|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-772 |
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: 1347.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 580 FALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGGKKKGSSFQTVSALFRE 659
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 660 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 739
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 153791586 740 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-772 |
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: 1319.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEitSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKK--DSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14913 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14913 319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 580 FALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSgaqTAEGEGAGGGAKKGGKKKGSSFQTVSALFRE 659
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYA---TFATADADSGKKKVAKKKGSSFQTVSALFRE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 660 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 739
Cdd:cd14913 556 NLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEG 635
|
650 660 670
....*....|....*....|....*....|...
gi 153791586 740 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14913 636 QFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
100-772 |
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: 1310.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEitsGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKES---GKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd01377 238 DILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd01377 318 KEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKvvKGKAEA 578
Cdd:cd01377 398 EQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 579 HFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAqtaegeGAGGGAKKGGKKKGSSFQTVSALFR 658
Cdd:cd01377 476 HFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDY------EESGGGGGKKKKKGGSFRTVSQLHK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 659 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 738
Cdd:cd01377 550 EQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPK 629
|
650 660 670
....*....|....*....|....*....|....
gi 153791586 739 GQFiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd01377 630 GFD-DGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
100-772 |
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: 1264.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEitSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEE--SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 580 FALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSgaqTAEGEGAGGGAKKGGKKKGSSFQTVSALFRE 659
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFS---TYASAEADSGAKKGAKKKGSSFQTVSALFRE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 660 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 739
Cdd:cd14918 556 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEG 635
|
650 660 670
....*....|....*....|....*....|...
gi 153791586 740 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14918 636 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-772 |
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: 1254.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 580 FALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTaeGEGAGGGAKKGGKKKGSSFQTVSALFRE 659
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAA--AEAEEGGGKKGGKKKGSSFQTVSALFRE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 660 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 739
Cdd:cd14910 559 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 638
|
650 660 670
....*....|....*....|....*....|...
gi 153791586 740 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14910 639 QFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-772 |
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: 1237.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 580 FALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTaeGEGAGGGAKKGGKKKGSSFQTVSALFRE 659
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQT--AEAEGGGGKKGGKKKGSSFQTVSALFRE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 660 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 739
Cdd:cd14915 559 NLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 638
|
650 660 670
....*....|....*....|....*....|...
gi 153791586 740 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14915 639 QFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-772 |
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: 1205.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEiTSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQ-QPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14923 240 DILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 580 FALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGaQTAEGEGAGGGAKKGGKKKGSSFQTVSALFRE 659
Cdd:cd14923 480 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSN-YAGAEAGDSGGSKKGGKKKGSSFQTVSAVFRE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 660 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 739
Cdd:cd14923 559 NLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEG 638
|
650 660 670
....*....|....*....|....*....|...
gi 153791586 740 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14923 639 QFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
101-772 |
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: 1165.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 181 SGAGKTVNTKRVIQYFATIAVTGE--KKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDgpGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 259 GKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSA 338
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 339 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 419 TVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 499 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKV-VKGKAE 577
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPdKKRKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 578 AHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGGKKKGSSFQTVSALF 657
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDPKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 658 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 737
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 153791586 738 EGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14927 642 DDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-772 |
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: 1145.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKiqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14917 159 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 580 FALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSgaqTAEGEGAGGGAKKGGKKKGSSFQTVSALFRE 659
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFA---NYAGADAPIEKGKGKAKKGSSFQTVSALHRE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 660 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 739
Cdd:cd14917 556 NLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEG 635
|
650 660 670
....*....|....*....|....*....|...
gi 153791586 740 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14917 636 QFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-772 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 1127.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKiQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNAN-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14916 240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14916 400 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 580 FALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTaeGEGAGGGAKKGGKKKGSSFQTVSALFRE 659
Cdd:cd14916 480 FSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYAS--ADTGDSGKGKGGKKKGSSFQTVSALHRE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 660 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 739
Cdd:cd14916 558 NLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEG 637
|
650 660 670
....*....|....*....|....*....|...
gi 153791586 740 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14916 638 QFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
100-772 |
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: 1034.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEeitsgkiQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKpELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14929 154 MLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14929 233 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14929 313 IEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14929 393 EQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 580 FALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFsgaQTAEGEGAGGGAKKGGKKKGSSFQTVSALFRE 659
Cdd:cd14929 473 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF---ENYISTDSAIQFGEKKRKKGASFQTVASLHKE 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 660 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 739
Cdd:cd14929 550 NLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKS 629
|
650 660 670
....*....|....*....|....*....|...
gi 153791586 740 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14929 630 KFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
88-772 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1031.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 88 IEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFML 167
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 168 TDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEeitsgkiqGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV--------GRLEEQILQSNPILEAFGNAKTVRNNNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 248 GKFIRIHFGTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQ-GEISVASI 326
Cdd:pfam00063 153 GKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTIDGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 327 DDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPR 406
Cdd:pfam00063 232 DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 407 VKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:pfam00063 312 IKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 486 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSA 564
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 565 NFQKPKVvkgKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGG- 643
Cdd:pfam00063 470 HFQKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTPk 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 644 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 723
Cdd:pfam00063 547 RTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 153791586 724 FKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:pfam00063 627 FVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
81-784 |
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: 990.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 81 NPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISD 160
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 161 NAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKkeeitsgkiqGTLEDQIISANPLLEAFGNAKTVR 240
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV----------GSVEDQILESNPILEAFGNAKTLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 241 NDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQG- 319
Cdd:smart00242 151 NNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 320 EISVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQA-EPDGTEVADKAAYLQSLNSADL 398
Cdd:smart00242 230 CLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 399 LKALCYPRVKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQ 478
Cdd:smart00242 310 EKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 479 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYd 557
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 558 QHLGKSANFQKPKVvkgKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTaegegagg 637
Cdd:smart00242 468 QHHKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVS-------- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 638 gakkgGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPS 717
Cdd:smart00242 537 -----NAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPY 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791586 718 RILYADFKQRYKVLNASAIPEGQFiDSKKASEKLLASIDIDHTQYKFGHTKVFFKAGLLGLLEEMRD 784
Cdd:smart00242 612 RLPFDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
101-772 |
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: 986.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgkiQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTGKQSSDG------KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 261 LASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd14934 156 LAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 341 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd14934 236 VLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 421 EQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14934 316 EQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 501 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGK-AEAH 579
Cdd:cd14934 396 QEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 580 FALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFsgaqtaegEGAGGGAKKGGKKKGSSFQTVSALFRE 659
Cdd:cd14934 476 FELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLF--------KEEEAPAGSKKQKRGSSFMTVSNFYRE 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 660 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 739
Cdd:cd14934 548 QLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG 627
|
650 660 670
....*....|....*....|....*....|...
