKLEkeksELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQrlinELSTQKARLHTESGEFS 1292
Cdd:COG3096 506 SQQALAQRLQ----QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA----ELEAQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1293 RQLdekdamvSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHalqsarhdcdlLREQYEEEQEAKAELQRAMSK-ANSE 1371
Cdd:COG3096 578 EQR-------SELRQQLEQLRARIKELAARAPAWLAAQDALER-----------LREQSGEALADSQEVTAAMQQlLERE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1372 VAQWRTKYEtdAIQRTEELEEAKKKLAQ-------RLQDAEEHVEAV----------------------NSKCA----SL 1418
Cdd:COG3096 640 REATVERDE--LAARKQALESQIERLSQpggaedpRLLALAERLGGVllseiyddvtledapyfsalygPARHAivvpDL 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1419 EKTKQRLQNeVEDLMIDV------------------ERSNAACAALDKKQRNFDKV-------LAEWKQKYEETQAELEA 1473
Cdd:COG3096 718 SAVKEQLAG-LEDCPEDLyliegdpdsfddsvfdaeELEDAVVVKLSDRQWRYSRFpevplfgRAAREKRLEELRAERDE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1474 SQKESRSLSTELFKVKNAYEeSLDQLETLKRE---NKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEE 1550
Cdd:COG3096 797 LAEQYAKASFDVQKLQRLHQ-AFSQFVGGHLAvafAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQL 875
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1551 -----AEASLEHEEGKILRIQlelnQVKSEIDrkIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSrNDALRIkkkmegD 1625
Cdd:COG3096 876 lnkllPQANLLADETLADRLE----ELREELD--AAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQ-FEQLQA------D 942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1626 LNEMEIQLNHAnRQAAEAIRNLR---------NTQGMLKDTQlHLDDALRGQ--------DDLKEQLAMVERRANLMQAE 1688
Cdd:COG3096 943 YLQAKEQQRRL-KQQIFALSEVVqrrphfsyeDAVGLLGENS-DLNEKLRARleqaeearREAREQLRQAQAQYSQYNQV 1020
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1689 IEELRASLEQTERSRRVAEQELLD------------ASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAE 1756
Cdd:COG3096 1021 LASLKSSRDAKQQTLQELEQELEElgvqadaeaeerARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAE 1100
|
..
gi 67189167 1757 EK 1758
Cdd:COG3096 1101 RD 1102
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1132-1334 |
5.41e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1132 SRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELGEQI 1211
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAA--------------QAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1212 DNLQrvkQKLEKEKSELKM----------------------EIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEE 1269
Cdd:COG3883 75 AEAE---AEIEERREELGEraralyrsggsvsyldvllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67189167 1270 QQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALA 1334
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1028-1553 |
5.74e-07 |
|
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: 54.75 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1028 KTKLEQQVDDLEGSLEQEKKLRMDLERA----KRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQA 1103
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKasalKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1104 LGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEIsERLEEaggatsaQIEMNKKREAEFQKMRRDLE 1183
Cdd:pfam05557 88 LNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSEL-EELQE-------RLDLLKAKASEAEQLRQNLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1184 EAtlQHEATAAALRKK--------HADSVAELGEQIDNLQRVKqKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRT 1255
Cdd:pfam05557 160 KQ--QSSLAEAEQRIKelefeiqsQEQDSEIVKNSKSELARIP-ELEKELERLREHNKHLNENIENKLLLKEEVEDLKRK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1256 L---EDQLSEVKTKEEEQQRLINELSTQKaRLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNA 1332
Cdd:pfam05557 237 LereEKYREEAATLELEKEKLEQELQSWV-KLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1333 LAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWR------------TKYETDAIQRTEELEEakkkLAQR 1400
Cdd:pfam05557 316 LEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRailesydkeltmSNYSPQLLERIEEAED----MTQK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1401 LQDAEEHVEAVNSKcASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVlaewKQKYEETQAELEASQKESRS 1480
Cdd:pfam05557 392 MQAHNEEMEAQLSV-AEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSL----RRKLETLELERQRLREQKNE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1481 LSTEL-------------FKV--------KNAYEESLDQLETLKRENKNLQQEISDLtEQIAEGGKHIHelEKIKKQIDQ 1539
Cdd:pfam05557 467 LEMELerrclqgdydpkkTKVlhlsmnpaAEAYQQRKNQLEKLQAEIERLKRLLKKL-EDDLEQVLRLP--ETTSTMNFK 543
|
570
....*....|....
gi 67189167 1540 EKSELQASLEEAEA 1553
Cdd:pfam05557 544 EVLDLRKELESAEL 557
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1385-1831 |
5.86e-07 |
|
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: 54.31 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1385 QRTEELE-------EAKKKLAQ---RLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFD 1454
Cdd:pfam05622 14 QRCHELDqqvsllqEEKNSLQQenkKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1455 KVLAEWKQKYEEtqaeLEASQKESRSLSTELFKVKNA-------------YEESLDQLETLKRENKNLQQEISDLTEQIA 1521
Cdd:pfam05622 94 KEVLELQHRNEE----LTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAEYMQRTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1522 EGGKHIHELEKIKKQIDQEKSELQasleEAEASLEHEEGKILRIQLELNQ-------VKSEIDRKIAEKD---EEIDQLK 1591
Cdd:pfam05622 170 QLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKleekleaLQKEKERLIIERDtlrETNEELR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1592 RNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEaiRNLRNTQGMLKDTQLHLDDALRGQDDL 1671
Cdd:pfam05622 246 CAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRL--GQEGSYRERLTELQQLLEDANRRKNEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1672 KEQLAMVERRANLMQAEIEELRASLeqtersrrvaeqelldaservQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQE 1751
Cdd:pfam05622 324 ETQNRLANQRILELQQQVEELQKAL---------------------QEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1752 ARNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---TVKDLQHRLDEAEQLALKGGKKQIQKLEARV 1823
Cdd:pfam05622 383 KEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPASPPEIQALKNQLLEKDKKI 462
|
....*...
gi 67189167 1824 RELENEVE 1831
Cdd:pfam05622 463 EHLERDFE 470
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1454-1643 |
5.90e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1454 DKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEG----GKH--- 1526
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreelGERara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1527 -----------------------IHELEKIKKQIDQEKSEL------QASLEEAEASLEHEEGKILRIQLELNQVKSEID 1577
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdfLDRLSALSKIADADADLLeelkadKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 1578 RKIAEKDEEIDQLKRNhLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEA 1643
Cdd:COG3883 175 AQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
857-1176 |
6.29e-07 |
|
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: 54.74 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 857 KEDFEKAKEDLAKSEAKRKELEEKMVAlMQEKNDLQLQVQAEADGLADAEERCDQliktKIQLEAKIKELtERAEdEEEI 936
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKA-RQAEMDRQAAIYAEQERMAMERERELE----RIRQEERKREL-ERIR-QEEI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 937 NAELTaKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDeniaKLTKEKKALQEAHQQTLDDLQA 1016
Cdd:pfam17380 371 AMEIS-RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME----QIRAEQEEARQREVRRLEEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1017 EEdkVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRklegDLKLAQESTMDI------ENDKQQLDEKLKKK--E 1088
Cdd:pfam17380 446 RE--MERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKR----DRKRAEEQRRKIlekeleERKQAMIEEERKRKllE 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1089 FEMSNLQSKIEDEQalgmqlQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLsreleEISERLEEaggaTSAQIEMN 1168
Cdd:pfam17380 520 KEMEERQKAIYEEE------RRREAEEERRKQQEMEERRRIQEQMRKATEERSRL-----EAMERERE----MMRQIVES 584
|
....*...
gi 67189167 1169 KKREAEFQ 1176
Cdd:pfam17380 585 EKARAEYE 592
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1005-1189 |
7.04e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.23 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1005 EAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRM-------DLERAKRKLEGDLKLAQEstmDIENDK 1077
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEaakteleDLEKEIKRLELEIEEVEA---RIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1078 QQLDEKLKKKEFEmsNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIeaerasrAKAEKQRSDLSRELEEISERLEEA 1157
Cdd:COG1579 80 EQLGNVRNNKEYE--ALQKEIESLKRRISDLEDEILELMERIEELEEEL-------AELEAELAELEAELEEKKAELDEE 150
|
170 180 190
....*....|....*....|....*....|..
gi 67189167 1158 GGATSAQIEmnkKREAEFQKMRRDLEEATLQH 1189
Cdd:COG1579 151 LAELEAELE---ELEAEREELAAKIPPELLAL 179
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
866-1021 |
8.23e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.23 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 866 DLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIKELTER-AEDEEEINAELTAKK 944
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARiKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67189167 945 RK-LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQAEEDKV 1021
Cdd:COG1579 91 YEaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1731-1894 |
9.61e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.63 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1731 KKKLETDISQIQGEMEDIVQEARN-AEEKAKKAITDAAMMAEELKKEQDTSAHLERMK-KNMEQTVKDLQHRLDEAEQLa 1808
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKeAEAIKKEALLEAKEEIHKLRNEFEKELRERRNElQKLEKRLLQKEENLDRKLEL- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1809 LKGGKKQIQKLEARVRELENEVENEQKrniEAVKGLRKHERRVKELTYQTEEDRKNVLrLQDLVDKLQTKVKAYKRQAE- 1887
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEE---ELEELIEEQLQELERISGLTAEEAKEIL-LEKVEEEARHEAAVLIKEIEe 180
|
....*..
gi 67189167 1888 EAEEQSN 1894
Cdd:PRK12704 181 EAKEEAD 187
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1448-1935 |
9.65e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.87 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1448 KKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHI 1527
Cdd:TIGR04523 54 KELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1528 HELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDrkiaEKDEEIDQLKRNHLRVvESMQSTLDA 1607
Cdd:TIGR04523 134 KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKL----NIQKNIDKIKNKLLKL-ELLLSNLKK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1608 EIRSrndalriKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQA 1687
Cdd:TIGR04523 209 KIQK-------NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1688 EIEELRASLEQTErsrrvAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQgEMEDIVQEARNAEEKAKKAITDAA 1767
Cdd:TIGR04523 282 KIKELEKQLNQLK-----SEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIS-QNNKIISQLNEQISQLKKELTNSE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1768 MMAEELKKEqdtsahLERMKKNMEQTVKDLQHRLDEAEQLalkggKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKH 1847
Cdd:TIGR04523 356 SENSEKQRE------LEEKQNEIEKLKKENQSYKQEIKNL-----ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1848 ERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVK 1927
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
....*...
gi 67189167 1928 SREVHTKV 1935
Cdd:TIGR04523 505 KKELEEKV 512
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
801-1277 |
1.06e-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: 53.90 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 801 MRVEFKKMMERRESIFCIQYNVRAFMNVKHWPWMKLYFKIKPLLKSAETEKEMANMKEDFEKAKEDLAKSEAKrKELEEK 880
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGA-TAVYSQ 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 881 MVALMQEKNDLQLQVqaeadgladaeerCDQLIKTKIQLEAKIKELTERAEDEEEINAELTAKKRKLEDECSELKKDIDD 960
Cdd:TIGR00606 668 FITQLTDENQSCCPV-------------CQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPG 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 961 LELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKAL---QEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDD 1037
Cdd:TIGR00606 735 RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpeEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1038 LEG-----SLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKI 1112
Cdd:TIGR00606 815 LQGsdldrTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS 894
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1113 KELQARIEELEEEIEAErasrAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATlqhEAT 1192
Cdd:TIGR00606 895 TEVQSLIREIKDAKEQD----SPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKI---QDG 967
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1193 AAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDdlaSNMETVSKAKGNLEKMCRtlEDQLSEVKTKEEEQQR 1272
Cdd:TIGR00606 968 KDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDID---TQKIQERWLQDNLTLRKR--ENELKEVEEELKQHLK 1042
|
....*
gi 67189167 1273 LINEL 1277
Cdd:TIGR00606 1043 EMGQM 1047
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1329-1472 |
1.14e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.63 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1329 AKNALAHALQSARHDCDLLREqyEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqdaeehV 1408
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK-------E 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67189167 1409 EAVNSKCASLEKTKQRLQNEVEDlmidversnaacaaLDKKQRNFDKVLAEWKQKYEETQAELE 1472
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKE--------------LEQKQQELEKKEEELEELIEEQLQELE 145
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1137-1431 |
1.34e-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: 53.59 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1137 EKQRSDLSRELEEISERLEEAggatsaQIEMNKKREAEFQKMRRDLEEATLQHEAT---AAALRKKHADSVAELGEQIDN 1213
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQE------RLRQEKEEKAREVERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1214 LQRVKQKLEKEK---SELKMEIDDLaSNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESG- 1289
Cdd:pfam17380 353 IRQEERKRELERirqEEIAMEISRM-RELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEe 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1290 ----EFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAE----- 1360
Cdd:pfam17380 432 arqrEVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQamiee 511
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67189167 1361 ------LQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHveavNSKCASLEKTKQRLQNEVED 1431
Cdd:pfam17380 512 erkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE----RSRLEAMEREREMMRQIVES 584
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1457-1938 |
1.49e-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: 53.57 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1457 LAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQ 1536
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1537 IDQEKSELQASLEEAEASLEHeegkiLRIQLElnQVKSEIDRKIAEKDEEIDQLKRNHLRVV---ESMQSTLDAEIRSRN 1613
Cdd:pfam05483 181 TRQVYMDLNNNIEKMILAFEE-----LRVQAE--NARLEMHFKLKEDHEKIQHLEEEYKKEIndkEKQVSLLLIQITEKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1614 DALR----IKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEI 1689
Cdd:pfam05483 254 NKMKdltfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1690 EELRASLEQTERSRRVAEQELLDASERVQ-LLHTQNTSLINTKKKLETDISQIQ---GEMEDIVQEARNAE---EKAKKA 1762
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFEATTCSLEeLLRTEQQRLEKNEDQLKIITMELQkksSELEEMTKFKNNKEvelEELKKI 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1763 ITDAAMMAEELKKEQDTSahlERMKKNMEQTVKDLQHRLDEAEQLALK--GGKKQIQKLEARVRELENEVENEQKRNIE- 1839
Cdd:pfam05483 414 LAEDEKLLDEKKQFEKIA---EELKGKEQELIFLLQAREKEIHDLEIQltAIKTSEEHYLKEVEDLKTELEKEKLKNIEl 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1840 --------------------AVKGLRKHERRVKELTYQTEEDRKNVLRLQD----LVDKLQTKVKAYKRQAEEAEEQSNV 1895
Cdd:pfam05483 491 tahcdklllenkeltqeasdMTLELKKHQEDIINCKKQEERMLKQIENLEEkemnLRDELESVREEFIQKGDEVKCKLDK 570
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 67189167 1896 NLAKFRKIQHELEEAEERADIAESQVNKLRvKSREVHTKVISE 1938
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLK-KQIENKNKNIEE 612
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
914-1245 |
1.66e-06 |
|
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: 53.22 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 914 KTKIQLEAKIKELTERAEDEEEINAELTAKKRKLEDECSELKKDIDD-LELTLAKVEK----EKHATENKVKNLTEEMAG 988
Cdd:pfam09731 86 KKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEvLKEAISKAESatavAKEAKDDAIQAVKAHTDS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 989 LDENIAklTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDL-EGSLEQEKKLRMDLERAKRKLEGDLKLAQ 1067
Cdd:pfam09731 166 LKEASD--TAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLlDAAPETPPKLPEHLDNVEEKVEKAQSLAK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1068 ---ESTMDIENDKQQLDEKLKKKE------------FEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEaeras 1132
Cdd:pfam09731 244 lvdQYKELVASERIVFQQELVSIFpdiipvlkednlLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERAL----- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1133 rakaEKQRSDLSRELEEISERLEEAGGATSAQIEmnKKREAEFQKMRRDLEE---ATLQHEATAAALRKKHADSVAELGE 1209
Cdd:pfam09731 319 ----EKQKEELDKLAEELSARLEEVRAADEAQLR--LEFEREREEIRESYEEklrTELERQAEAHEEHLKDVLVEQEIEL 392
|
330 340 350
....*....|....*....|....*....|....*.
gi 67189167 1210 QIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKA 1245
Cdd:pfam09731 393 QREFLQDIKEKVEEERAGRLLKLNELLANLKGLEKA 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1626-1939 |
1.75e-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: 53.52 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1626 LNEMEIQLNHANRQAAEAIRNLrntqgmlkdtqlhlddalrgqdDLKEQLAMVERRanLMQAEIEELRASLEQTERSRRV 1705
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYK----------------------ELKAELRELELA--LLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1706 AEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAitdaammAEELKKEQDTSAHLEr 1785
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL-------RERLANLERQLEELE- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1786 mkknmEQTVKDLQHRLDEAEQLAlkggkkqiqKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNV 1865
Cdd:TIGR02168 323 -----AQLEELESKLDELAEELA---------ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67189167 1866 LrlqdlvdklqtkvkaykrqaeEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 1939
Cdd:TIGR02168 389 A---------------------QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1493-1691 |
2.47e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.55 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1493 EESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKikkqidqEKSELQASLEEAEASLEHEEGKILRIQLELNQv 1572
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-------EVEELEAELEEKDERIERLERELSEARSEERR- 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1573 KSEIDRKIAEKDEEIDQLKRNhLRVVESMQSTLDAEIRsrndalRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQG 1652
Cdd:COG2433 460 EIRKDREISRLDREIERLERE-LEEERERIEELKRKLE------RLKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYG 532
|
170 180 190
....*....|....*....|....*....|....*....