gi 153791586 740 qFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14934 628 -FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-772 |
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: 971.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAA----KSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14909 157 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14909 317 VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVK-GKAEA 578
Cdd:cd14909 397 EQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 579 HFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFsgAQTAEGEGAGGGAKKGGKKKGSSFQTVSALFR 658
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIF--ADHAGQSGGGEQAKGGRGKKGGGFATVSSAYK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 659 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 738
Cdd:cd14909 555 EQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQG 634
|
650 660 670
....*....|....*....|....*....|....
gi 153791586 739 GQfiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14909 635 EE--DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
100-772 |
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: 833.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQ-EAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 179 GESGAGKTVNTKRVIQYFATIAvtgekKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALS-----GSGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 259 GKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPF----VSQGEISVASIDDQEELMA 334
Cdd:cd00124 156 GRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEFQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 335 TDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREE--QAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNE 412
Cdd:cd00124 236 LLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 413 YVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 490
Cdd:cd00124 316 TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 491 FFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKP 569
Cdd:cd00124 396 FFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 570 KvvkgKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLyqksaMKTLAQlfsgaqtaegegagggakkggkkkgss 649
Cdd:cd00124 475 R----KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDL-----LRSGSQ--------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 650 fqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 729
Cdd:cd00124 519 -------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 153791586 730 VLNASAiPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd00124 592 ILAPGA-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
30-1118 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 833.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 30 RPFDAKTSVFVAEPKESFVKGTIQsregGKVTVKTEGGATLTVKDDQVFPMNPPKYDKIEDMAMMTHLHEPAVLYNLKER 109
Cdd:COG5022 14 IPDEEKGWIWAEIIKEAFNKGKVT----EEGKKEDGESVSVKKKVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 110 YAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNT 189
Cdd:COG5022 90 YNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 190 KRVIQYFAtiAVTGekkkeeiTSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETY 269
Cdd:COG5022 170 KRIMQYLA--SVTS-------SSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 270 LLEKSRVVFQLKAERSYHIFYQITSNKkPELIEMLLITTNPYDYPFVSQGE-ISVASIDDQEELMATDSAIDILGFTNEE 348
Cdd:COG5022 241 LLEKSRVVHQNKNERNYHIFYQLLAGD-PEELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 349 KVSIYKLTGAVMHYGNLKFKqKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVEQVSNAVG 428
Cdd:COG5022 320 QDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 429 ALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEG 508
Cdd:COG5022 399 SLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 509 IEWTFIDFgMDLAACIELIEK--PMGIFSILEEECMFPKATDTSFKNKLYDQ-HLGKSANFQKPKVVKGKaeahFALIHY 585
Cdd:COG5022 479 IEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVKHY 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 586 AGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQtaegegagggakkgGKKKGSSFQTVSALFRENLNKLM 665
Cdd:COG5022 554 AGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEE--------------NIESKGRFPTLGSRFKESLNSLM 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 666 TNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI--- 742
Cdd:COG5022 620 STLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwke 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 743 DSKKASEKLLASIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDDKLAQLITRTQARCRGFLARVEYQRMVERREAIFCIQY 822
Cdd:COG5022 700 DTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQH 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 823 NIRSFMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKIKDELaKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAE 902
Cdd:COG5022 780 GFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTI-KREKKLRETEEVEFSLKAEVLIQKFGRSLKAK 858
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 903 GLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINaELTAKKRKLEDECSELKKDID-----DLELTLAKVEKEKHAT 977
Cdd:COG5022 859 KRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELESEIIELKKSLSsdlieNLEFKTELIARLKKLL 937
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 978 EN-KVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQekklRMDLER 1056
Cdd:COG5022 938 NNiDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQ----YGALQE 1013
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791586 1057 AKRKLEgdlklaqesIMDIENEKQQLDEKLKKKEFEISNLQSKIED-EQALGI---QLQKKIKELQ 1118
Cdd:COG5022 1014 STKQLK---------ELPVEVAELQSASKIISSESTELSILKPLQKlKGLLLLennQLQARYKALK 1070
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
101-772 |
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: 789.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 181 SGAGKTVNTKRVIQYFATIAVTGEKK-----KEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASKPKGsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 256 GTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGEISVASIDDQEELMAT 335
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 336 DSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 414
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 415 TKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 494 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLgksanfQKPKVVK 573
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 574 G--KAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGGKKKGSS-F 650
Cdd:cd14911 474 TdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRKGmF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 651 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 730
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 153791586 731 LNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
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 ... |
101-772 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 768.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEeitsGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVASSHKGRKD----HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 261 LASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLIttNPYD-YPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14920 158 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL--EGFNnYRFLSNGYIPIPGQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 419 TVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14920 315 TKEQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 497 FVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKVVK 573
Cdd:cd14920 394 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 574 GKAEahFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSG-----AQTAEGEGAGGGAKKGGKKKGS 648
Cdd:cd14920 473 DKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivGLDQVTGMTETAFGSAYKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 649 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 728
Cdd:cd14920 551 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 153791586 729 KVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
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 ... |
101-772 |
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: 714.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 261 LASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCL-EDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 341 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14932 320 QEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 499 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKvvKGK 575