gi 67189167 1653 MLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEE 1691
Cdd:COG2433 533 LKEGDVVYLRDASGAGRSTAELLAEAGPRAVIVPGELSE 571
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
839-1276 |
2.62e-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: 52.81 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 839 KIKPLLKSAETEKEM-ANMKEDFEKAKEDLAKSEAKRKEL----EEKMVAL---------MQEKNDLQLQ----VQAEAD 900
Cdd:pfam15921 462 KVSSLTAQLESTKEMlRKVVEELTAKKMTLESSERTVSDLtaslQEKERAIeatnaeitkLRSRVDLKLQelqhLKNEGD 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 901 GLADAEERCDQLiktKIQLEAK---IKELTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATEN 977
Cdd:pfam15921 542 HLRNVQTECEAL---KLQMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 978 KVKNLTEEMAGLDENIAKLTKEKKALQEAhqqtLDDLQAEEDKV-NTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAK 1056
Cdd:pfam15921 619 KIRELEARVSDLELEKVKLVNAGSERLRA----VKDIKQERDQLlNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1057 RKLEGDLKLAQEstmDIENDKQQLdeklkkKEFEMSNLQSKiedEQALGMQLQ-----KKIKELQARIEELEEEIEAERA 1131
Cdd:pfam15921 695 NKLKMQLKSAQS---ELEQTRNTL------KSMEGSDGHAM---KVAMGMQKQitakrGQIDALQSKIQFLEEAMTNANK 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1132 SRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQ----------HEATAAALRKKHA 1201
Cdd:pfam15921 763 EKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQfaecqdiiqrQEQESVRLKLQHT 842
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 1202 DSVAEL-GEQIDNLQRVKQKLEKEKSELKMEiDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINE 1276
Cdd:pfam15921 843 LDVKELqGPGYTSNSSMKPRLLQPASFTRTH-SNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINE 917
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
848-1334 |
2.83e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 848 ETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQlqvQAEADGLADAEERCDQLIKTKIQLEAKIK--- 924
Cdd:PRK01156 239 SALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHM---KIINDPVYKNRNYINDYFKYKNDIENKKQils 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 925 ----------ELTERAEDEEEINAELTAKKRKLED---ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDE 991
Cdd:PRK01156 316 nidaeinkyhAIIKKLSVLQKDYNDYIKKKSRYDDlnnQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 992 NIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEqekklrMDLERAKRKLEGDlKLAQESTM 1071
Cdd:PRK01156 396 ILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNME------MLNGQSVCPVCGT-TLGEEKSN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1072 DI----ENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQK-----------KIKELQARIEELEEEIEAERASRAKA 1136
Cdd:PRK01156 469 HIinhyNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeeinksineynKIESARADLEDIKIKINELKDKHDKY 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1137 EKQRSDL-SRELEEISERLEEAGGATSA----QIEMNKKREAEFQKMRRDLEEATlqheataaalrkkhadsvaelGEQI 1211
Cdd:PRK01156 549 EEIKNRYkSLKLEDLDSKRTSWLNALAVisliDIETNRSRSNEIKKQLNDLESRL---------------------QEIE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1212 DNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLiNELSTQKARLHTESGEF 1291
Cdd:PRK01156 608 IGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDL-KEITSRINDIEDNLKKS 686
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 67189167 1292 SRQLD-------EKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALA 1334
Cdd:PRK01156 687 RKALDdakanraRLESTIEILRTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
989-1197 |
2.83e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 989 LDENIAKLtkeKKALQEAhQQTLDDLQAEEDKVNTLTKAKTkLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQE 1068
Cdd:COG3206 180 LEEQLPEL---RKELEEA-EAALEEFRQKNGLVDLSEEAKL-LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1069 STMDIENDK--QQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERAS-RAKAEKQRSDLSR 1145
Cdd:COG3206 255 ALPELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAeLEALQAREASLQA 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 67189167 1146 ELEEISERLEEAGgatsaqiemnkKREAEFQKMRRDLEEATLQHEATAAALR 1197
Cdd:COG3206 335 QLAQLEARLAELP-----------ELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1090-1332 |
3.04e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1090 EMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEaggatsaqiemnk 1169
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1170 kREAEFQKMRRDLEEATLQHEATAAALrkkHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNL 1249
Cdd:COG3883 84 -RREELGERARALYRSGGSVSYLDVLL---GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1250 EKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKA 1329
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
...
gi 67189167 1330 KNA 1332
Cdd:COG3883 240 AAA 242
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
655-679 |
3.41e-06 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 49.27 E-value: 3.41e-06
10 20
....*....|....*....|....*
gi 67189167 655 FRENLNKLMTNLKSTHPHFVRCLIP 679
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1457-1591 |
3.52e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1457 LAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLK--RENKNLQQEISDLTEQIAEggkhiheLEKIK 1534
Cdd:COG1579 40 LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQKEIESLKRRISD-------LEDEI 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 67189167 1535 KQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLK 1591
Cdd:COG1579 113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1485-1931 |
3.57e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 51.78 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1485 LFKVKNAYEEsLDQLETLKRE--NKNLQQEISDLtEQIAEGGKHIHELEKIKKQ----IDQEKSELQASLEEAEASLEhe 1558
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1559 EGKILRIQLELNQVKS---EIDRKIAEKDEEIDQL----KRNHLRV--VESMQSTLDAEIRSRNDAL-RIKKKMEGDLNE 1628
Cdd:pfam06160 78 KYRFKKAKKALDEIEElldDIEEDIKQILEELDELleseEKNREEVeeLKDKYRELRKTLLANRFSYgPAIDELEKQLAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1629 MEIQLNHANRqaaeairnlRNTQGMLKDTQLHLDDALRGQDDLKEQL----AMVERRANLMQAEIEELRASLEQTERSRR 1704
Cdd:pfam06160 158 IEEEFSQFEE---------LTESGDYLEAREVLEKLEEETDALEELMedipPLYEELKTELPDQLEELKEGYREMEEEGY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1705 VAEQelLDASERVQLLHTQNTSLINTKKKLETD-----ISQIQGEMEDIvQEARNAEEKAKKaitdaammaeELKKEQDT 1779
Cdd:pfam06160 229 ALEH--LNVDKEIQQLEEQLEENLALLENLELDeaeeaLEEIEERIDQL-YDLLEKEVDAKK----------YVEKNLPE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1780 -SAHLERMKKNMEQTVKDLQH-----RLDEAEQLALKGGKKQIQKLEARVRELENEVENEQKRNI-------EAVKGLRK 1846
Cdd:pfam06160 296 iEDYLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSelqeeleEILEQLEE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1847 HERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAE----------------EAEEQSNVNLAKFRKIQHELEEA 1910
Cdd:pfam06160 376 IEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEksnlpglpesyldyffDVSDEIEDLADELNEVPLNMDEV 455
|
490 500
....*....|....*....|.
gi 67189167 1911 EERADIAESQVNKLRVKSREV 1931
Cdd:pfam06160 456 NRLLDEAQDDVDTLYEKTEEL 476
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1444-1880 |
3.90e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1444 AALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLtEQIAEG 1523
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1524 GKHIHELEKIKKQIDQEKSELQAsLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQS 1603
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1604 TLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQ-----------AAEAIRNLRNTQGMLKDTQLHLDDAL------- 1665
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearllllIAAALLALLGLGGSLLSLILTIAGVLflvlgll 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1666 --------RGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETD 1737
Cdd:COG4717 287 allflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1738 ISQIQ-------------GEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmKKNMEQTVKDLQHRLDEA 1804
Cdd:COG4717 367 ELEQEiaallaeagvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD--EEELEEELEELEEELEEL 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 1805 EQlALKGGKKQIQKLEARVRELENEVENEQKRnieavkglRKHERRVKELTYQTEEDRKNVLrLQDLVDKLQTKVK 1880
Cdd:COG4717 445 EE-ELEELREELAELEAELEQLEEDGELAELL--------QELEELKAELRELAEEWAALKL-ALELLEEAREEYR 510
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1206-1531 |
4.50e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1206 ELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLH 1285
Cdd:pfam07888 42 ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1286 TESGEFS---RQLDEKDAMVSQLSRGKQA----FTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAK 1358
Cdd:pfam07888 122 AQRAAHEariRELEEDIKTLTQRVLERETelerMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1359 AELQRAMSKANSEVAQWRTKYETdAIQRTEELEEAKKKLA---QRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMID 1435
Cdd:pfam07888 202 AQRDTQVLQLQDTITTLTQKLTT-AHRKEAENEALLEELRslqERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1436 VERSNAACAALDKKQRNFDkvlAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEE------------------SLD 1497
Cdd:pfam07888 281 AAQLTLQLADASLALREGR---ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEermereklevelgrekdcNRV 357
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 67189167 1498 QLETLKRENKNL-------QQEISDLTEQIAEGGKHIHELE 1531
Cdd:pfam07888 358 QLSESRRELQELkaslrvaQKEKEQLQAEKQELLEYIRQLE 398
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1255-1411 |
4.68e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1255 TLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAK--NA 1332
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 1333 LAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAV 1411
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
938-1164 |
4.99e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 938 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQ-- 1015
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1016 -AEEDKVNTLTKAK--TKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlaqestmDIENDKQQLDEKLKKKEFEMS 1092
Cdd:COG3883 99 gGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKA-------ELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67189167 1093 NLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQ 1164
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1306-1595 |
5.30e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 52.00 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1306 SRGKQAFTQQIEELKRQLEEESKAKNalahalqsarhdcdLLREQYEEEQEAKAE--LQRAMSKANSEVAQWRTKYETDA 1383
Cdd:COG5022 805 LLGSRKEYRSYLACIIKLQKTIKREK--------------KLRETEEVEFSLKAEvlIQKFGRSLKAKKRFSLLKKETIY 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1384 IQRTEELEEAKKKLaQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVE-DLMIDVERSNAACAALDKKQRNFDKVLAEWKQ 1462
Cdd:COG5022 871 LQSAQRVELAERQL-QELKIDVKSISSLKLVNLELESEIIELKKSLSsDLIENLEFKTELIARLKKLLNNIDLEEGPSIE 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1463 KyeETQAELEASQKESRSLSTELFKVKNAYEESldqletlkrenknlqqeisdlTEQIAEGGKHIHELeKIKKQIDQEKS 1542
Cdd:COG5022 950 Y--VKLPELNKLHEVESKLKETSEEYEDLLKKS---------------------TILVREGNKANSEL-KNFKKELAELS 1005
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 67189167 1543 ELQASLEEAEASLEHEEGKILRIQLELNQVKSEidRKIAEKDEEIDQLKRNHL 1595
Cdd:COG5022 1006 KQYGALQESTKQLKELPVEVAELQSASKIISSE--STELSILKPLQKLKGLLL 1056
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
850-1913 |
6.95e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.59 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 850 EKEMANMKEDFEKAKEDLAKSEAKRKELeekmvalmqeKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIKELTER 929
Cdd:TIGR01612 764 EKELSNKINDYAKEKDELNKYKSKISEI----------KNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 930 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEkekhateNKVKN-LTEEMAGLDENiaKLTKEKKALQEahq 1008
Cdd:TIGR01612 834 INEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELT-------NKIKAeISDDKLNDYEK--KFNDSKSLINE--- 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1009 qTLDDLQAEEDKVNTLTKaktkLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKL--KK 1086
Cdd:TIGR01612 902 -INKSIEEEYQNINTLKK----VDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLidKI 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1087 KEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASraKAEKQRSDLSRELEE----------------- 1149
Cdd:TIGR01612 977 NELDKAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFD--EKEKATNDIEQKIEDanknipnieiaihtsiy 1054
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1150 -ISERLEEAGGATSAQIEMNKKREAE-----FQKMRRDLEEATLQHEATAAALR-----KKHADSVAELGEQIDN----L 1214
Cdd:TIGR01612 1055 nIIDEIEKEIGKNIELLNKEILEEAEinitnFNEIKEKLKHYNFDDFGKEENIKyadeiNKIKDDIKNLDQKIDHhikaL 1134
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1215 QRVKQKLEKEKSELKMEIDDLASNMETvSKAKGNLEKMCRTLEDQLSEVKTKE---EEQQRLINELStqkarlHTESGEF 1291
Cdd:TIGR01612 1135 EEIKKKSENYIDEIKAQINDLEDVADK-AISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIA------EIEKDKT 1207
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1292 SrqLDEKDAMvsQLSRGK---QAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQrAMSKA 1368
Cdd:TIGR01612 1208 S--LEEVKGI--NLSYGKnlgKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEME-TFNIS 1282
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1369 NSEvaqwRTKYETDAIQRTEELEEAKKKLAQRLQDaeehveavNSKCASLEKTKQRLQNEVEDlmidversnaacaaldk 1448
Cdd:TIGR01612 1283 HDD----DKDHHIISKKHDENISDIREKSLKIIED--------FSEESDINDIKKELQKNLLD----------------- 1333
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1449 kqrnfdkvlaewkqkyeetqaeleaSQKESRSLSTELFKVKNAYEesldqleTLKREN-KNLQQEISDLTEQIAEGGKHI 1527
Cdd:TIGR01612 1334 -------------------------AQKHNSDINLYLNEIANIYN-------ILKLNKiKKIIDEVKEYTKEIEENNKNI 1381
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1528 H-ELEKIKKQIdqekselqasleeaeasleheegKILRIQLELNQVKSEIDRKIAEKDeeIDQLKRNhlrVVESMQSTLD 1606
Cdd:TIGR01612 1382 KdELDKSEKLI-----------------------KKIKDDINLEECKSKIESTLDDKD--IDECIKK---IKELKNHILS 1433
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1607 AEirsRNDALRIKKKMEGDLNemeIQLNHANRQAAEairnlRNTQGMLKDTQlhlDDALRGQDDLKEQLAMVERRANLMQ 1686
Cdd:TIGR01612 1434 EE---SNIDTYFKNADENNEN---VLLLFKNIEMAD-----NKSQHILKIKK---DNATNDHDFNINELKEHIDKSKGCK 1499
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1687 AEIEElraSLEQTERSRRVAEQ------ELLDASERVQLlhtqNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAK 1760
Cdd:TIGR01612 1500 DEADK---NAKAIEKNKELFEQykkdvtELLNKYSALAI----KNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIK 1572
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1761 KAITDAAMMAEELKKEQDTSahleRMKKNMEQTVKDLQHRLDEAEQLALKGGK--KQIQKLEARVRELE-NEVENEQKRN 1837
Cdd:TIGR01612 1573 EIKKEKFRIEDDAAKNDKSN----KAAIDIQLSLENFENKFLKISDIKKKINDclKETESIEKKISSFSiDSQDTELKEN 1648
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1838 IEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQ-----AEEAEEQSNVNLAKFRKIQHELEEAEE 1912
Cdd:TIGR01612 1649 GDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNyeigiIEKIKEIAIANKEEIESIKELIEPTIE 1728
|
.
gi 67189167 1913 R 1913
Cdd:TIGR01612 1729 N 1729
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1306-1582 |
7.35e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 50.30 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1306 SRGKQAFTQQIEELKRQLEEESKAKnalahalqsarhdcdllreqyeeeqeAKAELQRamSKANSEVAQWRTKYETDAIQ 1385
Cdd:pfam00038 46 SRLYSLYEKEIEDLRRQLDTLTVER--------------------------ARLQLEL--DNLRLAAEDFRQKYEDELNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1386 RTeELEEAKKKLAQRLQDA-------EEHVEAVNSKCASLEKTKQR----LQNEVEDLMIDVERSNAACAALdkkqrnfD 1454
Cdd:pfam00038 98 RT-SAENDLVGLRKDLDEAtlarvdlEAKIESLKEELAFLKKNHEEevreLQAQVSDTQVNVEMDAARKLDL-------T 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1455 KVLAEWKQKYEEtQAELeasqkeSRSLSTELFKVKnaYEESLDQLETLKRENKNLQQEISDLTEQIAEggkHIHELEKIK 1534
Cdd:pfam00038 170 SALAEIRAQYEE-IAAK------NREEAEEWYQSK--LEELQQAAARNGDALRSAKEEITELRRTIQS---LEIELQSLK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 67189167 1535 KQidqeKSELQASLEEAEASLEHE----EGKILRIQLELNQVKSEIDRKIAE 1582
Cdd:pfam00038 238 KQ----KASLERQLAETEERYELQladyQELISELEAELQETRQEMARQLRE 285
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1236-1546 |
8.97e-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: 8.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1236 ASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINelstqKARLHTESGEFSRQL-DEKDAMVSQLSRGKQAFTQ 1314
Cdd:COG3096 271 ADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVE-----MARELEELSARESDLeQDYQAASDHLNLVQTALRQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1315 Q---------IEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMskansEVAQWRTKYETDAIQ 1385
Cdd:COG3096 346 QekieryqedLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQAL-----DVQQTRAIQYQQAVQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1386 RTEELEE-------AKKKLAQRLQDAEEHVEAVNSKCASLEktkQRL--------QNE-----VEDLMIDVERSNAACAA 1445
Cdd:COG3096 421 ALEKARAlcglpdlTPENAEDYLAAFRAKEQQATEEVLELE---QKLsvadaarrQFEkayelVCKIAGEVERSQAWQTA 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1446 --LDKKQRNFdKVLAEWKQKYEETQAELE---ASQKESRSLSTELFKVKNAYEESLDQLETLKREnknLQQEISDLTEQI 1520
Cdd:COG3096 498 reLLRRYRSQ-QALAQRLQQLRAQLAELEqrlRQQQNAERLLEEFCQRIGQQLDAAEELEELLAE---LEAQLEELEEQA 573
|
330 340
....*....|....*....|....*.
gi 67189167 1521 AEGGKHIHELEKIKKQIDQEKSELQA 1546
Cdd:COG3096 574 AEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1385-1914 |
1.05e-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: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1385 QRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKY 1464
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1465 EETQAELEaSQKESRSLSTELFKVKNAYEEsldqLETLKRENKNLQQEIsDLTEQIAEGGKHIHELEKIKKQIDQEKSEL 1544
Cdd:TIGR00618 243 AYLTQKRE-AQEEQLKKQQLLKQLRARIEE----LRAQEAVLEETQERI-NRARKAAPLAAHIKAVTQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1545 QASLEEAEASLEHEEgkilriqlelNQVKSEIDRKIAEKDEEIDQLKRNHLRVvESMQSTLDAEIRSRNDALRIKKKMEG 1624
Cdd:TIGR00618 317 QSKMRSRAKLLMKRA----------AHVKQQSSIEEQRRLLQTLHSQEIHIRD-AHEVATSIREISCQQHTLTQHIHTLQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1625 DLNEMEIQLNHANRQAAEAIRNLRNTQgmlkDTQLHLDDALRGQ-DDLKEQLAMVERRANLMQAEIEELRASLEQTERSR 1703
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKELDILQREQATI----DTRTSAFRDLQGQlAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1704 RVAEQELldaSERVQLLHTQNTSLintkkKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHL 1783
Cdd:TIGR00618 462 QESAQSL---KEREQQLQTKEQIH-----LQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRG 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1784 ERMKKNMEQTVKDLQHRLDEAeqlalkggKKQIQKLEARVRELENEveneqkrnieavkgLRKHERRVKELTYQTEEDRK 1863
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQLTSE--------RKQRASLKEQMQEIQQS--------------FSILTQCDNRSKEDIPNLQN 591
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 67189167 1864 NVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERA 1914
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA 642
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1133-1372 |
1.06e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1133 RAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAEFQKMRR-----DLEEATLQHEATAAALRKKHADSVAEL 1207
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEA--------------EAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1208 GEQIDNLQRVKQKLEKEKSELKMEIDDlasnmETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTE 1287
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1288 SGefsRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAhALQsarHDCDLLREQYEE--EQEAKAELQRAM 1365
Cdd:COG3206 311 AQ---RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR-RLE---REVEVARELYESllQRLEEARLAEAL 383
|
....*..