Cdd:cd14932 400 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPK--KLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 576 AEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQ----TAEGEGAGGGAKKGGKKKGSSFQ 651
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDrivgLDKVAGMGESLHGAFKTRKGMFR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 652 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 731
Cdd:cd14932 557 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 153791586 732 NASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14932 637 TPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
101-772 |
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: 696.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASSHKGKKDT----SITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 261 LASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPyDYPFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd14921 158 IVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN-NYTFLSNGFVPIPAAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 341 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14921 316 KEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 499 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGK 575
Cdd:cd14921 396 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLC-TEQGNHPKFQKPKQLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 576 AEahFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGGKKKGSS-----F 650
Cdd:cd14921 475 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKtkkgmF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 651 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 730
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 153791586 731 LNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14921 633 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-772 |
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: 679.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 179 GESGAGKTVNTKRVIQYFATiaVTGEKKKEeiTSgkiqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFAT--VGGSSSGE--TQ------VEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 259 GKLASADIETYLLEKSRVVFQLKAERSYHIFYQI-TSNKKPELIEMLLitTNPYDYPFVSQGE-ISVASIDDQEELMATD 336
Cdd:cd01380 151 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLcAAASLPELKELHL--GSAEDFFYTNQGGsPVIDGVDDAAEFEETR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 337 SAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd01380 229 KALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 417 GQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 494
Cdd:cd01380 309 PLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 495 HMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGK-SANFQKPKVVK 573
Cdd:cd01380 389 HVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 574 GKaeahFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKtlaqlfsgaqtaegegagggakkggkkkgssFQTV 653
Cdd:cd01380 468 TA----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR-------------------------------KKTV 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 654 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 733
Cdd:cd01380 513 GSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLP 592
|
650 660 670
....*....|....*....|....*....|....*....
gi 153791586 734 SAipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd01380 593 SK--EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-772 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 671.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 261 LASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL-ENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 341 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 421 EQVSNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKvvKGKA 576
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVL-QEQGTHPKFFKPK--KLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 577 EAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQT---AEGEGAGGGAKKGGKKKGSSFQTV 653
Cdd:cd15896 478 EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRivgLDKVSGMSEMPGAFKTRKGMFRTV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 654 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 733
Cdd:cd15896 558 GQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 637
|
650 660 670
....*....|....*....|....*....|....*....
gi 153791586 734 SAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd15896 638 NAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-772 |
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: 669.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEeitsgkiQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 261 LASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLIttNPYD-YPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14919 155 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 419 TVEQVSNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14919 312 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 498 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKG 574
Cdd:cd14919 392 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 575 KAEahFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGG-----KKKGSS 649
Cdd:cd14919 471 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETAlpgafKTRKGM 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 650 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 729
Cdd:cd14919 549 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 153791586 730 VLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14919 629 ILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-772 |
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: 658.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPKGRKEP----GVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 261 LASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYdYPFVSQGEiSVASIDDQEELMATDSAID 340
Cdd:cd14930 158 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGP-SSSPGQERELFQETLESLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 341 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14930 236 VLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14930 315 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 498 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKVVKG 574
Cdd:cd14930 394 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPRHLRD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 575 KAEahFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLF---SGAQTAEGEGAGGGAKKGGKKKGSSFQ 651
Cdd:cd14930 473 QAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRRGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 652 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 731
Cdd:cd14930 551 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 153791586 732 NASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14930 631 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-772 |
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: 636.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRgkKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIAVTGekkkeeitsgkiqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd01383 79 ESGAGKTETAKIAMQYLAALGGGS-------------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGE-ISVASIDDQEELMATDSA 338
Cdd:cd01383 146 KICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNcLTIDGVDDAKKFHELKEA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 339 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd01383 225 LDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 419 TVEQVSNAVGALAKAVYEKMFLWMVARINQQLDT-KQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd01383 305 TLQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 498 VLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFqkpkvvKGKA 576
Cdd:cd01383 385 KLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGER 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 577 EAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKtLAQLFsgAQTAEGEGAGGGAKKGGKKKGSSFQTVSAL 656
Cdd:cd01383 457 GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQ-LPQLF--ASKMLDASRKALPLTKASGSDSQKQSVATK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 657 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAI 736
Cdd:cd01383 534 FKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV 613
|
650 660 670
....*....|....*....|....*....|....*.