gi 67189167 1366 SKANSEV 1372
Cdd:COG3206 384 TVGNVRV 390
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
845-1088 |
1.17e-05 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 50.54 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 845 KSAETEKEMANMKEdFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEErCDQLIKTKIQLEAKIK 924
Cdd:pfam18971 598 KAVAEAKSTGNYDE-VKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDE-IFALINKEANRDARAI 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 925 ELTEraedeeeinaELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAkLTKEKKALQ 1004
Cdd:pfam18971 676 AYTQ----------NLKGIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLG-INPEWISKV 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1005 EAHQQTLDDLQAEEDK-VNTLTKAKTKLEQQVDDLEGSLEQEKKL-RMDLERAKRKLEGDLKLAQESTMDIEN-DKQQLD 1081
Cdd:pfam18971 745 ENLNAALNEFKNGKNKdFSKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfSKEQLA 824
|
....*..
gi 67189167 1082 EKLKKKE 1088
Cdd:pfam18971 825 QQAQKNE 831
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1538-1924 |
1.33e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1538 DQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSeidrkiAEKDEEID-QLKRNHLRVVesmqstldaeirsrNDAL 1616
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLVEMARELAELNE------AESDLEQDyQAASDHLNLV--------------QTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1617 RIKKKME---GDLNEMEIQLNHANRQAAEAirnlrntQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELR 1693
Cdd:PRK04863 345 RQQEKIEryqADLEELEERLEEQNEVVEEA-------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1694 ASLEQTERSRR---VAEQELLDASERVQLLHTQNTSLINTKKKLETDISqiqgemedIVQEARNAEEKAKKAIT------ 1764
Cdd:PRK04863 418 QAVQALERAKQlcgLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLS--------VAQAAHSQFEQAYQLVRkiagev 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1765 ---DAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDE---AEQLALKGGKKQIQKL-------------EARVRE 1825
Cdd:PRK04863 490 srsEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQqqrAERLLAEFCKRLGKNLddedeleqlqeelEARLES 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1826 LENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEdrknVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQH 1905
Cdd:PRK04863 570 LSESVSEARERRMALRQQLEQLQARIQRLAARAPA----WLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTV 645
|
410
....*....|....*....
gi 67189167 1906 ELEEAEERADIAESQVNKL 1924
Cdd:PRK04863 646 ERDELAARKQALDEEIERL 664
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1502-1907 |
1.51e-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: 50.35 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1502 LKRENKNLQQEISDLTE-----QIAEGGKHIHELEKIKKQIDQEKSEL--------QASLEEAEASLEHEEGKILRIQLE 1568
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPldqytQLALMEFAKKKSLHGKAELLTLRSQLltlctpcmPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1569 LNQVKSEIDRKIaEKDEEIDQLKRNHLRVVESMQS--TLDAEIRSRNDALRIKKKMEGDLNEMEiQLNHANRQAAEAIRN 1646
Cdd:TIGR00618 238 TQQSHAYLTQKR-EAQEEQLKKQQLLKQLRARIEElrAQEAVLEETQERINRARKAAPLAAHIK-AVTQIEQQAQRIHTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1647 LRNTQGMLKDTQLHLDDALRGQDDLKEQlamvERRANLMQAEIEELRASLEQTERSRRVAEQELLDaSERVQLLHTQNTS 1726
Cdd:TIGR00618 316 LQSKMRSRAKLLMKRAAHVKQQSSIEEQ----RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL-TQHIHTLQQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1727 LINTKKKLETDISQIQGEMEDivQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVK-----DLQHRL 1801
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQAT--IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEkihlqESAQSL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1802 DEAEQLalKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKA 1881
Cdd:TIGR00618 469 KEREQQ--LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEED 546
|
410 420
....*....|....*....|....*.
gi 67189167 1882 YKRQAEEAEEQSNVNLAKFRKIQHEL 1907
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQSF 572
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
844-1072 |
1.58e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 844 LKSAETEKEMANMKEDFEKAKEDLAKSEAKRKE---------LEEKMVALMQEKNDLQLQ-VQAEADgLADAEERCDQLi 913
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQlAEARAE-LAEAEARLAAL- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 914 ktKIQLEAKIKELTERAEDEEEinaeltakkrkledecSELKKDIDDLELTLAkvEKEKHATEN--KVKNLTEEMAGLDE 991
Cdd:COG3206 246 --RAQLGSGPDALPELLQSPVI----------------QQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAALRA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 992 NIAKLTKEKKALQEAhqqtldDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTM 1071
Cdd:COG3206 306 QLQQEAQRILASLEA------ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
.
gi 67189167 1072 D 1072
Cdd:COG3206 380 A 380
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1465-1731 |
1.68e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.91 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1465 EETQAELEASQKeSRSLSTELFKVKNAYEESLDQL---ETLKRENKNLQQEISDLTEQIAEGGKhihELEKIKKQIDQEK 1541
Cdd:PRK11281 39 ADVQAQLDALNK-QKLLEAEDKLVQQDLEQTLALLdkiDRQKEETEQLKQQLAQAPAKLRQAQA---ELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1542 SE--LQASLEEAEASLEHEEGKILRIQLELNQVKSEIdrkiaekdeeIDQLKRNhlrvvESMQSTLDA------EIRSRN 1613
Cdd:PRK11281 115 REtlSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQL----------VSLQTQP-----ERAQAALYAnsqrlqQIRNLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1614 DALRIKKKmegDLNEMEIQLNHANRQAAEAiRNLRNTQGMLKDTQLHldDALRGQ-DDLKEQLAMVERRANLMQAEIEEL 1692
Cdd:PRK11281 180 KGGKVGGK---ALRPSQRVLLQAEQALLNA-QNDLQRKSLEGNTQLQ--DLLQKQrDYLTARIQRLEHQLQLLQEAINSK 253
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 67189167 1693 RasLEQTERSrrVAEQELLDASERVQ---LLHTQntSLINTK 1731
Cdd:PRK11281 254 R--LTLSEKT--VQEAQSQDEAARIQanpLVAQE--LEINLQ 289
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
893-1017 |
1.74e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 893 LQVQAEADGLADAEERCDQLIKTKIQLEAKIKELTERAEDEEEI---NAELTAKKRKLEDECSELKKDIDDLELTLAKVE 969
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELrerRNELQKLEKRLLQKEENLDRKLELLEKREEELE 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 67189167 970 KEKHATENKVKNLTEEMAGLD----------ENIAKLTKEkkalqEAHQQTLDDLQAE 1017
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEelieeqlqelERISGLTAE-----EAKEILLEKVEEE 166
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1499-1939 |
1.95e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 49.52 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1499 LETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASL--------EEAEASLEHEEGKILRIQLELN 1570
Cdd:COG5278 78 LEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1571 QVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNT 1650
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1651 QGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINT 1730
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1731 KKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALK 1810
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1811 GGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAE 1890
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 67189167 1891 EQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 1939
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
871-1338 |
2.14e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 49.75 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 871 EAKRKELEEKMVALMQEKNDLQLQVqaeadgladaeercdQLIKTKIQ-----LEAKIKELTERAEDEEEINAELTAKKR 945
Cdd:pfam07111 241 ELERQELLDTMQHLQEDRADLQATV---------------ELLQVRVQslthmLALQEEELTRKIQPSDSLEPEFPKKCR 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 946 KLedecseLKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTL- 1024
Cdd:pfam07111 306 SL------LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLq 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1025 ------TKAKTKLEQQVDDLEgslEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEfemsnlqski 1098
Cdd:pfam07111 380 melsraQEARRRQQQQTASAE---EQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVH---------- 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1099 edeqalgmqlqkKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISE---RL--EEAGGATSAQIEMNKKREa 1173
Cdd:pfam07111 447 ------------TIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREernRLdaELQLSAHLIQQEVGRARE- 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1174 EFQKMRRDLEEATLQHEATAaalrKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEiddLASNMETVSKAkgnlekmc 1253
Cdd:pfam07111 514 QGEAERQQLSEVAQQLEQEL----QRAQESLASVGQQLEVARQGQQESTEEAASLRQE---LTQQQEIYGQA-------- 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1254 rtLEDQLSEVKTKEEEQ----QRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLSR-GKQAFTQQIEELKRQLEEESK 1328
Cdd:pfam07111 579 --LQEKVAEVETRLREQlsdtKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRlQDEARKEEGQRLARRVQELER 656
|
490
....*....|
gi 67189167 1329 AKNALAHALQ 1338
Cdd:pfam07111 657 DKNLMLATLQ 666
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1315-1555 |
2.74e-05 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 47.79 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1315 QIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVaqwrtkyeTDAIQRTEELEEAK 1394
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAES--------ERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1395 KKLAQRLQDAEEHVEAVNSKCASL-EKTKQRLQNEVEDLMIDVERSNaacaaLDKKQRNFDKVLAEWKQKYEETQAELEA 1473
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALpSSDLSRMLAEAQRMLGEIRSRD-----FGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1474 SQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTeqiAEGGKHIHELEKIKKQIDQEKSELQASLEEAEA 1553
Cdd:pfam06008 167 PQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLN---LANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
..
gi 67189167 1554 SL 1555
Cdd:pfam06008 244 SL 245
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1391-1586 |
2.84e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1391 EEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAAcaaLDKKQRNFDKVLAEWKQKYEETQAE 1470
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1471 LEASQKESRSLS--TELFKVKNaYEESLDQLETLKRENKN-------LQQEISDLTEQIAEGGKHIHELEKIKKQIDQEK 1541
Cdd:COG3883 92 ARALYRSGGSVSylDVLLGSES-FSDFLDRLSALSKIADAdadlleeLKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 67189167 1542 SELQASLEEAEA---SLEHEEGKILRIQLELNQVKSEIDRKIAEKDEE 1586
Cdd:COG3883 171 AELEAQQAEQEAllaQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1209-1675 |
3.46e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.14 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1209 EQIDNLQRVKQKLEKEKSEL----------KMEIDDL-ASNMETVSKAKGNLEkmCRTLEDQLSEVKTKEEEQQRLINEL 1277
Cdd:PRK11281 70 ALLDKIDRQKEETEQLKQQLaqapaklrqaQAELEALkDDNDEETRETLSTLS--LRQLESRLAQTLDQLQNAQNDLAEY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1278 STQKARLHTesgefsrqldekdamvsQLSRGKQAFT---QQIEELKRQLEEESKAKNALAHALQsarhdcdllrEQYEEE 1354
Cdd:PRK11281 148 NSQLVSLQT-----------------QPERAQAALYansQRLQQIRNLLKGGKVGGKALRPSQR----------VLLQAE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1355 Q---EAKAELQRAMSKANS---EVAQWRTKYETDAIQRTEeleeakkKLAQRLQdaeehvEAVNSKCASL-EKTKQRLQN 1427
Cdd:PRK11281 201 QallNAQNDLQRKSLEGNTqlqDLLQKQRDYLTARIQRLE-------HQLQLLQ------EAINSKRLTLsEKTVQEAQS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1428 evedlmidversnaacaaLDKKQR-NFDKVLAewkqkyEETQAELEASQK------ESRSLSTELFKVKNayeesldQLE 1500
Cdd:PRK11281 268 ------------------QDEAARiQANPLVA------QELEINLQLSQRllkateKLNTLTQQNLRVKN-------WLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1501 TLKRENKNLQQEISDLTEQIAeggkhiheLEKIkkqIDQEKSELQASLEEAEASleheeGKI--LRI-QLELNQVKSeid 1577
Cdd:PRK11281 317 RLTQSERNIKEQISVLKGSLL--------LSRI---LYQQQQALPSADLIEGLA-----DRIadLRLeQFEINQQRD--- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1578 rKIAEKDEEIDQLKRNHlrvvesmQSTLDAEIR-SRNDALRIKKKMEGDLN-EMEIQLNHANrqaaeairNLRNTQGMLK 1655
Cdd:PRK11281 378 -ALFQPDAYIDKLEAGH-------KSEVTDEVRdALLQLLDERRELLDQLNkQLNNQLNLAI--------NLQLNQQQLL 441
|
490 500
....*....|....*....|
gi 67189167 1656 DTQlhldDALrgQDDLKEQL 1675
Cdd:PRK11281 442 SVS----DSL--QSTLTQQI 455
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1568-1811 |
3.64e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1568 ELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQStLDAEIRSRNDALRikkKMEGDLNEMEIQLNHANRQAAEAIRNL 1647
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA-LERRIAALARRIR---ALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1648 RNTQGMLKDtQLHLDDALRGQDDLK-----EQLAMVERRANLMQAEIEELRASLEQTERSRrvaeqelldaservQLLHT 1722
Cdd:COG4942 100 EAQKEELAE-LLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADL--------------AELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1723 QNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLD 1802
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
....*....
gi 67189167 1803 EAEQLALKG 1811
Cdd:COG4942 245 AAGFAALKG 253
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1296-1559 |
3.97e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.77 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1296 DEKDAMVSQLsRGKQAFtqQIEELKRQLEEESKAKnalahalqsarhdcdlLREQYEEEQEAKAELQRAMSKANSEVaqw 1375
Cdd:PRK05771 16 SYKDEVLEAL-HELGVV--HIEDLKEELSNERLRK----------------LRSLLTKLSEALDKLRSYLPKLNPLR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1376 rtkyETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLM------IDVER----SNAACAA 1445
Cdd:PRK05771 74 ----EEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdLDLSLllgfKYVSVFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1446 LDKKQRNFDKVLAEWKQKYEEtqaelEASQKESRSLSTeLFKVKNAYEESLDQLETLKRENKNL------QQEISDLTEQ 1519
Cdd:PRK05771 150 GTVPEDKLEELKLESDVENVE-----YISTDKGYVYVV-VVVLKELSDEVEEELKKLGFERLELeeegtpSELIREIKEE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 67189167 1520 IAEGGKHIHEL-EKIKKQIDQEKSELQASLEEAEASLEHEE 1559
Cdd:PRK05771 224 LEEIEKERESLlEELKELAKKYLEELLALYEYLEIELERAE 264
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
919-1343 |
4.37e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.14 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 919 LEAKIKELTERAEDEEEINAELTAKKRKLEDECSEL---KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAK 995
Cdd:pfam19220 8 LRVRLGEMADRLEDLRSLKADFSQLIEPIEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 996 LTKEKKALQEAhqqtLDDLQAEEDKVNTLTKAKTkleQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIEN 1075
Cdd:pfam19220 88 LVARLAKLEAA----LREAEAAKEELRIELRDKT---AQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1076 DKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQarieeleeeieaeraSRAKAEKQRSdlsRELE-EISERL 1154
Cdd:pfam19220 161 ELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELE---------------TQLDATRARL---RALEgQLAAEQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1155 EEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEAT-------AAALRKKhADSVAELGEQIDNLQRVKQKLEKEKSE 1227
Cdd:pfam19220 223 AERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATeqllaeaRNQLRDR-DEAIRAAERRLKEASIERDTLERRLAG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1228 LKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSevkTKEEEQQRLINELSTQKARLHTESGEFSRQldekdamvsqlsr 1307
Cdd:pfam19220 302 LEADLERRTQQFQEMQRARAELEERAEMLTKALA---AKDAALERAEERIASLSDRIAELTKRFEVE------------- 365
|
410 420 430
....*....|....*....|....*....|....*.
gi 67189167 1308 gKQAFTQQIEELKRQLEEESKAKNALAHALQSARHD 1343
Cdd:pfam19220 366 -RAALEQANRRLKEELQRERAERALAQGALEIARES 400
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
885-1094 |
5.19e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 885 MQEKNDLQLQVQAEADgLADAEERCDQLIKTKIQLEAKIKELTERAEDEEEINAELTAKKRKLEDECSELKKDIDdlelT 964
Cdd:PHA02562 199 TYNKNIEEQRKKNGEN-IARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE----Q 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 965 LAKVEK--EKHATenkVKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEqqvdDLEGSL 1042
Cdd:PHA02562 274 FQKVIKmyEKGGV---CPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLL----ELKNKI 346
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 67189167 1043 EQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNL 1094
Cdd:PHA02562 347 STNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1757-1929 |
6.69e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1757 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLalkggkKQIQKLEARVRELENEVENEQKR 1836
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1837 nieaVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQA-EEAEEQSNVNLAKFRKIQHELEEAEERAD 1915
Cdd:COG4717 148 ----LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....
gi 67189167 1916 IAESQVNKLRVKSR 1929
Cdd:COG4717 224 ELEEELEQLENELE 237
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
850-1263 |
7.19e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.52 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 850 EKEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKI-----------Q 918
Cdd:PRK04778 90 EAEELNDKFRFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLanrfsfgpaldE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 919 LEAKIKELTERAEDEEEINAE---LTAKK--RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN----LTEEMAGL 989
Cdd:PRK04778 170 LEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreLVEEGYHL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 990 DENiaKLTKEKKALQEAHQQTLDDLqaEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQES 1069
Cdd:PRK04778 250 DHL--DIEKEIQDLKEQIDENLALL--EELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQ 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1070 TMDIENDKQQLDEKlkkkeFEMSnlqskiEDEQALGMQLQKKIKELQARIEELEEEIeaerasrAKAEKQRSDLSRELEE 1149
Cdd:PRK04778 326 NKELKEEIDRVKQS-----YTLN------ESELESVRQLEKQLESLEKQYDEITERI-------AEQEIAYSELQEELEE 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1150 ISERLEEAggatsaqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsvaelgeqidnLQRVKQKLEK------ 1223
Cdd:PRK04778 388 ILKQLEEI-----------EKEQEKLSEMLQGLRKDELEAREKLERYRNK--------------LHEIKRYLEKsnlpgl 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 67189167 1224 ------EKSELKMEIDDLAS-------NMETVSKAKGNLEKMCRTLEDQLSEV 1263
Cdd:PRK04778 443 pedyleMFFEVSDEIEALAEeleekpiNMEAVNRLLEEATEDVETLEEETEEL 495
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1222-1374 |
7.82e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.88 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1222 EKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAM 1301
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67189167 1302 VSQLSRGKQAFTQQIEELKRQLeeeskakNALAHALQSARhdcdllreqyEEEQEAKAELQRAMSKANSEVAQ 1374
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQL-------AALEAALDASE----------KRDRESQAKIADLGRRLNVALAQ 187
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1379-1621 |
8.26e-05 |
|
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: 47.91 E-value: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1379 YETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKcASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNfdkvla 1458
Cdd:NF012221 1529 YILDNVVATSESSQQADAVSKHAKQDDAAQNALADK-ERAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALE------ 1601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1459 ewkqkyEETQAELEASQKESRSLSTELFKVKnayeESLDQLETLKRENKNLQQE---------ISDLTEQIAEGGKHIHE 1529
Cdd:NF012221 1602 ------TNGQAQRDAILEESRAVTKELTTLA----QGLDALDSQATYAGESGDQwrnpfagglLDRVQEQLDDAKKISGK 1671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1530 -LEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKiaeKDEEIDQLKRNHLRVVESMQSTLDAE 1608
Cdd:NF012221 1672 qLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKR---KDDALAKQNEAQQAESDANAAANDAQ 1748
|
250
....*....|...
gi 67189167 1609 IRSRNDALRIKKK 1621
Cdd:NF012221 1749 SRGEQDASAAENK 1761
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1038-1434 |
8.54e-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: 47.20 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1038 LEGSLEQEKKLRMDLERAKRKLEGDlklaqesTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQA 1117
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKE-------KERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1118 rieeleeeieaeraSRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQheataaaLR 1197
Cdd:pfam07888 109 --------------SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQ-------RK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1198 KKHADSvaelgeqiDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINEL 1277
Cdd:pfam07888 168 EEEAER--------KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1278 STQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQ---QIEELKRQLEEESKaknALAHALQSARHDCDLLREQYEEE 1354
Cdd:pfam07888 240 RSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQarlQAAQLTLQLADASL---ALREGRARWAQERETLQQSAEAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1355 QEAKAELQRAMSKANSEVAQWRTKYEtdaiqrTEELEEAKKKLAQRLQDAEEHVEAVNSKCA--SLEKTKQRLQNEVEDL 1432
Cdd:pfam07888 317 KDRIEKLSAELQRLEERLQEERMERE------KLEVELGREKDCNRVQLSESRRELQELKASlrVAQKEKEQLQAEKQEL 390
|
..
gi 67189167 1433 MI 1434
Cdd:pfam07888 391 LE 392
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1283-1806 |
9.26e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 47.33 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1283 RLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEeesKAKnalaHALQSARHDCDLLREQYEEEQEAKAELQ 1362
Cdd:pfam05701 46 KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLE---RAQ----TEEAQAKQDSELAKLRVEEMEQGIADEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1363 RAMSKANSEVAQWR-TKYETDAIQRTEELEEAKKK---LAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVER 1438
Cdd:pfam05701 119 SVAAKAQLEVAKARhAAAVAELKSVKEELESLRKEyasLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATKESLES 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1439 SNAACaaLDKKQRNFDKVLAeWKQKYEETQAELEASQKESRSLSTELFKVKNAYEEsldqLETLKRENKNLQQEI----- 1513
Cdd:pfam05701 199 AHAAH--LEAEEHRIGAALA-REQDKLNWEKELKQAEEELQRLNQQLLSAKDLKSK----LETASALLLDLKAELaayme 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1514 SDLTEQIAEGGKHIHELEKIKKQIDQEKSELqaslEEAEASLEH--EEGKILRIQLElnQVKSEIDRKIAEKDEeidqlk 1591
Cdd:pfam05701 272 SKLKEEADGEGNEKKTSTSIQAALASAKKEL----EEVKANIEKakDEVNCLRVAAA--SLRSELEKEKAELAS------ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1592 rnhLRVVESMQST----LDAEIRSRNDALRIKKKMEGDLNEMEI----QLNHANRQAAEAIRNLRNTQGMLKDTQLHLDD 1663
Cdd:pfam05701 340 ---LRQREGMASIavssLEAELNRTKSEIALVQAKEKEAREKMVelpkQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQ 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1664 AlrgqddlKEQLAMVERRANLMQAEIEELRASleqtERSRRVAEQELLDaSErvqlLHTQNTSLINTKKKLETDISqiqg 1743
Cdd:pfam05701 417 A-------KAAASTVESRLEAVLKEIEAAKAS----EKLALAAIKALQE-SE----SSAESTNQEDSPRGVTLSLE---- 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67189167 1744 EMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTS-AHLERMKKNMEQTVKDLQHRLDEAEQ 1806
Cdd:pfam05701 477 EYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSlEKLEEVNREMEERKEALKIALEKAEK 540
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1671-1939 |
9.42e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.43 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1671 LKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKklETDISQIQGEMEDIVQ 1750
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQ--ERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1751 EARNAEEKAkkaitdaaMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENEV 1830
Cdd:pfam17380 356 EERKRELER--------IRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1831 ENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRL-QDLVDKLQTKVKAYKRQAE--EAEEQSnvnlakfRKIQHEL 1907
Cdd:pfam17380 428 EQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLrQQEEERKRKKLELEKEKRDrkRAEEQR-------RKILEKE 500
|
250 260 270
....*....|....*....|....*....|..
gi 67189167 1908 EEAEERADIAESQVNKLRVKSREVHTKVISEE 1939
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEE 532
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1538-1781 |
9.83e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1538 DQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDR---KIAEKDEEIDQLKRnhlrvvesmqstldaeirsrnd 1614
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNElqaELEALQAEIDKLQA---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1615 alrikkkmegDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTqlhldDALRGQDDLKEQLamveRRANLMQAEIEELRA 1694
Cdd:COG3883 73 ----------EIAEAEAEIEERREELGERARALYRSGGSVSYL-----DVLLGSESFSDFL----DRLSALSKIADADAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1695 SLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELK 1774
Cdd:COG3883 134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
....*..
gi 67189167 1775 KEQDTSA 1781
Cdd:COG3883 214 AAAAAAA 220
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1350-1554 |
9.83e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1350 QYEEEQEAKAELQRAMSKANSEVAQWRTKYEtdaiqrteELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEV 1429
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE--------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1430 EDLMIDVERSNAACAALDK--KQRNFDKVLAEWK-------------QKYEETQAELEASQKESRSLSTELFKVKNAYEE 1494
Cdd:COG3883 89 GERARALYRSGGSVSYLDVllGSESFSDFLDRLSalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1495 SLDQLETLKRENknlQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEAS 1554
Cdd:COG3883 169 AKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1750-1918 |
1.15e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1750 QEARNAEEKAKKAITDAAMMAEELKKEQdtsahlermkknmEQTVKDLQHRLdeaeqlalkggkkqIQKLEARVRELENE 1829
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEA-------------LLEAKEEIHKL--------------RNEFEKELRERRNE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1830 VENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKV-KAYKRQAEEAEEQSNVNLAKFRKIQHELE 1908
Cdd:PRK12704 84 LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELeELIEEQLQELERISGLTAEEAKEILLEKV 163
|
170
....*....|
gi 67189167 1909 EAEERADIAE 1918
Cdd:PRK12704 164 EEEARHEAAV 173
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1750-1939 |
1.20e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1750 QEARNAEE----KAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAE------QLALKGGKKQIQKL 1819
Cdd:COG1196 207 RQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEaeleelRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1820 EARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAK 1899
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 67189167 1900 FRKIQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 1939
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1678-1922 |
1.20e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1678 VERRANLMQAEIEELRAsleqtersrrvAEQELLDASERVQLLhTQNTSLINTKKKLETDISQIQGEMEDI-VQEARNAE 1756
Cdd:COG4913 223 TFEAADALVEHFDDLER-----------AHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALrLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1757 EKAKKAITDAAmmaEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAeqlalkGGkkqiqkleARVRELENEVENEQKR 1836
Cdd:COG4913 291 ELLEAELEELR---AELARLEAELERLEARLDALREELDELEAQIRGN------GG--------DRLEQLEREIERLERE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1837 NIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEeaEERADI 1916
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE--AEIASL 431
|
....*.
gi 67189167 1917 AESQVN 1922
Cdd:COG4913 432 ERRKSN 437
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
847-979 |
1.30e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 847 AETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQ--EKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIK 924
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAriKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 925 ELTERAEDEE----EINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV 979
Cdd:COG1579 114 ELMERIEELEeelaELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1406-1758 |
1.33e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.04 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1406 EHVEAVNSKCAS--LEKTKQ-RLQNEVEDLMIDVERSNAACAALDKKQRNFDK---VLAEWKQKYEETQAELEASQKESR 1479
Cdd:pfam17380 279 QHQKAVSERQQQekFEKMEQeRLRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1480 slstelfkvknayeesldqletlKRENKNLQQEisdlteQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEAS--LEH 1557
Cdd:pfam17380 359 -----------------------KRELERIRQE------EIAMEISRMRELERLQMERQQKNERVRQELEAARKVkiLEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1558 E-EGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVV--ESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEiqln 1634
Cdd:pfam17380 410 ErQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVrlEEQERQQQVERLRQQEEERKRKKLELEKEKRD---- 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1635 hanRQAAEAIRNLRNTQGMLKDTQLHLDDalrgqddlkeqlamvERRANLMQAEIEELRASLEQTERsRRVAEQELLDAS 1714
Cdd:pfam17380 486 ---RKRAEEQRRKILEKELEERKQAMIEE---------------ERKRKLLEKEMEERQKAIYEEER-RREAEEERRKQQ 546
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 67189167 1715 ERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEK 1758
Cdd:pfam17380 547 EMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1078-1240 |
1.37e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1078 QQLDEKLKKKEFEMSNLQSKIEDeqalgmqLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEA 1157
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1158 GG-----ATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEI 1232
Cdd:COG1579 86 RNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*...
gi 67189167 1233 DDLASNME 1240
Cdd:COG1579 166 EELAAKIP 173
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
912-1158 |
1.43e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 912 LIKTKIQLEAK-IKELTERAEdeeEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLD 990
Cdd:PHA02562 192 HIQQQIKTYNKnIEEQRKKNG---ENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 991 ENIAKLTKEKKALQEAHQ-----QTLDDlqaEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLegdlkl 1065
Cdd:PHA02562 269 SKIEQFQKVIKMYEKGGVcptctQQISE---GPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL------ 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1066 aQESTMDIENDKQQLdeklkkkefemSNLQSKIEDeqalgmqLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR 1145
Cdd:PHA02562 340 -LELKNKISTNKQSL-----------ITLVDKAKK-------VKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVK 400
|
250
....*....|....*.
gi 67189167 1146 ELEE---ISERLEEAG 1158
Cdd:PHA02562 401 EKYHrgiVTDLLKDSG 416
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
947-1239 |
1.47e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 947 LEDECSELKKDIDDLELTLAKVEkEKHATENKvkNLTEEMAGLDENIAkltkEKKALQEAHQQTLDDLQAEEDKVNTltk 1026
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQ-QQIKTYNK--NIEEQRKKNGENIA----RKQNKYDELVEEAKTIKAEIEELTD--- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1027 AKTKLEQQVDDLEGSLeqeKKLRMDLERAKRKLEgdlKLAQESTMDIEND-----KQQL---DEKLKKKEFEMSNLQSKI 1098
Cdd:PHA02562 242 ELLNLVMDIEDPSAAL---NKLNTAAAKIKSKIE---QFQKVIKMYEKGGvcptcTQQIsegPDRITKIKDKLKELQHSL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1099 EDeqalgmqLQKKIKELQarieeleeeieaerasraKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKm 1178
Cdd:PHA02562 316 EK-------LDTAIDELE------------------EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEE- 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67189167 1179 rrdleeatlqheatAAALRKKHADSVAELGEQidnlqrvKQKLEKEKSELKMEID--DLASNM 1239
Cdd:PHA02562 370 --------------LQAEFVDNAEELAKLQDE-------LDKIVKTKSELVKEKYhrGIVTDL 411
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1465-1833 |
1.57e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.21 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1465 EETQAELEASQKESRSLSTELfkvknayEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSEL 1544
Cdd:pfam19220 37 EAILRELPQAKSRLLELEALL-------AQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1545 QASL-------EEAEASLEHEEGKILRIQLELNQVKSEI---DRKIAEKDEEIDQLKRNHLRvvesmqstLDAEIRSRNd 1614
Cdd:pfam19220 110 RIELrdktaqaEALERQLAAETEQNRALEEENKALREEAqaaEKALQRAEGELATARERLAL--------LEQENRRLQ- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1615 alRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAmVERRANLMqaEIEELRA 1694
Cdd:pfam19220 181 --ALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHR-AERASLRM--KLEALTA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1695 SLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDivQEARNAE-EKAKKAITD-AAMMAEE 1772
Cdd:pfam19220 256 RAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLER--RTQQFQEmQRARAELEErAEMLTKA 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 67189167 1773 LKkeqDTSAHLERMkknmEQTVKDLQHRLDEAEQLALKggkkQIQKLEARVRELENEVENE 1833
Cdd:pfam19220 334 LA---AKDAALERA----EERIASLSDRIAELTKRFEV----ERAALEQANRRLKEELQRE 383
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
856-1103 |
1.62e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 46.77 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 856 MKEDFEKAKEDLAKSEAKRK----ELEEKMVALMQEKN------------DLQLQVQAEADGLADAEERCDQLIKTKIQL 919
Cdd:PLN03229 484 LQERLENLREEFSKANSQDQlmhpVLMEKIEKLKDEFNkrlsrapnylslKYKLDMLNEFSRAKALSEKKSKAEKLKAEI 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 920 EAKIKELTERAEDEEEINAeltakkRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMaGLDENIAKltke 999
Cdd:PLN03229 564 NKKFKEVMDRPEIKEKMEA------LKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSM-GLEVIGVT---- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1000 KKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKklrmdLERAKRKLEGDLKLAQEstmdIENDKQQ 1079
Cdd:PLN03229 633 KKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSKIELLK-----LEVAKASKTPDVTEKEK----IEALEQQ 703
|
250 260
....*....|....*....|....
gi 67189167 1080 LDEKLKKKeFEMSNLQSKIEDEQA 1103
Cdd:PLN03229 704 IKQKIAEA-LNSSELKEKFEELEA 726
|
|
| COG6 |
smart01087 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
1376-1511 |
1.63e-04 |
|
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: 46.55 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1376 RTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQrnfdK 1455
Cdd:smart01087 9 RSDLEKRLLKINGEFLSEFKPVAEQLQRLSEDVQKLNNSCDSMKDQLNTAKNQTQDLISEASELQEELALLELKK----K 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 1456 VLAEWKQKYEETQAELEASQKESRSLSTELFKVknayeesLDQLETLKRENKNLQQ 1511
Cdd:smart01087 85 LLDAFLSKFTLSQDELDVLTSREGPIDDEFFQV-------LDKVQEIHEDCSVLLQ 133
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
884-1115 |
1.71e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.82 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 884 LMQEKNDLQLQVQAEADGLADAEERCDQLIKTKI-------QLEAKIKELTERAEDEEEINAELTAKKRKLEDECSELKK 956
Cdd:PLN02939 161 ILTEKEALQGKINILEMRLSETDARIKLAAQEKIhveileeQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 957 DIDDLELTLAKVEKekhaTENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQtLDDLQAEE--DKVNTLTKAKTKLEQQ 1034
Cdd:PLN02939 241 DIQFLKAELIEVAE----TEERVFKLEKERSLLDASLRELESKFIVAQEDVSK-LSPLQYDCwwEKVENLQDLLDRATNQ 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1035 VDDLEGSLEQEKKLRMDLERAKRKLEgDLKLAQESTMDIENDKQQLdeKLKKKEFEMSN--LQSKIEDEQALGMQLQKKI 1112
Cdd:PLN02939 316 VEKAALVLDQNQDLRDKVDKLEASLK-EANVSKFSSYKVELLQQKL--KLLEERLQASDheIHSYIQLYQESIKEFQDTL 392
|
...