gi 153791586 737 PEGQFIDSkkASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd01383 614 SASQDPLS--TSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
101-772 |
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: 632.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 181 SGAGKTVNTKRVIQYFATIavtgekkkeeitSGKiQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd01381 82 SGAGKTESTKLILQYLAAI------------SGQ-HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 261 LASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGE-ISVASIDDQEELMATDSAI 339
Cdd:cd01381 149 IEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD-ASDYYYLTQGNcLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQRE--EQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 417
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 418 QTVEQVSNAVGALAKAVYEKMFLWMVARIN----QQLDTKQPRQYfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINsaiyKPRGTDSSRTS-IGVLDIFGFENFEVNSFEQLCINFANENLQQFFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 494 HHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPkvv 572
Cdd:cd01381 387 RHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 573 KGKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFS-----GAQTAEGEgagggakkggkkkg 647
Cdd:cd01381 462 KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNedismGSETRKKS-------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 648 ssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 727
Cdd:cd01381 528 ---PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVER 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 153791586 728 YKVLnASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd01381 605 YRVL-VPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
101-772 |
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: 628.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 181 SGAGKTVNTKRVIQYFAtiAVTGEkkkeeiTSGKIQGTlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd01378 82 SGAGKTEASKRIMQYIA--AVSGG------SESEVERV-KDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 261 LASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd01378 153 PVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 341 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDgTEVADKAAYLQSLNSADLLKALCYPRVKVGNEY---VTKG 417
Cdd:cd01378 233 VIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 418 QTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQ-YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHhm 496
Cdd:cd01378 312 LNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 497 FVL--EQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNKLyDQHLGKSANFQKPKVV 572
Cdd:cd01378 390 LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 573 KGKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLF-SGAQTAEGEGAGggakkggkkkgssfq 651
Cdd:cd01378 468 FELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFpEGVDLDSKKRPP--------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 652 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 731
Cdd:cd01378 533 TAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLL 612
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 153791586 732 NASAIPEGQFIDsKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd01378 613 SPKTWPAWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
101-772 |
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: 594.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 181 SGAGKTVNTKRVIQYFAtiAVTGEkkkeeitsgkiQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14883 82 SGAGKTETTKLILQYLC--AVTNN-----------HSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 261 LASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKK--PELIEmLLITTNPYDYPFVSQ-GEISVASIDDQEELMATDS 337
Cdd:cd14883 149 IKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKE-KLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 338 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd14883 228 AMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 417 GQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14883 308 PLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKvvKGK 575
Cdd:cd14883 388 FKLEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPD--RRR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 576 AEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGGKKKGSSFQ--TV 653
Cdd:cd14883 464 WKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTSRGTSKGkpTV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 654 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 733
Cdd:cd14883 544 GDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDP 623
|
650 660 670
....*....|....*....|....*....|....*....
gi 153791586 734 SAIPEGQFIDsKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14883 624 RARSADHKET-CGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
100-772 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 583.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 179 GESGAGKTVNTKRVIQYFATIAvtgekkKEEITSGKiqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG------GRAVTEGR---SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 259 GKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGE-ISVASIDDQEELMATDS 337
Cdd:cd01384 152 GRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKD-PKQFHYLNQSKcFELDGVDDAEEYRATRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 338 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKqkqreEQAEPDGTEVADKAAYLQSLNSADLL--------KALCYPRVKV 409
Cdd:cd01384 231 AMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEKSEFHLKAAAELLmcdekaleDALCKRVIVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 410 GNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 489
Cdd:cd01384 306 PDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 490 QFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSANFQK 568
Cdd:cd01384 386 QHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 569 PKvvkgKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFsgaqtaegegagGGAKKGGKKKGS 648
Cdd:cd01384 464 PK----LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF------------PPLPREGTSSSS 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 649 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 728
Cdd:cd01384 528 KFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRF 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 153791586 729 KVLnASAIPEGQFiDSKKASEKLLASIDIDhtQYKFGHTKVFFK 772
Cdd:cd01384 608 GLL-APEVLKGSD-DEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
101-772 |
4.78e-172 |
|
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: 539.36 E-value: 4.78e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVTAYRGKKRQEAPPHIFSISDNAY-QFM---LTDRENQSI 175
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtQLIqsgVLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 176 LITGESGAGKTVNTKRVIQYFATIavTGEKKKEEITSG--------KIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARI--TSGFAQGASGEGeaaseaieQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 248 GKFIRIHFGTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGEISVASID 327
Cdd:cd14890 160 GKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 328 DQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGT-EVADKAAYLQSLNSADLLKALCYPR 406
Cdd:cd14890 239 DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 407 VKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 486
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 487 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-----KPmGIFSILEEECMFPKA-TDTSFKNKLYDQHL 560
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgkvngKP-GIFITLDDCWRFKGEeANKKFVSQLHASFG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 561 GKS------------ANFQKPKVvkgKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAmKTLAQLFSGAQ 628
Cdd:cd14890 477 RKSgsggtrrgssqhPHFVHPKF---DADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR-RSIREVSVGAQ 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 629 taegegagggakkggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGI 708
Cdd:cd14890 553 ----------------------------FRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAI 604
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791586 709 RICRKGFPSRILYADFKQRYKVLNASAipegqfiDSKKASEKLLASI-DIDHTQYKFGHTKVFFK 772
Cdd:cd14890 605 QIRQQGFALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKMlGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
103-772 |
7.79e-170 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 532.98 E-value: 7.79e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 182 GAGKTVNTKRVIQYFATIAvtgekkkeeitsGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01382 84 GAGKTESTKYILRYLTESW------------GSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 262 ASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLittnpydypfvsqgeiSVASIDDQEELMATDSAIDI 341
Cdd:cd01382 152 VGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 342 LGFTNEEKVSIYKLTGAVMHYGNLKFkqkqrEEQAEPD--GTEVADK-------AAYLQSLNSADLLKALCYpRVKVGNE 412
Cdd:cd01382 216 IGLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSggGCNVKPKseqsleyAAELLGLDQDELRVSLTT-RVMQTTR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 413 YVTKGQ------TVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQpRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 486
Cdd:cd01382 290 GGAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 487 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLgKSAN 565
Cdd:cd01382 369 KLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-NHFR 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 566 FQKPKvvKGKAEAH--------FALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGG 637
Cdd:cd01382 447 LSIPR--KSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSKQK 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 638 GAKKggkkkgsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPS 717
Cdd:cd01382 525 AGKL-------SFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPS 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 153791586 718 RILYADFKQRYKVLNASAIPEgqfIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd01382 598 RTSFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
852-1929 |
9.73e-167 |
|
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: 539.38 E-value: 9.73e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 852 EKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTER 931