gi 67189167 1113 KEL 1115
Cdd:PLN02939 393 SKL 395
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1495-1939 |
1.73e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1495 SLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKilriqlelnqvKS 1574
Cdd:PTZ00121 1068 QDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-----------KA 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1575 EIDRKIAEKDEEIDQLKRNHLRVVESMQSTldAEIRSRNDAlrikKKMEGDLNEMEIQLNHANRQAAEAirnlRNTQGML 1654
Cdd:PTZ00121 1137 EDARKAEEARKAEDAKRVEIARKAEDARKA--EEARKAEDA----KKAEAARKAEEVRKAEELRKAEDA----RKAEAAR 1206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1655 KDTQLHLDDALRGQDDlkeqlamvERRANLMQaEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLI------ 1728
Cdd:PTZ00121 1207 KAEEERKAEEARKAED--------AKKAEAVK-KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAikaeea 1277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1729 ----NTKKKLETDISQIQGEMEDI--VQEARNAEEKAKKAiTDAAMMAEELKKEQDTsahlerMKKNMEQTVKDlqhrlD 1802
Cdd:PTZ00121 1278 rkadELKKAEEKKKADEAKKAEEKkkADEAKKKAEEAKKA-DEAKKKAEEAKKKADA------AKKKAEEAKKA-----A 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1803 EAEQLALKGGKKQIQKLEARVRELENEVEnEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAY 1882
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKE-EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 67189167 1883 KRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 1939
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
860-1559 |
1.92e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 860 FEKAKEdlAKSEAKRKELEEKMVALMQEKNDLQLQVQAEAdgLADAEErcdQLIKTKIQLEAKIKELTERAEDEEEINAE 939
Cdd:PRK10246 190 FEQHKS--ARTELEKLQAQASGVALLTPEQVQSLTASLQV--LTDEEK---QLLTAQQQQQQSLNWLTRLDELQQEASRR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 940 LTAK---KRKLEDECSELKK---------------DIDDLELTLAKVEKEKhateNKVKNLTEEMAGLDENIAKLTKEKK 1001
Cdd:PRK10246 263 QQALqqaLAAEEKAQPQLAAlslaqparqlrphweRIQEQSAALAHTRQQI----EEVNTRLQSTMALRARIRHHAAKQS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1002 ALQEAHQQTLDDLQAEEDKV----NTLTKAKTKLEQQVDDLEgsleQEKKLRMDLERAKRKLEG----DLKLAQEST--- 1070
Cdd:PRK10246 339 AELQAQQQSLNTWLAEHDRFrqwnNELAGWRAQFSQQTSDRE----QLRQWQQQLTHAEQKLNAlpaiTLTLTADEVaaa 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1071 MDIENDKQQLDEKLkkkefemSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERAS---------RAKAEKQRS 1141
Cdd:PRK10246 415 LAQHAEQRPLRQRL-------VALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRykektqqlaDVKTICEQE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1142 DLSRELEEISERLEEA------GGATSAQIEMNKKREAEFQKMRRDL---EEATLQHEatAAALRKkhadsvaelgeQID 1212
Cdd:PRK10246 488 ARIKDLEAQRAQLQAGqpcplcGSTSHPAVEAYQALEPGVNQSRLDAlekEVKKLGEE--GAALRG-----------QLD 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1213 NLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGnlekMCRTLEDQLSEVKTKEEEQQRLINELStQKARLHTesgefs 1292
Cdd:PRK10246 555 ALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLN----ITLQPQDDIQPWLDAQEEHERQLRLLS-QRHELQG------ 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1293 rQLDEKDAMVSQlsrgkqaFTQQIEELKRQLEEeskAKNALAHALQSARHDCDLLREQYEEE---QEAKAELQRAMSKAN 1369
Cdd:PRK10246 624 -QIAAHNQQIIQ-------YQQQIEQRQQQLLT---ALAGYALTLPQEDEEASWLATRQQEAqswQQRQNELTALQNRIQ 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1370 SEVAQWRTKYETDaiqrtEELEEAKKKLAQRLQDAEEhveavnsKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKK 1449
Cdd:PRK10246 693 QLTPLLETLPQSD-----DLPHSEETVALDNWRQVHE-------QCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQA 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1450 QRNFDK--VLA-----EWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAE 1522
Cdd:PRK10246 761 SVFDDQqaFLAalldeETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRE 840
|
730 740 750
....*....|....*....|....*....|....*...
gi 67189167 1523 GGKHIHELEKIKKQIDQEKSELQASLEE-AEASLEHEE 1559
Cdd:PRK10246 841 NTTRQGEIRQQLKQDADNRQQQQALMQQiAQATQQVED 878
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1488-1927 |
2.10e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1488 VKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEA---EASLEHEEGKILR 1564
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKnryESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1565 IQLELNQVKS--------EIDRKIAEKDEEIDQLK-RNHLRVVESMQSTLDAEIRSRNDALR-------------IKKKM 1622
Cdd:PRK01156 268 ELEKNNYYKEleerhmkiINDPVYKNRNYINDYFKyKNDIENKKQILSNIDAEINKYHAIIKklsvlqkdyndyiKKKSR 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1623 EGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDAlrgQDDLKEQLAMVERRANLMQAEIEELRASLEQTE-- 1700
Cdd:PRK01156 348 YDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERM---SAFISEILKIQEIDPDAIKKELNEINVKLQDISsk 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1701 -----RSRRVAEQELLDASERVQLLHTQNTSLI------------------NTKKKLETDISQIQGEMEDIVQEAR---- 1753
Cdd:PRK01156 425 vsslnQRIRALRENLDELSRNMEMLNGQSVCPVcgttlgeeksnhiinhynEKKSRLEEKIREIEIEVKDIDEKIVdlkk 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1754 -----------------NAEEKAKKAITDAAMMAEELK---------KEQDTSAHLERMKKNMEQTVKDLQHRLD---EA 1804
Cdd:PRK01156 505 rkeyleseeinksineyNKIESARADLEDIKIKINELKdkhdkyeeiKNRYKSLKLEDLDSKRTSWLNALAVISLidiET 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1805 EQLALKGGKKQIQKLEARVRELENEVENEQKRNieaVKGLRKHERRVKELTYQTEEDRKNvlrlQDLVDKLQTKVKAYKR 1884
Cdd:PRK01156 585 NRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYI---DKSIREIENEANNLNNKYNEIQEN----KILIEKLRGKIDNYKK 657
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 67189167 1885 QAEEAEE----QSNVNlAKFRKIQHELEEAEERADIAESQVNKLRVK 1927
Cdd:PRK01156 658 QIAEIDSiipdLKEIT-SRINDIEDNLKKSRKALDDAKANRARLEST 703
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
933-1325 |
2.35e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 933 EEEINAEL-TAKKRKL-EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQT 1010
Cdd:PRK11281 38 EADVQAQLdALNKQKLlEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1011 LDDLQAEEdkvntltkaktkLEQQVDDLEGSLEQEKK-----------LRMDLERAKRKLEGDLKLAQEstmdIENdkqQ 1079
Cdd:PRK11281 118 LSTLSLRQ------------LESRLAQTLDQLQNAQNdlaeynsqlvsLQTQPERAQAALYANSQRLQQ----IRN---L 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1080 LDEKLKKKEFEMSNLQSKIEDEQA-LGMQLQKKIKELQARIEELEEeieaerasrakAEKQRSDLSrelEEISeRLEEAg 1158
Cdd:PRK11281 179 LKGGKVGGKALRPSQRVLLQAEQAlLNAQNDLQRKSLEGNTQLQDL-----------LQKQRDYLT---ARIQ-RLEHQ- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1159 gATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQI------------DNLqRVKQKLEkeks 1226
Cdd:PRK11281 243 -LQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLlkateklntltqQNL-RVKNWLD---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1227 elkmeiddlasnmetvskakgNLEKMCRTLEDQ---------LSEVKTKEEE---QQRLINELSTQKARLHTESGEFSRQ 1294
Cdd:PRK11281 317 ---------------------RLTQSERNIKEQisvlkgsllLSRILYQQQQalpSADLIEGLADRIADLRLEQFEINQQ 375
|
410 420 430
....*....|....*....|....*....|....*
gi 67189167 1295 LDE---KDAMVSQLSRG-KQAFTqqiEELKRQLEE 1325
Cdd:PRK11281 376 RDAlfqPDAYIDKLEAGhKSEVT---DEVRDALLQ 407
|
|
| EcCorA_ZntB-like |
cd12821 |
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily ... |
1299-1411 |
2.37e-04 |
|
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: 45.39 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1299 DAMVSQLSRGKQAFTQQIEELKRQLEEESKAKnALAHALqSARHDCDLLREQYEEEQEAKAELQRAMSKANSEvaQWRTK 1378
Cdd:cd12821 110 GAIIKALLTGIDQFEEKLEELEWDLLEGNNAI-KLDRIL-ELRRELLRLTNLIEPQQEVLMALQEAFAELLFS--EDEEE 185
|
90 100 110
....*....|....*....|....*....|...
gi 67189167 1379 YEtDAIQRTEELEEAKKKLAQRLQDAEEHVEAV 1411
Cdd:cd12821 186 LR-RTLDRIERLLQLIEEYEQELDTLQDIEEVV 217
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
929-1061 |
2.53e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 45.44 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 929 RAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENI-AKLTKEKKALQEAH 1007
Cdd:cd22656 101 DDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALkDLLTDEGGAIARKE 180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 1008 qqtLDDLQAEEDKVNT-----LTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEG 1061
Cdd:cd22656 181 ---IKDLQKELEKLNEeyaakLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDN 236
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1315-1524 |
2.71e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1315 QIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQwrtkyetdaiqRTEELEEAK 1394
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-----------AEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1395 KKLAQRLQDAEEHVEAVN---------------SKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAE 1459
Cdd:COG3883 86 EELGERARALYRSGGSVSyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67189167 1460 wkqkYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGG 1524
Cdd:COG3883 166 ----LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
856-983 |
2.88e-04 |
|
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: 45.14 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 856 MKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAeercdQLIKTKI-QLEAKIKELTERAEdee 934
Cdd:pfam10186 17 ARNRLYELRVDLARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKL-----RLLKSEVaISNERLNEIKDKLD--- 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 67189167 935 EINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLT 983
Cdd:pfam10186 89 QLRREIAEKKKKIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSI 137
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1207-1430 |
3.19e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1207 LGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMEtvskAKGNLEKMcRTLEDQLSEVKTKEEEQQRLINELSTQKARLHT 1286
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVDLSEE----AKLLLQQL-SELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1287 ESGEFSRqldekdamvsqlSRGKQAFTQQIEELKRQLEEESKaknalahalqsarhdcdLLREQYEEEQEAKAELQRAMS 1366
Cdd:COG3206 255 ALPELLQ------------SPVIQQLRAQLAELEAELAELSA-----------------RYTPNHPDVIALRAQIAALRA 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67189167 1367 KANSEVAQWRTKYETDAiqrtEELEEAKKKLAQRLQDAEEHVEAVNSKcaslEKTKQRLQNEVE 1430
Cdd:COG3206 306 QLQQEAQRILASLEAEL----EALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVE 361
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1686-1913 |
3.24e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1686 QAEIEELRASLEQTERSrrVAEQELLDASERVQLLHTQNTSlintKKKLETDISQIQgEMEDIVQEARNAEEKAKKAITD 1765
Cdd:pfam05557 1 RAELIESKARLSQLQNE--KKQMELEHKRARIELEKKASAL----KRQLDRESDRNQ-ELQKRIRLLEKREAEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1766 AAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRL-DEAEQLalkggKKQIQKLEARVRELENEVENEQKRNIEAVKGL 1844
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSEL-----RRQIQRAELELQSTNSELEELQERLDLLKAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 1845 RKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVkaykrQAEEAEEQSNVNLAKFRKIQHELEEAEER 1913
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQE-----QDSEIVKNSKSELARIPELEKELERLREH 212
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1191-1406 |
3.28e-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: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1191 ATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETvskAKGNLEKmcrtLEDQLSEVKTKEEEQ 1270
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA---LQAEIDK----LQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1271 QRLINEL--STQKARLHT-------ESGEFSRQLDEKDAmVSQLSRGKQAFTQQIEELKRQLEEeskAKNALAHALQSar 1341
Cdd:COG3883 85 REELGERarALYRSGGSVsyldvllGSESFSDFLDRLSA-LSKIADADADLLEELKADKAELEA---KKAELEAKLAE-- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67189167 1342 hdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEE 1406
Cdd:COG3883 159 -----LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
847-1010 |
3.48e-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: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 847 AETEKEMANMKEDFEKAKEDLAKSEAK----RKELEEKMVALMQEKNDLQ-LQVQAEADGLADAEERCDQLikTKI---- 917
Cdd:COG3883 54 NELQAELEALQAEIDKLQAEIAEAEAEieerREELGERARALYRSGGSVSyLDVLLGSESFSDFLDRLSAL--SKIadad 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 918 -----QLEAKIKELTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEN 992
Cdd:COG3883 132 adlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
170
....*....|....*...
gi 67189167 993 IAKLTKEKKALQEAHQQT 1010
Cdd:COG3883 212 AAAAAAAAAAAAAAAAAA 229
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
999-1407 |
3.62e-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: 45.45 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 999 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgdlkLAQESTMDIENDKQ 1078
Cdd:pfam05622 8 EKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLE----QLQEENFRLETARD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1079 QLDEKLKKKEFEMSNLQSKIEDEQALG---MQLQKKIKELQARIEELEEEIEAERASRAKAEkQRSDLSRELEEISER-- 1153
Cdd:pfam05622 84 DYRIKCEELEKEVLELQHRNEELTSLAeeaQALKDEMDILRESSDKVKKLEATVETYKKKLE-DLGDLRRQVKLLEERna 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1154 --------LEEA---GGATSAQIEMNKKREAEFQKMrrdLEEATLQHEATAAALRKKHadsvaelgEQIDNLQRVKQKLE 1222
Cdd:pfam05622 163 eymqrtlqLEEElkkANALRGQLETYKRQVQELHGK---LSEESKKADKLEFEYKKLE--------EKLEALQKEKERLI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1223 KEKSELKMEIDDL---ASNMETVSKAKGNLEKMCRTLEDQLSEVKTKE--EEQQRLINE----LSTQKARLHTESGEFSR 1293
Cdd:pfam05622 232 IERDTLRETNEELrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPAEirEKLIRLQHEnkmlRLGQEGSYRERLTELQQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1294 QLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAhalqSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVA 1373
Cdd:pfam05622 312 LLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQG----SKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIE 387
|
410 420 430
....*....|....*....|....*....|....
gi 67189167 1374 QWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEH 1407
Cdd:pfam05622 388 ELEPKQDSNLAQKIDELQEALRKKDEDMKAMEER 421
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1455-1659 |
3.78e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1455 KVLAEWKQKYEETQAEL--EASQKESRSLSTELFKVKNAYEESLDQLETLKRENK--NLQQEISDLTEQIAEGGKHIH-- 1528
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAea 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1529 --ELEKIKKQIDQEKSELQASLEEAEASLEHEE-----GKILRIQLELNQVKS----------EIDRKIAEKDEEIDQLK 1591
Cdd:COG3206 232 raELAEAEARLAALRAQLGSGPDALPELLQSPViqqlrAQLAELEAELAELSArytpnhpdviALRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67189167 1592 RNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQL 1659
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1135-1398 |
4.05e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1135 KAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKmrrDLEEATLQHEataaalrkkhaDSVAELGEQIDNL 1214
Cdd:PRK05771 47 KLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIK---DVEEELEKIE-----------KEIKELEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1215 QRVKQKLEKEKSELK------MEIDDLASNmETVSKAKGNLEKmcrtleDQLSEVktKEEEQQRLINELSTQKARL---- 1284
Cdd:PRK05771 113 ENEIKELEQEIERLEpwgnfdLDLSLLLGF-KYVSVFVGTVPE------DKLEEL--KLESDVENVEYISTDKGYVyvvv 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1285 --HTE-SGEFSRQLDEKDAMVSQLSRGKqAFTQQIEELKRQLEEESKAKNALAHALQSarhdcdlLREQYEEEQEAKAEL 1361
Cdd:PRK05771 184 vvLKElSDEVEEELKKLGFERLELEEEG-TPSELIREIKEELEEIEKERESLLEELKE-------LAKKYLEELLALYEY 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 67189167 1362 QRAMS-KANSEVAQWRTKYeTDAIQ------RTEELEEAKKKLA 1398
Cdd:PRK05771 256 LEIELeRAEALSKFLKTDK-TFAIEgwvpedRVKKLKELIDKAT 298
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
839-1060 |
4.23e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 839 KIKPLLKSAETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQ 918
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 919 LEAKIKELTERAEDEEEInAELTAKKRKLEDECSELKKDIDDLElTLAKVEKEKHATEN-KVKNLTEEmagLDENIAKLT 997
Cdd:PRK02224 577 LNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREALA-ELNDERRERLAEKReRKRELEAE---FDEARIEEA 651
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67189167 998 KEKKALQEAHQQTLDdlqaeeDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLE 1060
Cdd:PRK02224 652 REDKERAEEYLEQVE------EKLDELREERDDLQAEIGAVENELEELEELRERREALENRVE 708
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1438-1582 |
4.64e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1438 RSNAACAALDKKQRNFDKVLAEWKQKYEET--QAELEAsQKESRSLSTELFKVKNAYEESLDQLE-TLKRENKNLQQEIS 1514
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIkkEALLEA-KEEIHKLRNEFEKELRERRNELQKLEkRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67189167 1515 DLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEH------EEGKilriQLELNQVKSEIDRKIAE 1582
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaEEAK----EILLEKVEEEARHEAAV 173
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1673-1914 |
4.70e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1673 EQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQllhTQNTSLINTKKKLETDISQIQGEMEDIVQEA 1752
Cdd:pfam07888 20 TDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYK---RDREQWERQRRELESRVAELKEELRQSREKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1753 RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEqLALKGGKKQIQKLEARVRELENEVEN 1832
Cdd:pfam07888 97 EELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE-TELERMKERAKKAGAQRKEEEAERKQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1833 EQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQsnvnLAKFRKIQHELEEAEE 1912
Cdd:pfam07888 176 LQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL----LEELRSLQERLNASER 251
|
..
gi 67189167 1913 RA 1914
Cdd:pfam07888 252 KV 253
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
964-1195 |
4.80e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 964 TLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDdlegslE 1043
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE------E 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1044 QEKKLRMDLERAKRKLEGDLKLAQ----ESTMD-----------IENDKQQLDEkLKKKEFEMSNLQSKIEDEQAlgmQL 1108
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVllgsESFSDfldrlsalskiADADADLLEE-LKADKAELEAKKAELEAKLA---EL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1109 QKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQ 1188
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
....*..
gi 67189167 1189 HEATAAA 1195
Cdd:COG3883 240 AAAAASA 246
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1540-1924 |
5.11e-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: 45.33 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1540 EKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIA-EKDEEID-QLKRNHLRVVESmqstldaeirsrndALR 1617
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSArESDLEQDyQAASDHLNLVQT--------------ALR 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1618 IKKKME---GDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRA------------ 1682
Cdd:COG3096 345 QQEKIEryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyqqavqalek 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1683 --------NLMQAEIEE----LRASLEQTERSRRVAEQELLDASERvqllHTQNtslintKKKLETdISQIQGEMEdivq 1750
Cdd:COG3096 425 aralcglpDLTPENAEDylaaFRAKEQQATEEVLELEQKLSVADAA----RRQF------EKAYEL-VCKIAGEVE---- 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1751 eARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQtvkdlQHRLDE-AEQLALKGGKK---------QIQKLE 1820
Cdd:COG3096 490 -RSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQ-----QQNAERlLEEFCQRIGQQldaaeeleeLLAELE 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1821 ARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKnvlrLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKF 1900
Cdd:COG3096 564 AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLA----AQDALERLREQSGEALADSQEVTAAMQQLLERE 639
|
410 420
....*....|....*....|....