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 932 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQ 1011
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1012 TLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEF 1091
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1092 EISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNK 1171
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1172 KREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNL 1251
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1252 EKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKA 1331
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1332 KNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQAAEEHVE 1411
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1412 AVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIK 1491
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1492 NAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLEL 1571
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1572 NQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRN 1651
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1652 TQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLIN 1731
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1732 TKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLAL 1811
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1812 KGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEA 1891
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 153791586 1892 EEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVK 1929
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
100-772 |
2.18e-166 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 524.26 E-value: 2.18e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVTAYRgKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 179 GESGAGKTVNTKRVIQYFATIAVTGEKKKEEItsgkiqgtlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF--- 255
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSLV---------EAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFskl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 256 ------GTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITS-----------------------NKKPELIEMLLI 306
Cdd:cd14888 151 kskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 307 TT-NPYDYPFVSqGEISVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQA---EPDGTE 382
Cdd:cd14888 231 EPhLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 383 VADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIG 461
Cdd:cd14888 310 DLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 462 VLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPMGIFSILEEE 540
Cdd:cd14888 390 VLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 541 CMFPKATDTSFKNKLYDQHlgksANFQKPKVVKGKAEAhFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTL 620
Cdd:cd14888 469 CFVPGGKDQGLCNKLCQKH----KGHKRFDVVKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFI 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 621 AQLFSgaqtaegegAGGGAKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLR 700
Cdd:cd14888 544 SNLFS---------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLK 614
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791586 701 CNGVLEGIRICRKGFPSRILYADFKQRYKVLnasAIPEGQfidskkasekllasidIDHTQYKFGHTKVFFK 772
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRIL---LNGEGK----------------KQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
100-772 |
2.53e-165 |
|
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: 520.49 E-value: 2.53e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIAVTgekkkeeiTSGkiqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS--------TNG-----VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSnkKPELIEMLLITTNPyDYPFVSQGE-ISVASIDDQEELMATDSA 338
Cdd:cd14872 148 RICGASTENYLLEKSRVVYQIKGERNFHIFYQLLA--SPDPASRGGWGSSA-AYGYLSLSGcIEVEGVDDVADFEEVVLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 339 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEP----DGTEVADKAAYLQsLNSADLLKALCYPRVKVgneyv 414
Cdd:cd14872 225 MEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGstvaNRDVLKEVATLLG-VDAATLEEALTSRLMEI----- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 415 tKGQ-------TVEQVSNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 486
Cdd:cd14872 299 -KGCdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 487 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLyDQHLGKSAN 565
Cdd:cd14872 378 KLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAA-NQTHAAKST 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 566 FQKPKVvkGKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSgaqtaegegagggakKGGKK 645
Cdd:cd14872 456 FVYAEV--RTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP---------------PSEGD 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 646 KGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFK 725
Cdd:cd14872 519 QKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFL 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 153791586 726 QRYKVLNaSAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14872 599 KRYRFLV-KTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
100-772 |
1.14e-164 |
|
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: 519.33 E-value: 1.14e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 179 GESGAGKTVNTKRVIQYFATIAvtgekkkeeitSGKIQGTLEdQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA-----------GGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 259 GKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELiEMLLITTNPYDYPFvSQGEISVASIDDQEELMATDSA 338
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEE-RLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 339 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE--PDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd14903 227 LSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 417 GQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14903 307 PLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKgka 576
Cdd:cd14903 387 FKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR--- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 577 eAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGGKKKGSSF--QTVS 654
Cdd:cd14903 463 -TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALttTTVG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 655 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnas 734
Cdd:cd14903 542 TQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF--- 618
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 153791586 735 aIPEGQFIDSKKAS--EKLLASIDIDH-TQYKFGHTKVFFK 772
Cdd:cd14903 619 -LPEGRNTDVPVAErcEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
101-772 |
2.14e-162 |
|
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: 512.76 E-value: 2.14e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgkiqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTGK 260
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVNQRRNNLVTE------------QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 261 LASADIETYLLEKSRVVFQLKAERSYHIFYQI------TSNKKPELIEmllittnPYDYPFVSQG-EISVASIDDQEELM 333
Cdd:cd01387 149 IVGAITSQYLLEKSRIVTQAKNERNYHVFYELlaglpaQLRQKYGLQE-------AEKYFYLNQGgNCEIAGKSDADDFR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 334 ATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEpdGTEVADKA-----AYLQSLNSADLLKALCYPRVK 408
Cdd:cd01387 222 RLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQE--GVSVGSDAeiqwvAHLLQISPEGLQKALTFKVTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 409 VGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd01387 300 TRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 489 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQ 567
Cdd:cd01387 380 QYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYS 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 568 KPKVvkGKAEahFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGGKKKG 647
Cdd:cd01387 458 KPRM--PLPE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKGRFVTMK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 648 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 727
Cdd:cd01387 534 PRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDR 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 153791586 728 YKVLNASAIPEGQFIDSKKASEKLLASIDIDhTQYKFGHTKVFFK 772
Cdd:cd01387 614 YRCLVALKLPRPAPGDMCVSLLSRLCTVTPK-DMYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
103-772 |
6.53e-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: 512.69 E-value: 6.53e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESG 182
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 183 AGKTVNTKRVIQYFATIAVTGEkkkeeiTSGkiqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 262
Cdd:cd01385 84 SGKTESTNFLLHHLTALSQKGY------GSG-----VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 263 SADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGE-ISVASIDDQEELMATDSAIDI 341
Cdd:cd01385 153 GAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDcYTLEGEDEKYEFERLKQAMEM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 342 LGFTNEEKVSIYKLTGAVMHYGNLKFKQK--QREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd01385 232 VGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQL----DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 495
Cdd:cd01385 312 LPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 496 MFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKlYDQHLGKSANFQKPKvvkg 574
Cdd:cd01385 392 IFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ---- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 575 KAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKS---------------------------AMKTLAQlfSGA 627
Cdd:cd01385 466 VMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSssafvreligidpvavfrwavlraffrAMAAFRE--AGR 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 628 QTAEGEGAGGGAKKGGKK-------KGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLR 700
Cdd:cd01385 544 RRAQRTAGHSLTLHDRTTksllhlhKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLR 623
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791586 701 CNGVLEGIRICRKGFPSRILYADFKQRYKVLnasaIPEGQfIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd01385 624 YTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-772 |