gi 67189167 1901 RKIQHELEEAEERADIAESQVNKL 1924
Cdd:COG3096 640 REATVERDELAARKQALESQIERL 663
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
906-1047 |
5.53e-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: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 906 EERCDQLIKTKIQLEAKIKELTEraeDEEEINAELTakkrkledECSELKKDIDDLELTL-AKVEKEKHATENKVKNLTE 984
Cdd:smart00787 136 EWRMKLLEGLKEGLDENLEGLKE---DYKLLMKELE--------LLNSIKPKLRDRKDALeEELRQLKQLEDELEDCDPT 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67189167 985 EMAGLDENIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKK 1047
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1661-1939 |
5.59e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1661 LDDALRGQDDLKEQLAMVER-----RANLMQAEIEELRASLEQTERSRRVAEQELLDASERVqllhtqntslintkkkle 1735
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEADEVL------------------ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1736 TDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQhrLDEAEQLALKggkKQ 1815
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER---LEELEEERDDLLAEAG--LDDADAEAVE---AR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1816 IQKLEARVRELENEVEnEQKRNIEAVKGLRKHER-RVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSN 1894
Cdd:PRK02224 316 REELEDRDEELRDRLE-ECRVAAQAHNEEAESLReDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 67189167 1895 VNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 1939
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1462-1853 |
6.33e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1462 QKYEETQ-AELEASQKE--SRSLSTELFKVKNAY--EESLDQLETLKRENknlqQEISdlTEQIAEGGKHIHELEKikkQ 1536
Cdd:PRK04778 24 RKRNYKRiDELEERKQEleNLPVNDELEKVKKLNltGQSEEKFEEWRQKW----DEIV--TNSLPDIEEQLFEAEE---L 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1537 IDQEK-SELQASLEEAEASLEHEEGKILRIQLELNQ-VKSEidrkiAEKDEEIDQLKRNHlrvvESMQSTLDAEIRSRND 1614
Cdd:PRK04778 95 NDKFRfRKAKHEINEIESLLDLIEEDIEQILEELQElLESE-----EKNREEVEQLKDLY----RELRKSLLANRFSFGP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1615 ALrikKKMEGDLNEMEIQLNHANR--------QAAEAIRNLRNTQGMLkdtqlhlddalrgQDDLKEQLAMVERRANLMQ 1686
Cdd:PRK04778 166 AL---DELEKQLENLEEEFSQFVEltesgdyvEAREILDQLEEELAAL-------------EQIMEEIPELLKELQTELP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1687 AEIEELRASLEQTERSRRVAEQELLDasERVQLLHTQNTSLINTKKKLETD-----ISQIQGEME---DIVQ---EARNA 1755
Cdd:PRK04778 230 DQLQELKAGYRELVEEGYHLDHLDIE--KEIQDLKEQIDENLALLEELDLDeaeekNEEIQERIDqlyDILErevKARKY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1756 EEKAKKAITDAAMMAEELKKEqdTSAHLERMKKNME------QTVKDLQHRLDEAE------QLALKGGKKQIQKLEARV 1823
Cdd:PRK04778 308 VEKNSDTLPDFLEHAKEQNKE--LKEEIDRVKQSYTlneselESVRQLEKQLESLEkqydeiTERIAEQEIAYSELQEEL 385
|
410 420 430
....*....|....*....|....*....|...
gi 67189167 1824 RELEN---EVENEQKRNIEAVKGLRKHERRVKE 1853
Cdd:PRK04778 386 EEILKqleEIEKEQEKLSEMLQGLRKDELEARE 418
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
952-1098 |
6.74e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 952 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLDDL----------------- 1014
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQLDAAfrqgehtglqlilsgee 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1015 ---------------QAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIEN---- 1075
Cdd:PRK11637 151 sqrgerilayfgylnQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESslqk 230
|
170 180
....*....|....*....|...
gi 67189167 1076 DKQQLDEkLKKKEfemSNLQSKI 1098
Cdd:PRK11637 231 DQQQLSE-LRANE---SRLRDSI 249
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1310-1477 |
6.96e-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: 43.37 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1310 QAFTQQIEELKRQLEEESKAKNALAHALQSarhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKyetdaiqrtee 1389
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEAR----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1390 LEEAKKKLAQrLQDAEEhVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQA 1469
Cdd:COG1579 75 IKKYEEQLGN-VRNNKE-YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
....*...
gi 67189167 1470 ELEASQKE 1477
Cdd:COG1579 153 ELEAELEE 160
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1640-1840 |
7.40e-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: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1640 AAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERV-- 1717
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELge 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1718 QLLHTQNTSLINTK-------KKLETDISQIQGeMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNM 1790
Cdd:COG3883 91 RARALYRSGGSVSYldvllgsESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 67189167 1791 EQTVKDLQHRLDEAEQLaLKGGKKQIQKLEARVRELENEVENEQKRNIEA 1840
Cdd:COG3883 167 EAAKAELEAQQAEQEAL-LAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1210-1401 |
7.49e-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: 43.37 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1210 QIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKarlhtesg 1289
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1290 EFsrqldekdamvsqlsrgkQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKAN 1369
Cdd:COG1579 90 EY------------------EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180 190
....*....|....*....|....*....|..
gi 67189167 1370 SEVaqwrtkyETDAIQRTEELEEAKKKLAQRL 1401
Cdd:COG1579 152 AEL-------EAELEELEAEREELAAKIPPEL 176
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
806-1912 |
7.68e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.82 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 806 KKMMERRESIFCIQYNVRAfMNVKHWPWMKLYFKIKPLLKSAETEKEMANMKEDFEKAKEDLAkseakrKELEEKMVALM 885
Cdd:PTZ00440 316 KKIEKGKEYIKRIQNNNIP-PQVKKDELKKKYFESAKHYASFKFSLEMLSMLDSLLIKKEKIL------NNLFNKLFGDL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 886 QEKndlqlqvqaeADGLADAEercdQLIKTKIQLEAKIKELTERAEDEEEINAELTAK-KRKLEDECSELKKDID----D 960
Cdd:PTZ00440 389 KEK----------IETLLDSE----YFISKYTNIISLSEHTLKAAEDVLKENSQKIADyALYSNLEIIEIKKKYDekinE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 961 LELTLAKVEKEKHATENKVKNLTEEMAGLD---ENIAKLTKEKKAL----------QEAHQQTLDDLQAEEDKVNTLTKA 1027
Cdd:PTZ00440 455 LKKSINQLKTLISIMKSFYDLIISEKDSMDskeKKESSDSNYQEKVdellqiinsiKEKNNIVNNNFKNIEDYYITIEGL 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1028 KTKLEQQVDDLEGSLEQEKKLRMDlERAKRKLEGDLKlaqeSTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQ 1107
Cdd:PTZ00440 535 KNEIEGLIELIKYYLQSIETLIKD-EKLKRSMKNDIK----NKIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEALF 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1108 LQKKIKElQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKRE--AEFQKMRRDLEEA 1185
Cdd:PTZ00440 610 NKEKFIN-EKNDLQEKVKYILNKFYKGDLQELLDELSHFLDDHKYLYHEAKSKEDLQTLLNTSKNeyEKLEFMKSDNIDN 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1186 TLQheataaaLRKKHADSVAELGEQI--DNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEV 1263
Cdd:PTZ00440 689 IIK-------NLKKELQNLLSLKENIikKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEF 761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1264 KTKEEEQQRLINElstqkarLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEE-ESKAKNALAHALQSARH 1342
Cdd:PTZ00440 762 ILHLYENDKDLPD-------GKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLNSyNILIQKLEAHTEKNDEE 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1343 DCDLLREQYEEEQEAK-AELQRAMSKANSEVaqwrtkyetDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKT 1421
Cdd:PTZ00440 835 LKQLLQKFPTEDENLNlKELEKEFNENNQIV---------DNIIKDIENMNKNINIIKTLNIAINRSNSNKQLVEHLLNN 905
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1422 KQRLQNEVEDLMIDVERSNAACaalDKKQRNFDKVLAEWKQKYEETQAELEASQkesrsLSTELFKVKNAYEES------ 1495
Cdd:PTZ00440 906 KIDLKNKLEQHMKIINTDNIIQ---KNEKLNLLNNLNKEKEKIEKQLSDTKINN-----LKMQIEKTLEYYDKSkening 977
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1496 -----LDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELekikkqIDQEKSELQASLEEAEASLEHE-EGKILRIQLEL 1569
Cdd:PTZ00440 978 ndgthLEKLDKEKDEWEHFKSEIDKLNVNYNILNKKIDDL------IKKQHDDIIELIDKLIKEKGKEiEEKVDQYISLL 1051
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1570 NQVKSEIDRKIAEKDEEIDQ--LKRNHLRVVESMQSTLDAEIRSRNDAL-RIKKKMEGDL----NEMEIQLNHANRQAAE 1642
Cdd:PTZ00440 1052 EKMKTKLSSFHFNIDIKKYKnpKIKEEIKLLEEKVEALLKKIDENKNKLiEIKNKSHEHVvnadKEKNKQTEHYNKKKKS 1131
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1643 AIRNLRNTQGMLKdtqlhlddalrgqddlkeQLAMVERRANLMQaEIEELRasleqtersrrvAEQELLDASERVQLLHT 1722
Cdd:PTZ00440 1132 LEKIYKQMEKTLK------------------ELENMNLEDITLN-EVNEIE------------IEYERILIDHIVEQINN 1180
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1723 QNTSLINTKKKLETDISQIQGEMEDIVQEARN-AEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQhRL 1801
Cdd:PTZ00440 1181 EAKKSKTIMEEIESYKKDIDQVKKNMSKERNDhLTTFEYNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELK-EI 1259
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1802 DEAEQLALKGGKKQIQKLEARVRELENEVENEQKRNIEAV-KGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVK 1880
Cdd:PTZ00440 1260 KLQVFSYLQQVIKENNKMENALHEIKNMYEFLISIDSEKIlKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAK 1339
|
1130 1140 1150
....*....|....*....|....*....|....
gi 67189167 1881 AYKRQAEEAEE--QSNVNLAKFRKIQHELEEAEE 1912
Cdd:PTZ00440 1340 EHKNKIYGSLEdkQIDDEIKKIEQIKEEISNKRK 1373
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1392-1806 |
8.90e-04 |
|
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: 44.07 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1392 EAKKKLA---QRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMidversnaacaaldKKQRNFDKVLAEWKQKYEETQ 1468
Cdd:pfam06160 83 KAKKALDeieELLDDIEEDIKQILEELDELLESEEKNREEVEELK--------------DKYRELRKTLLANRFSYGPAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1469 AELEASQKESRSLSTELFKVKNA--YEESLDQLETLKRENKNLQQEI-----------SDLTEQIAEGGKHIHELEKIK- 1534
Cdd:pfam06160 149 DELEKQLAEIEEEFSQFEELTESgdYLEAREVLEKLEEETDALEELMedipplyeelkTELPDQLEELKEGYREMEEEGy 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1535 ----KQIDQEKSELQASLEEAEASLEheegkilriQLELNQVKSEIDrkiaEKDEEIDQLkrnhlrvvesmQSTLDAEIR 1610
Cdd:pfam06160 229 alehLNVDKEIQQLEEQLEENLALLE---------NLELDEAEEALE----EIEERIDQL-----------YDLLEKEVD 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1611 SRNDalrIKKKMEgdlnEMEIQLNHANRQAaeaiRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIE 1690
Cdd:pfam06160 285 AKKY---VEKNLP----EIEDYLEHAEEQN----KELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVERLE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1691 ElraslEQTERSrrVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKK--------- 1761
Cdd:pfam06160 354 E-----KEVAYS--ELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKsnlpglpes 426
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 67189167 1762 ---AITDAAMMAEELKKEqdtsahLERMKKNMEQtvkdLQHRLDEAEQ 1806
Cdd:pfam06160 427 yldYFFDVSDEIEDLADE------LNEVPLNMDE----VNRLLDEAQD 464
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1192-1307 |
9.82e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1192 TAAALRKKHADSVAElgeQIDNLQRVKQKLEKEKSELKMEIDDlasnmetVSKAK-GNLEKMCRTLEDQLSEVKTKEEEQ 1270
Cdd:COG0542 397 EAAARVRMEIDSKPE---ELDELERRLEQLEIEKEALKKEQDE-------ASFERlAELRDELAELEEELEALKARWEAE 466
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 67189167 1271 QRLINELSTQKARLHTESG---EFSRQLDEKDAMVSQLSR 1307
Cdd:COG0542 467 KELIEEIQELKEELEQRYGkipELEKELAELEEELAELAP 506
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1149-1398 |
1.13e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.78 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1149 EISERLEEAggatsAQIEMNKKR-EAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIdnlqRVKQKLEKEKSE 1227
Cdd:PRK05035 437 EIRAIEQEK-----KKAEEAKARfEARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARV----KAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1228 LKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQ-LS 1306
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAaIA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1307 RGK-----QAFTQQIEELKRQLEEESKAKNALAHALQSARHDC-DLLREQYEEEQEAKAELQRAMSKAnsevaqwRTKYE 1380
Cdd:PRK05035 588 RAKakkaaQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEqQANAEPEEPVDPRKAAVAAAIARA-------KARKA 660
|
250
....*....|....*...
gi 67189167 1381 TDAIQRTEELEEAKKKLA 1398
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKA 678
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
839-1279 |
1.15e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.79 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 839 KIKPLLKSAETEKEMANMKEDFEKAKEDLAKSEAKRKELEE---KMVALMQEKNDlqlqvQAEADGLADAEERCDQLIKT 915
Cdd:COG5185 90 KEKKLDTKILQEYVNSLIKLPNYEWSADILISLLYLYKSEIvalKDELIKVEKLD-----EIADIEASYGEVETGIIKDI 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 916 KIQLEAKIKELT---ERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEN 992
Cdd:COG5185 165 FGKLTQELNQNLkklEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 993 IAKLTKEKKALQEAHQQTlDDLQAEedkvntltkaktKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlAQESTMD 1072
Cdd:COG5185 245 LEDLAQTSDKLEKLVEQN-TDLRLE------------KLGENAESSKRLNENANNLIKQFENTKEKIAEYTK-SIDIKKA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1073 IENDKQQLDEKLKKKEFE--MSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSdLSRELEEI 1150
Cdd:COG5185 311 TESLEEQLAAAEAEQELEesKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDS-FKDTIEST 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1151 SERLEEAGGATSAQIEMNKKREA--------EFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQ-RVKQKL 1221
Cdd:COG5185 390 KESLDEIPQNQRGYAQEILATLEdtlkaadrQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQsRLEEAY 469
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 67189167 1222 EKEKSELKMEIDDLASNME----TVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELST 1279
Cdd:COG5185 470 DEINRSVRSKKEDLNEELTqiesRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMR 531
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1144-1587 |
1.15e-03 |
|
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: 43.86 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1144 SRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRkkhadsvaelgeqidnlQRVKQKLEK 1223
Cdd:pfam05667 188 SEYLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGLASRLTPEEYR-----------------KRKRTKLLK 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1224 EKSElkmeidDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLinelsTQKARL-HTESGEFsrqldEKDAMV 1302
Cdd:pfam05667 251 RIAE------QLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGL-----TKGSRFtHTEKLQF-----TNEAPA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1303 SQLSRGKQafTQQIEELKRQLEEESKAknalahalqsarhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQwrTKYETD 1382
Cdd:pfam05667 315 ATSSPPTK--VETEEELQQQREEELEE-----------------LQEQLEDLESSIQELEKEIKKLESSIKQ--VEEELE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1383 AIQRT-EELEEA---KKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEdlmidversnAACAALDKKQRNFDKVLA 1458
Cdd:pfam05667 374 ELKEQnEELEKQykvKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWE----------KHRVPLIEEYRALKEAKS 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1459 EWKQKYEETQAELEASQKESRSLSTELfKVKnayEESLDQLETlkrENKNLQQEI--SDLTEQIAEggkhihelekIKKQ 1536
Cdd:pfam05667 444 NKEDESQRKLEEIKELREKIKEVAEEA-KQK---EELYKQLVA---EYERLPKDVsrSAYTRRILE----------IVKN 506
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 67189167 1537 IDQEKSELQASLEEAEAsleheegkilrIQLELNQVKSEIDRKIAEKDEEI 1587
Cdd:pfam05667 507 IKKQKEEITKILSDTKS-----------LQKEINSLTGKLDRTFTVTDELV 546
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1300-1582 |
1.18e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 43.85 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1300 AMVSQLSRGKQAFTQQIEELKRQLEEE--SKAKNALAHALQSARHDCDLLREQYEE------EQEAKAELQRAMSKANSE 1371
Cdd:NF033838 88 ALNKKLSDIKTEYLYELNVLKEKSEAEltSKTKKELDAAFEQFKKDTLEPGKKVAEatkkveEAEKKAKDQKEEDRRNYP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1372 VAQWRT----KYETDAIQRTEELEEAKKKlAQRLQDaEEHVEAVNSKCASLEKTKQRLQNevedlmIDVERSNAAcaalD 1447
Cdd:NF033838 168 TNTYKTleleIAESDVEVKKAELELVKEE-AKEPRD-EEKIKQAKAKVESKKAEATRLEK------IKTDREKAE----E 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1448 KKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELF---KVKNAYEESLDQL--ETLKRENKNLQQEISDLTEQIAE 1522
Cdd:NF033838 236 EAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPAtpdKKENDAKSSDSSVgeETLPSPSLKPEKKVAEAEKKVEE 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 1523 GGKHIHELEK---------IKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAE 1582
Cdd:NF033838 316 AKKKAKDQKEedrrnyptnTYKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAE 384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1737-1930 |
1.25e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1737 DISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEqlalkggkKQI 1816
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE--------KEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1817 QKLEARVRELENEVEN------------------EQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTK 1878
Cdd:COG4942 93 AELRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 67189167 1879 VKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSRE 1930
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1575-1925 |
1.27e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1575 EIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGML 1654
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1655 KDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKL 1734
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1735 ETDISQIQGEMEDIvqEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGKK 1814
Cdd:COG4372 163 QEELAALEQELQAL--SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1815 QIQKLEARVRELENEVENEQKRNIEA-VKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQS 1893
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAiLVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350
....*....|....*....|....*....|..