1.81e-160 |
|
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: 506.81 E-value: 1.81e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIavtgekkkeeitsGKIQ-GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVL-------------GKANnRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 259 GKLASADIETYLLEKSRVVFQLKAERSYHIFYQI----TSNKKpeLIEMLLITTNPYDYPFVSQGEISVASIDD--QEEL 332
Cdd:cd01379 148 GAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIyaglAEDKK--LAKYKLPENKPPRYLQNDGLTVQDIVNNSgnREKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 333 MATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQ----AEPDGTEVADKAAYLQSLNSADLLKALCYPRVK 408
Cdd:cd01379 226 EEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 409 VGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQP---RQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd01379 306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSasdEPLSIGILDIFGFENFQKNSFEQLCINIAN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 486 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFG-----MDLaacieLIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHl 560
Cdd:cd01379 386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 561 gKSANFQKPKvvkgKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAqlfsgaqtaegegagggak 640
Cdd:cd01379 460 -KSKYYWRPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 641 kggkkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 720
Cdd:cd01379 516 ----------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRIL 585
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 153791586 721 YADFKQRYKVL--NASAIPEGqfidSKKASEKLLASIDIDHtqYKFGHTKVFFK 772
Cdd:cd01379 586 FADFLKRYYFLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
100-770 |
1.46e-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: 502.40 E-value: 1.46e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAY------RGKKRQEAPPHIFSISDNAYQFMLTDRE-- 171
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 172 --NQSILITGESGAGKTVNTKRVIQYFAtiAVTGEKKKEEitSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLA--SVSSATTHGQ--NATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 250 FIRIHFGTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNP-YDYPFVSQGEISVASIDD 328
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEeYKYLNSSQCYDRRDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 329 QEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAY-LQSLNSADLLKALCYPRV 407
Cdd:cd14901 237 SVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 408 KVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 486 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSA 564
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 565 NFQKPKVVKGKAEahFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAqlfsgaqtaegegagggakkggk 644
Cdd:cd14901 475 SFSVSKLQQGKRQ--FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS----------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 645 kkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 724
Cdd:cd14901 530 ------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAF 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 153791586 725 KQRYKVLNAS------AIPEGQFIDSKKASEKLLASIDIDHTQykFGHTKVF 770
Cdd:cd14901 604 VHTYSCLAPDgasdtwKVNELAERLMSQLQHSELNIEHLPPFQ--VGKTKVF 653
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
106-772 |
1.68e-155 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 493.89 E-value: 1.68e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKpevVTAYRGKKRQEA-----PPHIFSISDNAYQFMLTDR----ENQSI 175
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYD---VPGFDSQRKEEAtasspPPHVFSIAERAYRAMKGVGkgqgTPQSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 176 LITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14892 84 VVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 256 GTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKpELIEMLLITTNPYDYPFVSQGE-ISVASIDDQEELMA 334
Cdd:cd14892 164 NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGNcVEVDGVDDATEFKQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 335 TDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVAD--KAAYLQSLNSADLLKALCYpRVKVGne 412
Cdd:cd14892 243 LRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFKLVT-QTTST-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 413 yvTKGQTVE------QVSNAVGALAKAVYEKMFLWMVARIN----QQL------DTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:cd14892 320 --ARGSVLEikltarEAKNALDALCKYLYGELFDWLISRINachkQQTsgvtggAASPTFSPFIGILDIFGFEIMPTNSF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFP-KATDTSFKNK 554
Cdd:cd14892 398 EQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 555 LYDQHLGKSANFQKPKVvkgkAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMktlaqlfsgaqtaegeg 634
Cdd:cd14892 477 YHQTHLDKHPHYAKPRF----ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK----------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 635 agggakkggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKG 714
Cdd:cd14892 536 ----------------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREG 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791586 715 FPSRILYADFKQRYKVL-------NASAIPEGQFIDSKKASEKLLASIDIDHTQykFGHTKVFFK 772
Cdd:cd14892 594 FPIRRQFEEFYEKFWPLarnkagvAASPDACDATTARKKCEEIVARALERENFQ--LGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
101-772 |
8.31e-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: 492.00 E-value: 8.31e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIAvtgeKKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVIS----QQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQ-GEISVASIDDQEELMATDSA 338
Cdd:cd14873 158 NIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 339 IDILGFTNEEKVSIYKLTGAVMHYGNLKFkqkqreeqAEPDGTEVADK-----AAYLQSLNSADLLKALCYPRVKVGNEY 413
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLRGEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 414 VTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQyFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14873 309 ILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 494 HHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKVvk 573
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPRV-- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 574 gkAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGGKkkgssfQTV 653
Cdd:cd14873 464 --AVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRR------PTV 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 654 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL-N 732
Cdd:cd14873 536 SSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLmR 615
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 153791586 733 ASAIPEgqfiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14873 616 NLALPE----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-772 |
3.22e-148 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 473.41 E-value: 3.22e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKK-RQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 181 SGAGKTVNTKRVIQYFATIavtgekkkeeitSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKL------------SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 261 LASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEEL-----MAT 335
Cdd:cd14897 151 LLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELeyyrqMFH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 336 DSaIDIL---GFTNEEKVSIYKLTGAVMHYGNLKFkqkqrEEQAEPDGTEVADK-----AAYLQSLNSADLLKALCYPRV 407
Cdd:cd14897 230 DL-TNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 408 KVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYF-----IGVLDIAGFEIFDFNSLEQLCIN 482
Cdd:cd14897 304 TIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCIN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 483 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDqHLG 561
Cdd:cd14897 384 LSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNK-YCG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 562 KSANFQKPKvvKGKAEahFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFsgaqtaegegagggakk 641
Cdd:cd14897 462 ESPRYVASP--GNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF----------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 642 ggkkkgssfqtvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILY 721
Cdd:cd14897 521 ------------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKY 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791586 722 ADFKQRYKVLnasaipegqFIDSKKASE-KLLASIDIDHTQ----YKFGHTKVFFK 772
Cdd:cd14897 589 EDFVKRYKEI---------CDFSNKVRSdDLGKCQKILKTAgikgYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
102-731 |
8.04e-146 |
|
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: 466.32 E-value: 8.04e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVTAY-----------RGKKRQEAPPHIFSISDNAYQFM--- 166
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 167 -LTDRENQSILITGESGAGKTVNTKRVIQYFATiaVTGEKKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQ--AGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 246 RFGKFIRIHFGTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYqitsnkkpeliEMLLittnpydypfvSQGEISVAS 325
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFY-----------EMAI-----------GASEAARKR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 326 iDDQEELMAtdsAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVA-------DKAAYLQSLNSADL 398
Cdd:cd14900 219 -DMYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 399 LKALCYPRVKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQL-----DTKQPRQYFIGVLDIAGFEIFDF 473
Cdd:cd14900 295 EKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 474 NSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFK 552
Cdd:cd14900 375 NSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 553 NKLYdQHLGKSANFQKPKVVKGKaeAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQksamktlaqlfSGAQtaeg 632
Cdd:cd14900 454 SKLY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV-----------YGLQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 633 egagggakkggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICR 712
Cdd:cd14900 516 ------------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVAR 571
|
650
....*....|....*....
gi 153791586 713 KGFPSRILYADFKQRYKVL 731
Cdd:cd14900 572 AGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-772 |
2.69e-141 |
|
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: 455.26 E-value: 2.69e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVTAYRG--KKRQEA------PPHIFSISDNAYQFMLTDREN 172
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiIQNGEYfdikkePPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 173 QSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEIT-------SGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTltssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 246 RFGKFIRIHFG-TTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYP--FVSQGEIS 322
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDRydYLKKSNCY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 323 -VASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQ--REEQAEPDGTEVADKAAYLQSLNSADLL 399
Cdd:cd14907 243 eVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 400 KALCYPRVKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQL--------DTKQPRQYFIGVLDIAGFEIF 471
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 472 DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF--IDFgMDLAACIELIEK-PMGIFSILEEECMFPKATD 548
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 549 TSFKNKLYDQHlgksANFQKPKVVKGKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGaq 628
Cdd:cd14907 482 EKLLNKIKKQH----KNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSG-- 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 629 taeGEGAGGGAKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGI 708
Cdd:cd14907 556 ---EDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESI 632
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791586 709 RICRKGFPSRILYADFKQRYKVLNasaipegqfidskkasekllasididhTQYKFGHTKVFFK 772
Cdd:cd14907 633 RVRKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
100-772 |
1.94e-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: 449.78 E-value: 1.94e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 179 GESGAGKTVNTKRVIQYFATIAvtGEKKKEEItsgkiqgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA--GGRKDKTI----------AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 259 GKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSN-KKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDS 337
Cdd:cd14904 149 GKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 338 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVAdKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 417
Cdd:cd14904 229 SLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLS-QVAKMLGLPTTRIEEALCNRSVVTRNESVTVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 418 QTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14904 308 LAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQH--LGKSANFQKPKVVKg 574
Cdd:cd14904 388 FKTVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 575 kaeAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQtaegeGAGGGAKKGGKKKGSSFQTVS 654
Cdd:cd14904 466 ---TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE-----APSETKEGKSGKGTKAPKSLG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 655 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 734
Cdd:cd14904 538 SQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPP 617
|
650 660 670
....*....|....*....|....*....|....*....
gi 153791586 735 AIPEGqfiDSKKASEKLLASIDIDHT-QYKFGHTKVFFK 772
Cdd:cd14904 618 SMHSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
102-772 |
1.03e-137 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 445.12 E-value: 1.03e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFML----TDRENQSILI 177
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 178 TGESGAGKTVNTKRVIQYFAtiavtgekkkeEITSGKIQgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgT 257
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIM-----------ELCRGNSQ--LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-R 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 258 TGKLASADIETYLLEKSRVVFQLKAERSYHIFYQI---TSNKKPELIEMLlittNPYDYPFVSQGEisvasidDQEELMA 334
Cdd:cd14889 149 NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNGA-------GCKREVQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 335 T--------DSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREE-QAEPDGTEVADKAAYLQSLNSADLLKALCYP 405
Cdd:cd14889 218 YwkkkydevCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 406 RVKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLdtkQPRQYF------IGVLDIAGFEIFDFNSLEQL 479
Cdd:cd14889 298 VTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 480 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLyDQH 559
Cdd:cd14889 375 CINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKL-NIH 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 560 LGKSANFqkpKVVKGKAEAhFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGA 639
Cdd:cd14889 454 FKGNSYY---GKSRSKSPK-FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAK 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 640 KKGGKKK---GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 716
Cdd:cd14889 530 LPQAGSDnfnSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFS 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791586 717 SRILYADFKQRYKVLnasaIPEGQFIDSKKASEKLLASIDIdhTQYKFGHTKVFFK 772
Cdd:cd14889 610 WRPSFAEFAERYKIL----LCEPALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
24-831 |
1.43e-133 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 439.08 E-value: 1.43e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 24 RIEAQNRPFDAKTSVFV-------------AEPKESFVKGTIQ-SREGGKVTVK---TEGGATLTVKDDQVF----PMNP 82
Cdd:PTZ00014 16 RRNSNVEAFDKSGNVLKgfyvwtdkapavkEDPDLMFAKCLVLpGSTGEKLTLKqidPPTNSTFEVKPEHAFnansQIDP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 83 PKYDkieDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYR-GKKRQEAPPHIFSISDN 161
Cdd:PTZ00014 96 MTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 162 AYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATiAVTGEkkkeeiTSGKIQGTledqIISANPLLEAFGNAKTVRN 241
Cdd:PTZ00014 173 ALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS-SKSGN------MDLKIQNA----IMAANPVLEAFGNAKTIRN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 242 DNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEI 321
Cdd:PTZ00014 242 NNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSLEEYKYINPKCL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 322 SVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-----PDGTEVADKAAYLQSLNSA 396
Cdd:PTZ00014 321 DVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDaaaisDESLEVFNEACELLFLDYE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 397 DLLKALCYPRVKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:PTZ00014 401 SLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGI-----EWTfidfgmDLAACIELI-EKPMGIFSILEEECMFPKATDTS 550