gi 67189167 1894 NVNLAKFRKIQHELEEAEERADIAESQVNKLR 1925
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
910-1101 |
1.28e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 43.31 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 910 DQLIKTKIQLEAKIKELTERaedEEEINAELTAKKR--KLEDECSELKKDIDDLEL--TLAKVEK--------EKHATEN 977
Cdd:pfam03148 133 ELLQRTLEQAWEQLRLLRAA---RHKLEKDLSDKKEalEIDEKCLSLNNTSPNISYkpGPTRIPPnsstpeewEKFTQDN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 978 KVKNLTEEMAGldeniAKLtkeKKALQEAHQQTLDDLQAEEDKVNT--------LTKAKTKLEQQVDDLEGSLEQEKKLR 1049
Cdd:pfam03148 210 IERAEKERAAS-----AQL---RELIDSILEQTANDLRAQADAVNFalrkrieeTEDAKNKLEWQLKKTLQEIAELEKNI 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 1050 MDLERAKRKLEGDLKLAQ------------ESTMD------------IENDKQQLDEKLKKKEFEMSNL---QSKIEDE 1101
Cdd:pfam03148 282 EALEKAIRDKEAPLKLAQtrlenrtyrpnvELCRDeaqyglvdevkeLEETIEALKQKLAEAEASLQALertRLRLEED 360
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
868-1070 |
1.29e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 43.70 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 868 AKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIKELTERAEDEEEINA---ELTAKK 944
Cdd:PRK00106 24 IKMKSAKEAAELTLLNAEQEAVNLRGKAERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSerqELKQIE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 945 RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEmaglDENIAKLTKEKkalqEAHQQTLDDLQAEEDKVNTL 1024
Cdd:PRK00106 104 SRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDER----EEQVEKLEEQK----KAELERVAALSQAEAREIIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 67189167 1025 TKAKTKLEQQVDDLEGSLEQEKKLRMD------LERAKRKLEGDLKLAQEST 1070
Cdd:PRK00106 176 AETENKLTHEIATRIREAEREVKDRSDkmakdlLAQAMQRLAGEYVTEQTIT 227
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
894-1146 |
1.32e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 894 QVQAEADGLADAEERCDQLIKTKIQLEAKIKELTERAEDeeeinaeltakkrkLEDECSELKKDIDDLELTLAKVEKEKH 973
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE--------------LQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 974 ATENKVKNLTEEMAGLDENIAKLTkekkALQEAhqQTLDDLQAEEDKVNTLTKAKTKLeqqvddlegsLEQEKKLRMDLE 1053
Cdd:COG3883 83 ERREELGERARALYRSGGSVSYLD----VLLGS--ESFSDFLDRLSALSKIADADADL----------LEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1054 RAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASR 1133
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
250
....*....|...
gi 67189167 1134 AKAEKQRSDLSRE 1146
Cdd:COG3883 227 AAAAAAAAAAAAA 239
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
852-1110 |
1.37e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 43.67 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 852 EMANMKEDFEKAK---EDLAKSEAKRKeleekmvaLMQEKNDLQLQVQaeadgladaeercdQLIKTKIQLEAKIKELTE 928
Cdd:pfam15066 296 KTPDTEQSFESLQpleEDMALNEVLQK--------LKHTNRKQQMQIQ--------------DLQCSNLYLEKKVKELQM 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 929 RaedeeeinaelTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQeahq 1008
Cdd:pfam15066 354 K-----------ITKQQVFVDIINKLKENVEELIEDKYNVILEKNDINKTLQNLQEILANTQKHLQESRKEKETLQ---- 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1009 qtlddLQAEEDKVNTL---TKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKR--KLEGDLKLAQESTMDI---ENDKQQL 1080
Cdd:pfam15066 419 -----LELKKIKVNYVhlqERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERlqQLKGELEKATTSALDLlkrEKETREQ 493
|
250 260 270
....*....|....*....|....*....|
gi 67189167 1081 DEKLKKKEFEMSNlQSKIEDEQALGMQLQK 1110
Cdd:pfam15066 494 EFLSLQEEFQKHE-KENLEERQKLKSRLEK 522
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
875-1234 |
1.53e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 875 KELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIKELTERAEDEEEINAELTAKKRKLEDECSEL 954
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 955 KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQ 1034
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1035 VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKE 1114
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1115 LQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1194
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 67189167 1195 ALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDD 1234
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1245-1871 |
1.64e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.64 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1245 AKGNLEKmcrtLEDQLSEVKTKEEEQQR--------LINELSTQKARLHTESGEFsRQLDEKDAMVSQLSRGKQAFTQQI 1316
Cdd:PRK10246 196 ARTELEK----LQAQASGVALLTPEQVQsltaslqvLTDEEKQLLTAQQQQQQSL-NWLTRLDELQQEASRRQQALQQAL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1317 EELkrqleeeSKAKNALAhALQSArHDCDLLREQYEEEQEAKAELQRAMSKANS------EVAQWRTKYETDAIQRTEEL 1390
Cdd:PRK10246 271 AAE-------EKAQPQLA-ALSLA-QPARQLRPHWERIQEQSAALAHTRQQIEEvntrlqSTMALRARIRHHAAKQSAEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1391 EEAKKKLAQRLQDAE------EHVEAVNSKCASLEKTKQRLQNEVEDLMIDVE-RSNAACAALDKKQrnfdkvlaewkqk 1463
Cdd:PRK10246 342 QAQQQSLNTWLAEHDrfrqwnNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQkLNALPAITLTLTA------------- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1464 yEETQAELeASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAE-------------GGKHIHEL 1530
Cdd:PRK10246 409 -DEVAAAL-AQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEmrqrykektqqlaDVKTICEQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1531 EKIKKQIDQEKSELQA--------SLE----EAEASLEHEEGKILRIQL--ELNQVKSEIDRKIAEKDEEIDQLKR--NH 1594
Cdd:PRK10246 487 EARIKDLEAQRAQLQAgqpcplcgSTShpavEAYQALEPGVNQSRLDALekEVKKLGEEGAALRGQLDALTKQLQRdeSE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1595 LRVVESMQSTLDAEIRSRNDALRIKKKMEGDLN-------EMEIQLNHANR------QAAEAIRNLRNTQGMLKDTQLHL 1661
Cdd:PRK10246 567 AQSLRQEEQALTQQWQAVCASLNITLQPQDDIQpwldaqeEHERQLRLLSQrhelqgQIAAHNQQIIQYQQQIEQRQQQL 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1662 DDALRG-----QDDLKEQLAMVER------------RANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQN 1724
Cdd:PRK10246 647 LTALAGyaltlPQEDEEASWLATRqqeaqswqqrqnELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQC 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1725 TSLINTKKKLETDISQIQGEMEDiVQEARNAEEKAKKAITDAAMMAEELKKEqdTSAHLERMKKNMEQtvkdlqhRLDEA 1804
Cdd:PRK10246 727 LSLHSQLQTLQQQDVLEAQRLQK-AQAQFDTALQASVFDDQQAFLAALLDEE--TLTQLEQLKQNLEN-------QRQQA 796
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 67189167 1805 EQLALKGGKKQIQKLEARVRELEN--EVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDL 1871
Cdd:PRK10246 797 QTLVTQTAQALAQHQQHRPDGLDLtvTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQAL 865
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1626-1925 |
1.87e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1626 LNEMEIQLnHANRQAAEAIRNLRNTQGMLK-------------------DTQLHLDDALRGQDDL---KEQLAMVERRAN 1683
Cdd:PRK04863 232 FQDMEAAL-RENRMTLEAIRVTQSDRDLFKhlitestnyvaadymrhanERRVHLEEALELRRELytsRRQLAAEQYRLV 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1684 LMQAEIEELrasleqtERSRRVAEQELLDASERVQLLhtqNTSLINTKKkletdISQIQGEMEDIVQEArnaeEKAKKAI 1763
Cdd:PRK04863 311 EMARELAEL-------NEAESDLEQDYQAASDHLNLV---QTALRQQEK-----IERYQADLEELEERL----EEQNEVV 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1764 TDAAMMAEELkKEQDTSAHLE--RMKKNME--QTVKDLQHR-----------LDEAEQ------LALKGGKKQIQKLEAR 1822
Cdd:PRK04863 372 EEADEQQEEN-EARAEAAEEEvdELKSQLAdyQQALDVQQTraiqyqqavqaLERAKQlcglpdLTADNAEDWLEEFQAK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1823 VRELENEV-ENEQKRNI---------EAVKGLRK---------HERRVKELTYQTEEDRKNVLRLQDLVDKLQT------ 1877
Cdd:PRK04863 451 EQEATEELlSLEQKLSVaqaahsqfeQAYQLVRKiagevsrseAWDVARELLRRLREQRHLAEQLQQLRMRLSEleqrlr 530
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 67189167 1878 KVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLR 1925
Cdd:PRK04863 531 QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1313-1750 |
1.88e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1313 TQQIEELKRQLEEESK---AKNALAHALQSARHDcdllreqyEEEQEAKAELQRAMSKANSEvaQWRTkyeTDAIQRTEE 1389
Cdd:PRK04863 252 TQSDRDLFKHLITESTnyvAADYMRHANERRVHL--------EEALELRRELYTSRRQLAAE--QYRL---VEMARELAE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1390 LEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTkQRLQNEVEDLMIDVERSNAacaaldkkqrnfdkVLAEWKQKYEETQA 1469
Cdd:PRK04863 319 LNEAESDLEQDYQAASDHLNLVQTALRQQEKI-ERYQADLEELEERLEEQNE--------------VVEEADEQQEENEA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1470 ELEASQKESRSLSTELFKVKNAYEE------SLDQLETLKRENKNLQQeISDLTEQIAEGgkHIHELEKIKKQIDQEKSE 1543
Cdd:PRK04863 384 RAEAAEEEVDELKSQLADYQQALDVqqtraiQYQQAVQALERAKQLCG-LPDLTADNAED--WLEEFQAKEQEATEELLS 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1544 LQASLEEAEASLE-HEEGKILriqleLNQVKSEIDRKIAekdeeiDQLKRNHLRVVESmQSTLDAeirsRNDALRIK-KK 1621
Cdd:PRK04863 461 LEQKLSVAQAAHSqFEQAYQL-----VRKIAGEVSRSEA------WDVARELLRRLRE-QRHLAE----QLQQLRMRlSE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1622 MEGDLNemeiQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTER 1701
Cdd:PRK04863 525 LEQRLR----QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAA 600
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 1702 SR-----------RVAEQ--ELLDASERV----QLLHTQNTSLINTKKKLETDISQIQGEMEDIVQ 1750
Cdd:PRK04863 601 RApawlaaqdalaRLREQsgEEFEDSQDVteymQQLLERERELTVERDELAARKQALDEEIERLSQ 666
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
843-1155 |
2.09e-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: 43.24 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 843 LLKSAETEKEMANMKEDFEKAKEDLAKSEAKRKELEekmvalmQEKNDLQlqvqaeaDGLADAEERCDQLIKTKIQLEAK 922
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQ-------QERDELA-------DEIASGASGKSALQDEKRRLEAR 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 923 IKELTERAEdEEEINAELTAKK-RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTeemagldeniAKLTKEKK 1001
Cdd:pfam01576 891 IAQLEEELE-EEQSNTELLNDRlRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELK----------AKLQEMEG 959
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1002 ALQEAHQQTLddlqaeedkvntltkakTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlaqESTMDIENDKQQLD 1081
Cdd:pfam01576 960 TVKSKFKSSI-----------------AALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLK---EVLLQVEDERRHAD 1019
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67189167 1082 EklKKKEFEMSNLQSKiedeqalgmQLQKKIKELQarieeleeeieaERASRAKAekQRSDLSRELEEISERLE 1155
Cdd:pfam01576 1020 Q--YKDQAEKGNSRMK---------QLKRQLEEAE------------EEASRANA--ARRKLQRELDDATESNE 1068
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
866-1587 |
2.11e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 866 DLAKSEAKRKE-------LEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIKELTERAEDEEEINA 938
Cdd:pfam10174 40 ELKKERALRKEeaarisvLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 939 ELTAKKRKLEDECSELKKDIDDLELtlaKVEKEKHATENKvknlteemaglDENIAKLtkekkaLQEAHQQTLDDLQAEE 1018
Cdd:pfam10174 120 RLQSEHERQAKELFLLRKTLEEMEL---RIETQKQTLGAR-----------DESIKKL------LEMLQSKGLPKKSGEE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1019 DkvNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDL-ERAKRKLEgdlkLAQESTmdiendkqqldeklkkkefEMSNLQSK 1097
Cdd:pfam10174 180 D--WERTRRIAEAEMQLGHLEVLLDQKEKENIHLrEELHRRNQ----LQPDPA-------------------KTKALQTV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1098 IEDEQALGMQLQKKIKELQarieeleEEIEAERAS-------------------------RAKAEKQRSDLSR---ELEE 1149
Cdd:pfam10174 235 IEMKDTKISSLERNIRDLE-------DEVQMLKTNgllhtedreeeikqmevykshskfmKNKIDQLKQELSKkesELLA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1150 ISERLEEAGGATS---AQIEMNKKREAEfqkmrRDLEEATLQHEATAAALRKKHADSVaeLGEQIDNLQRvkqkLEKEKS 1226
Cdd:pfam10174 308 LQTKLETLTNQNSdckQHIEVLKESLTA-----KEQRAAILQTEVDALRLRLEEKESF--LNKKTKQLQD----LTEEKS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1227 ELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESGEFSRQLDEKDAMVSQLS 1306
Cdd:pfam10174 377 TLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1307 rgkqaftQQIEELKRQLEEESKaknALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQR 1386
Cdd:pfam10174 457 -------EQREREDRERLEELE---SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAV 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1387 TEELEEAKK-----KLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWk 1461
Cdd:pfam10174 527 EQKKEECSKlenqlKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAEL- 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1462 QKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEqiaeggkhihELEKIKKQIDQEK 1541
Cdd:pfam10174 606 ESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMG----------ALEKTRQELDATK 675
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 67189167 1542 SEL---QASLEEAEA---SLEHEEGKILRIQLELNQvkSEIDRKIAEKDEEI 1587
Cdd:pfam10174 676 ARLsstQQSLAEKDGhltNLRAERRKQLEEILEMKQ--EALLAAISEKDANI 725
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1281-1479 |
2.51e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 42.90 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1281 KARLHTESGEFSRQLDEKDAMVSQLSRGKQAFT--QQIEELK-RQLEEESKAKNALAHALQSArhdcdlLREQYEEEQEA 1357
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNALADKERAEAdrQRLEQEKqQQLAAISGSQSQLESTDQNA------LETNGQAQRDA 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1358 KAELQRAMSKANSEVAQ------------------WRTKYET---DAIQrtEELEEAKKKLAQRLQDAEEHVEAVNSKCA 1416
Cdd:NF012221 1611 ILEESRAVTKELTTLAQgldaldsqatyagesgdqWRNPFAGgllDRVQ--EQLDDAKKISGKQLADAKQRHVDNQQKVK 1688
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67189167 1417 -SLEKTKQRLQNEvEDLMIDVErSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESR 1479
Cdd:NF012221 1689 dAVAKSEAGVAQG-EQNQANAE-QDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSR 1750
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1194-1341 |
2.73e-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: 41.45 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1194 AALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKakgNLEKmcrtLEDQLSEVKTkEEEQQRL 1273
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKK----YEEQLGNVRN-NKEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 67189167 1274 INELSTQKAR---LHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSAR 1341
Cdd:COG1579 95 QKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1168-1338 |
2.77e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1168 NKKREAEFQKmrrdlEEATLqhEATAAALRKKhADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKG 1247
Cdd:PRK12704 46 EAKKEAEAIK-----KEALL--EAKEEIHKLR-NEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1248 NLEKMCRTLEDQLSEVKTKEEEQ-QRL--INELSTQKARlhtesgefSRQLDEkdaMVSQLSRGKQAFTQQIEElKRQLE 1324
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQlQELerISGLTAEEAK--------EILLEK---VEEEARHEAAVLIKEIEE-EAKEE 185
|
170
....*....|....
gi 67189167 1325 EESKAKNALAHALQ 1338
Cdd:PRK12704 186 ADKKAKEILAQAIQ 199
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1688-1853 |
2.80e-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: 41.45 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1688 EIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITdaa 1767
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1768 mmAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVRELENEVENEQKRNIEAVKGLRKH 1847
Cdd:COG1579 88 --NKEYEALQKEIESLKRRISDLEDEILELMERIEELE--------EELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
....*.
gi 67189167 1848 ERRVKE 1853
Cdd:COG1579 158 LEELEA 163
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1706-1892 |
3.29e-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: 41.45 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1706 AEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEdivqEARNAEEKAKKAITDAAMMAEELKKE-QDTSAHLE 1784
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELA----ALEARLEAAKTELEDLEKEIKRLELEiEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1785 RMKKNMEQ--TVKDLQHRLDEAEQLalkggKKQIQKLEARVRELENEVENEQKRnieavkgLRKHERRVKELTYQTEEDR 1862
Cdd:COG1579 77 KYEEQLGNvrNNKEYEALQKEIESL-----KRRISDLEDEILELMERIEELEEE-------LAELEAELAELEAELEEKK 144
|
170 180 190
....*....|....*....|....*....|
gi 67189167 1863 KnvlRLQDLVDKLQTKVKAYKRQAEEAEEQ 1892
Cdd:COG1579 145 A---ELDEELAELEAELEELEAEREELAAK 171
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1669-1885 |
3.30e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1669 DDLKEQLAMVERRANLMQAEIEELRASleqtersrrvaeqelldASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDI 1748
Cdd:PHA02562 184 QTLDMKIDHIQQQIKTYNKNIEEQRKK-----------------NGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1749 VQEARNAEEKAKK---AITDAAMMAEELKKE--------------QDTSAHLERMKKNMEQtVKDLQHRLDEAE--QLAL 1809
Cdd:PHA02562 247 VMDIEDPSAALNKlntAAAKIKSKIEQFQKVikmyekggvcptctQQISEGPDRITKIKDK-LKELQHSLEKLDtaIDEL 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 1810 KGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQ 1885
Cdd:PHA02562 326 EEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1644-1920 |
3.39e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1644 IRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLamveRRANLmqaEIEELRASLEQTERSRRVAEQELLDASERVQ----- 1718
Cdd:PRK01156 161 INSLERNYDKLKDVIDMLRAEISNIDYLEEKL----KSSNL---ELENIKKQIADDEKSHSITLKEIERLSIEYNnamdd 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1719 LLHTQNT-----SLINTKKKLETDISQIQGEMEDI---VQEARNAEEKAKKAITDAAMMA-EELKKEQDTSAHLERMKKN 1789
Cdd:PRK01156 234 YNNLKSAlnelsSLEDMKNRYESEIKTAESDLSMElekNNYYKELEERHMKIINDPVYKNrNYINDYFKYKNDIENKKQI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1790 MEQTVKDLQHRLDEAEQLA-LKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELtyqtEEDRKNVLRL 1868
Cdd:PRK01156 314 LSNIDAEINKYHAIIKKLSvLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKI----EEYSKNIERM 389
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67189167 1869 QDLVDKLQTKVKAYKRQAEEAEEQSNVNL-----------AKFRKIQHELEEAEERADIAESQ 1920
Cdd:PRK01156 390 SAFISEILKIQEIDPDAIKKELNEINVKLqdisskvsslnQRIRALRENLDELSRNMEMLNGQ 452
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
850-1040 |
3.80e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 850 EKEMANMKEDF-EKAKEDLAKSEAKRKELEE----KMVALMQEKNDLQLQVQAEADGLAdaEERCDQLIK------TKIQ 918
Cdd:pfam12128 695 DKKHQAWLEEQkEQKREARTEKQAYWQVVEGaldaQLALLKAAIAARRSGAKAELKALE--TWYKRDLASlgvdpdVIAK 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 919 LEAKIKELTERAEDEEEINAE------------------LTAKKRKLEDECSELKKD----IDDLELTLAKVEKEKHATE 976
Cdd:pfam12128 773 LKREIRTLERKIERIAVRRQEvlryfdwyqetwlqrrprLATQLSNIERAISELQQQlarlIADTKLRRAKLEMERKASE 852
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 67189167 977 NKVKNLTEEMAGLDENIAKLT--KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEG 1040
Cdd:pfam12128 853 KQQVRLSENLRGLRCEMSKLAtlKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKN 918
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
877-1155 |
3.95e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 877 LEEKMVALMQEKNDLQLQVQAEADG--------LADAEERCDQLIKTKIQLEAKIKELTERAEDEEEINAELTAKKRKLE 948
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAEPSRlyslyekeIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 949 DECSELKKDIDdlELTLAKVEkekhaTENKVKNLTEEMAGLDENiakLTKEKKALQEAHQQTldDLQAEEDKVNT--LTK 1026
Cdd:pfam00038 103 NDLVGLRKDLD--EATLARVD-----LEAKIESLKEELAFLKKN---HEEEVRELQAQVSDT--QVNVEMDAARKldLTS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1027 AKTKLEQQVDdlegslEQEKKLRMDLERA-KRKLEGDLKLAQESTMDIENDKQQLDEKLKKkefeMSNLQSKIEDEQALG 1105
Cdd:pfam00038 171 ALAEIRAQYE------EIAAKNREEAEEWyQSKLEELQQAAARNGDALRSAKEEITELRRT----IQSLEIELQSLKKQK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 67189167 1106 MQLQKKIKELQARIEELeeeieaerasRAKAEKQRSDLSRELEEISERLE 1155
Cdd:pfam00038 241 ASLERQLAETEERYELQ----------LADYQELISELEAELQETRQEMA 280
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
913-1181 |
4.27e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 913 IKTKIQLEaKIKELTERAED--------EEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEkhatenkVKNLTE 984
Cdd:PRK05771 36 LKEELSNE-RLRKLRSLLTKlsealdklRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKE-------IKELEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 985 EMAGLDENIAKLTKEKKALQEAHqqTLD-DLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKklrmdLERAKRKLEGDL 1063
Cdd:PRK05771 108 EISELENEIKELEQEIERLEPWG--NFDlDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVEN-----VEYISTDKGYVY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1064 KLAqestMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGmQLQKKIKELqarieeleeeieaerasrakaEKQRSDL 1143
Cdd:PRK05771 181 VVV----VVLKELSDEVEEELKKLGFERLELEEEGTPSELIR-EIKEELEEI---------------------EKERESL 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 67189167 1144 SRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRD 1181
Cdd:PRK05771 235 LEELKELAKKYLEELLALYEYLEIELERAEALSKFLKT 272
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
845-1088 |
4.52e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 845 KSAETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIK-------TKI 917
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEkvkelkeERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 918 QLEAKIKELTERAEDEEEINAELTAKKRKLEdecsELKKDIDDLE-----------------LTLAKVEKEKHATE---- 976
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSID----KLRKEIERLEwrqqtevlspeeekelvEKIKELEKELEKAKkale 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 977 --NKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLER 1054
Cdd:COG1340 158 knEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 67189167 1055 AKRKLEGDLKLAQESTMDI---------ENDKQQLDEKLKKKE 1088
Cdd:COG1340 238 ELRELRKELKKLRKKQRALkrekekeelEEKAEEIFEKLKKGE 280
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1607-1767 |
4.56e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1607 AEIRSRNDALR-IKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMV--ERRAN 1683
Cdd:COG1579 13 QELDSELDRLEhRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1684 LMQAEIEELrasleqtERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAI 1763
Cdd:COG1579 93 ALQKEIESL-------KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....
gi 67189167 1764 TDAA 1767
Cdd:COG1579 166 EELA 169
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1004-1098 |
4.72e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 39.61 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1004 QEAHQQTLDDLQAE-EDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDE 1082
Cdd:pfam11559 54 RESLNETIRTLEAEiERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAH 133
|
90
....*....|....*.
gi 67189167 1083 KLKKKEFEMSNLQSKI 1098
Cdd:pfam11559 134 EVKKRDREIEKLKERL 149
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1550-1860 |
4.86e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1550 EAEASLEHEEGKILRIQLELNQVKSEIDRKiaekdeeidQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKM-EGDLNE 1628
Cdd:pfam12128 231 QAIAGIMKIRPEFTKLQQEFNTLESAELRL---------SHLHFGYKSDETLIASRQEERQETSAELNQLLRTlDDQWKE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1629 MEIQLNHANRQAAEAIRNLRNTQGMLKDtqlhldDALRGQDDLKEQLAMVERRANLMQAEIEELRASLE-QTERSRRVAE 1707
Cdd:pfam12128 302 KRDELNGELSAADAAVAKDRSELEALED------QHGAFLDADIETAAADQEQLPSWQSELENLEERLKaLTGKHQDVTA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1708 Q----ELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMM----AEELKKEQDT 1779
Cdd:pfam12128 376 KynrrRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRlksrLGELKLRLNQ 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1780 SAHLERMKKNMEQTVkDLQHRLDEAEQLALKGgkkqiqklearVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTE 1859
Cdd:pfam12128 456 ATATPELLLQLENFD-ERIERAREEQEAANAE-----------VERLQSELRQARKRRDQASEALRQASRRLEERQSALD 523
|
.
gi 67189167 1860 E 1860
Cdd:pfam12128 524 E 524
|
|
| zf-C4H2 |
pfam10146 |
Zinc finger-containing protein; This is a family of proteins which appears to have a highly ... |
1476-1605 |
5.10e-03 |
|
Zinc finger-containing protein; This is a family of proteins which appears to have a highly conserved zinc finger domain at the C terminal end, described as -C-X2-CH-X3-H-X5-C-X2-C-. The structure is predicted to contain a coiled coil. Members are annotated as being tumour-associated antigen HCA127 in humans but this could not confirmed.
Pssm-ID: 462963 [Multi-domain] Cd Length: 213 Bit Score: 40.44 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1476 KESRSLSTELFKVKNayeESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELekikKQIDQEKSELQASLEEAEASL 1555
Cdd:pfam10146 3 KDIRHKTAQLEKLKE---RLLKELEAHENEEKCLKEYKKEMELLLQEKMAHVEEL----RLIHADINKMEKVIKEAEEER 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 67189167 1556 EHEEGKILRIQLELNQVKSEIDRKIaEKDEEIDQLKRNHLRVVESMQSTL 1605
Cdd:pfam10146 76 NRVLEGAVRLHEEYIPLKLEIDRMR-RELLGLEELPLLHEEEEDLIQTTI 124
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1210-1483 |
5.13e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1210 QIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKgnlekmcRTLEDQLSEVKTKEEEQQRLINELSTQKARLHTESG 1289
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEY-------NELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1290 EFSRQLDEKDAMVSQL-----SRGKQAFTQQIEELKRQleeeskaknalahalqsARHDCDLLREQyeeeQEAKAELQRA 1364
Cdd:COG3883 90 ERARALYRSGGSVSYLdvllgSESFSDFLDRLSALSKI-----------------ADADADLLEEL----KADKAELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1365 MSKANSEVAqwrtkyetdaiqrteELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACA 1444
Cdd:COG3883 149 KAELEAKLA---------------ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
250 260 270
....*....|....*....|....*....|....*....
gi 67189167 1445 ALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLST 1483
Cdd:COG3883 214 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
957-1059 |
5.25e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 957 DIDDLELTLAKVEKEKHATENkvknltEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVD 1036
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100
....*....|....*....|...
gi 67189167 1037 DLEGSLEQEKKLRMDLERAKRKL 1059
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLL 508
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1388-1923 |
5.46e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.55 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1388 EELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKqrlqNEVEDLMIDVERsnaacAALDKKQRNFDKVLAewKQKYEET 1467
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTK----RLIEELKLNLER-----AQTEEAQAKQDSELA--KLRVEEM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1468 qaELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQ----IAEGGKHIHELEKIKKQIDQEKSE 1543
Cdd:pfam05701 111 --EQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSErdiaIKRAEEAVSASKEIEKTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1544 LQASLEEAE----ASLEHEEGKIlRIQLELNQVKSEIDRKIAEKDEEIDQLkRNHLRVVESMQSTLDAeirsrNDALRIK 1619
Cdd:pfam05701 189 LIATKESLEsahaAHLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-----ASALLLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1620 KKMEgdLNE-MEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQ 1698
Cdd:pfam05701 262 LKAE--LAAyMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAASLRSELEKEKAELAS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1699 TERSRRVAEqelldaservqllhtqntslintkkkleTDISQIQGEMEDIVQEARNAEEKAKKAitdAAMMAEELKKEQD 1778
Cdd:pfam05701 340 LRQREGMAS----------------------------IAVSSLEAELNRTKSEIALVQAKEKEA---REKMVELPKQLQQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1779 TSAHLERMKKNMEQTVKDLQHRLDEAEQlalkgGKKQIQKLEARVRELENEVE---NEQKRNIEAVKGLRKHER------ 1849
Cdd:pfam05701 389 AAQEAEEAKSLAQAAREELRKAKEEAEQ-----AKAAASTVESRLEAVLKEIEaakASEKLALAAIKALQESESsaestn 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 67189167 1850 ---RVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNK 1923
Cdd:pfam05701 464 qedSPRGVTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIALEKAEK 540
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1446-1835 |
6.02e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.58 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1446 LDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETlKRENKNLQQeisDLTEQIAEGGK 1525
Cdd:pfam13166 87 LGEESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECWKKIK-RKKNSALSE---ALNGFKYEANF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1526 HIHELEKIKKQIDQEKSEL-QASLEEAEASLEHEEGKILR------IQLELNQVKSEIDRKIAEKDEEIDQL-KRNHLRV 1597
Cdd:pfam13166 163 KSRLLREIEKDNFNAGVLLsDEDRKAALATVFSDNKPEIApltfnvIDFDALEKAEILIQKVIGKSSAIEELiKNPDLAD 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1598 -VES--------------MQSTLDAEIRSRNDAlrikkkmegdlnemeiqlnHANRQAAEAIRNLRNTqgmlkdtqlhLD 1662
Cdd:pfam13166 243 wVEQglelhkahldtcpfCGQPLPAERKAALEA-------------------HFDDEFTEFQNRLQKL----------IE 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1663 DALRGQDDLKEQLAMVERRANLMQA---EIEELRASLEQTERS----RRVAEQELLDASERVQLLHTQNtsLINTKKKLE 1735
Cdd:pfam13166 294 KVESAISSLLAQLPAVSDLASLLSAfelDVEDIESEAEVLNSQldglRRALEAKRKDPFKSIELDSVDA--KIESINDLV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1736 TDISQIQGEMEDIVQEARNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQHRLDEAEqlalkggkKQ 1815
Cdd:pfam13166 372 ASINELIAKHNEITDNFEEEKNKAKKKL--RLHLVEEFKSEIDE---YKDKYAGLEKAINSLEKEIKNLE--------AE 438
|
410 420
....*....|....*....|
gi 67189167 1816 IQKLEARVRELENEVENEQK 1835
Cdd:pfam13166 439 IKKLREEIKELEAQLRDHKP 458
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
858-1116 |
7.08e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.20 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 858 EDFEKAKEDLAKSEAKRKELEEkmvalMQEKNDLQLQVQAeadGLADAEERCDQLIKTKIQLEAKIKELTERAEDEEein 937
Cdd:pfam13166 212 DALEKAEILIQKVIGKSSAIEE-----LIKNPDLADWVEQ---GLELHKAHLDTCPFCGQPLPAERKAALEAHFDDE--- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 938 aeLTAKKRKLEDECSELKKDIDDLELTLAKV---EKEKHATENKVKNLTEEM----AGLDENIAKLtkEKKALQEAHQQT 1010
Cdd:pfam13166 281 --FTEFQNRLQKLIEKVESAISSLLAQLPAVsdlASLLSAFELDVEDIESEAevlnSQLDGLRRAL--EAKRKDPFKSIE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1011 LDDLQAEEDKVNTLtkaktkleqqVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKqqLDEKLKKKEFE 1090
Cdd:pfam13166 357 LDSVDAKIESINDL----------VASINELIAKHNEITDNFEEEKNKAKKKLRLHLVEEFKSEIDE--YKDKYAGLEKA 424
|
250 260
....*....|....*....|....*.
gi 67189167 1091 MSNLQSKIEDEQALGMQLQKKIKELQ 1116
Cdd:pfam13166 425 INSLEKEIKNLEAEIKKLREEIKELE 450
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1782-1903 |
7.20e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1782 HLERMKKNMEQTVKDLQHRLDEAEQLAlkggKKQIQKLEARVRELENEVENEQKRNiEAVKGLRKHERrvkeltyQTEED 1861
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELH----EKQKFYLRQSVIDLQTKLQEMQMER-DAMADIRRRES-------QSQED 142
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 67189167 1862 RKNvlRLQDLVDKLQtkvkAYKRQAEEAEEQSNVNLAKFRKI 1903
Cdd:pfam15921 143 LRN--QLQNTVHELE----AAKCLKEDMLEDSNTQIEQLRKM 178
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1536-1700 |
7.25e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.87 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1536 QIDQekSELQASLEEAEASLEHEEGKILRIQLELNQ---VKSEIDRKIAEKDEEIDQLKRnhlrvvesmqstLDAEIRSR 1612
Cdd:pfam00529 50 QLDP--TDYQAALDSAEAQLAKAQAQVARLQAELDRlqaLESELAISRQDYDGATAQLRA------------AQAAVKAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1613 NDALrikKKMEGDLNEMEIQLNH---ANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQD-DLKEQLAMVERRANLMQAE 1688
Cdd:pfam00529 116 QAQL---AQAQIDLARRRVLAPIggiSRESLVTAGALVAQAQANLLATVAQLDQIYVQITqSAAENQAEVRSELSGAQLQ 192
|
170
....*....|..
gi 67189167 1689 IEELRASLEQTE 1700
Cdd:pfam00529 193 IAEAEAELKLAK 204
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1678-1917 |
7.35e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.67 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1678 VERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLhtqntslintKKKLETDISQIQGEMEDIVQEARNAEE 1757
Cdd:pfam00038 45 PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDF----------RQKYEDELNLRTSAENDLVGLRKDLDE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1758 kAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQTVKDLQHRL-DEAEQLALKGGKKQiqKLEARVRELENEVENEQKR 1836
Cdd:pfam00038 115 -ATLARVDLEAKIESLKEE------LAFLKKNHEEEVRELQAQVsDTQVNVEMDAARKL--DLTSALAEIRAQYEEIAAK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1837 NIEAVKglRKHERRVKELTYQTE--------------EDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRK 1902
Cdd:pfam00038 186 NREEAE--EWYQSKLEELQQAAArngdalrsakeeitELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQE 263
|
250
....*....|....*..
gi 67189167 1903 IQHELEEA--EERADIA 1917
Cdd:pfam00038 264 LISELEAElqETRQEMA 280
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
844-974 |
7.38e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 844 LKSAETEKEMANMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVqaeadgladaeERCDQLIKtkiQLEAKI 923
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAEL-----------EEKDERIE---RLEREL 450
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 67189167 924 KELTERAEDEEEINAELTAKKRK---LEDECSELKKDIDDLEltlAKVEKEKHA 974
Cdd:COG2433 451 SEARSEERREIRKDREISRLDREierLERELEEERERIEELK---RKLERLKEL 501
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1294-1484 |
7.44e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1294 QLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKA----- 1368
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1369 -----------------------NSEVAQWRTKYETDAIQRT----EELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKT 1421
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldRLSALSKIADADADLLEELkadkAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67189167 1422 KQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTE 1484
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
878-1068 |
7.63e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 878 EEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIKELTERAedeEEINAELTAKKRKLEDECSELKKd 957
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 958 iddleltLAKVEKEKHATENKV------KNLTEEMAGLD--ENIAKLTKEKKALQEAHQQTLDDLQAE-EDKVNTLTKAK 1028
Cdd:COG3883 91 -------RARALYRSGGSVSYLdvllgsESFSDFLDRLSalSKIADADADLLEELKADKAELEAKKAElEAKLAELEALK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 67189167 1029 TKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQE 1068
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
858-1177 |
7.66e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 858 EDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIKELTERAEDEEEIN 937
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 938 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKalqeahQQTLDDLQAE 1017
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA------EQALDELLKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1018 EDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSK 1097
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1098 IEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQK 1177
Cdd:COG4372 272 DTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLL 351
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1669-1798 |
8.11e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.43 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67189167 1669 DDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTqNTSLINTKKKLETDISQIQGEMEDI 1748
Cdd:cd22656 117 KTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLT-DEGGAIARKEIKDLQKELEKLNEEY 195
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 67189167 1749 VQEARNAEEKAKKAITDAammAEELKKEQDTSAHLERMKKNMEQTVKDLQ 1798
Cdd:cd22656 196 AAKLKAKIDELKALIADD---EAKLAAALRLIADLTAADTDLDNLLALIG 242
|
|
| |