Cdd:PTZ00014 481 EQLFINITNEMLQKNFVDIVFERESKLYKDEGIsteelEYT------SNESVIDLLcGKGKSVLSILEDQCLAPGGTDEK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 551 FKNKLYDQhLGKSANFQKPKVVKGKaeaHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTA 630
Cdd:PTZ00014 555 FVSSCNTN-LKNNPKYKPAKVDSNK---NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVE 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 631 EGEGAGGgakkggkkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRI 710
Cdd:PTZ00014 631 KGKLAKG-------------QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQL 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 711 CRKGFPSRILYADFKQRYKVLNAsAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDDKLAQ- 789
Cdd:PTZ00014 698 RQLGFSYRRTFAEFLSQFKYLDL-AVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAw 776
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 153791586 790 --LITRTQArcrgFLARVEYQRMVERR-EAIFCIQYNIRSFMNVK 831
Cdd:PTZ00014 777 epLVSVLEA----LILKIKKKRKVRKNiKSLVRIQAHLRRHLVIA 817
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
100-772 |
3.42e-132 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 429.08 E-value: 3.42e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAA--WMIYTYSGLFCVTVNPYKWLPvyKPEVvTAYRGKKRQEAPPHIFSISDNAYQFMLTDRE---NQS 174
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 175 ILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKIQG------TLEDQIISANPLLEAFGNAKTVRNDNSSRFG 248
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 249 KFIRIHFGTTG-KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQ-GEISVASI 326
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLL-LSPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 327 DDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREE----QAEPDGTEVADKAAYLQSLNSADLLKAL 402
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 403 CYPRVKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFD-FNSLEQLCI 481
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 482 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHl 560
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 561 GKSANFQKPKvVKGKAEAhFALIHYAGVVDYNITGWLEKNKDplnetvvglyqksamkTLAQLFsgaqtaegegagggak 640
Cdd:cd14891 475 KRHPCFPRPH-PKDMREM-FIVKHYAGTVSYTIGSFIDKNND----------------IIPEDF---------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 641 kggkkkgSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 720
Cdd:cd14891 521 -------EDLLASSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVT 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791586 721 YADFKQRYKVLNASAI------PEGQFIdskkasEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14891 594 YAELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
100-772 |
1.32e-131 |
|
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: 428.94 E-value: 1.32e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYR--GKKRQ---EAP----PHIFSISDNAYQFMLTD- 169
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKiQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELG-KLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 250 FIRIHFGTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQI------TSNKKPELIEMLLITTN-PYDYPFVSQGEI- 321
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLlrggdeEEHEKYEFHDGITGGLQlPNEFHYTGQGGAp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 322 SVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQRE---EQAEPDGTEVADKAAYLQSLNSADL 398
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDgaaEIAEEGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 399 LKALCYPRVKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNK 554
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 555 LYDQHL-------GKSANFQKPKVVKGKaeAHFALIHYAGVVDYNI-TGWLEKNKDPLNETVVGLYQksamktlaqlfSG 626
Cdd:cd14908 479 LYETYLpeknqthSENTRFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFE-----------SG 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 627 AQtaegegagggakkggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLE 706
Cdd:cd14908 546 QQ----------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLE 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 707 GIRICRKGFPSRILYADFKQRYKVLnASAIPE----------------GQFIDSKKA----SEKLLASIDIDHTQYKFGH 766
Cdd:cd14908 598 AVRVARSGYPVRLPHKDFFKRYRML-LPLIPEvvlswsmerldpqklcVKKMCKDLVkgvlSPAMVSMKNIPEDTMQLGK 676
|
....*.
gi 153791586 767 TKVFFK 772
Cdd:cd14908 677 SKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
100-729 |
4.97e-130 |
|
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: 425.46 E-value: 4.97e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP---------VYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFML-TD 169
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdlysesqlnAYKASMTSTSPVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKIQGTledQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVEIGK---RILQTNPILESFGNAQTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 250 FIRIHFGTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEmLLITTNPYDYPFVSQGEISVA----- 324
Cdd:cd14902 158 FIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD-LLGLQKGGKYELLNSYGPSFArkrav 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 325 SIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKqkqrEEQAEPDGTEVA-------DKAAYLQSLNSAD 397
Cdd:cd14902 237 ADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFT----AENGQEDATAVTaasrfhlAKCAELMGVDVDK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 398 LLKALCYPRVKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLD-------TKQPRQYF--IGVLDIAGF 468
Cdd:cd14902 313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsISDEDEELatIGILDIFGF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 469 EIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKAT 547
Cdd:cd14902 393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 548 DTSFKNKLYDQHLGksanfqkpkvvkgkaEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLaQLFSGA 627
Cdd:cd14902 472 NQALSTKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVV-VAIGAD 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 628 QTAEGEGAGGGAKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEG 707
Cdd:cd14902 536 ENRDSPGADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEA 615
|
650 660
....*....|....*....|..
gi 153791586 708 IRICRKGFPSRILYADFKQRYK 729
Cdd:cd14902 616 VRIARHGYSVRLAHASFIELFS 637
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-772 |
5.07e-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: 408.19 E-value: 5.07e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKpevVTAYRGK--KRQEAPPHIFSISDNAYQFMLT-------D 169
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 170 RENQSILITGESGAGKTVNTKRVIQYfatIAVTGEKKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNY---LAESSKHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 250 FIRIHFG-----TTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPE-LIEMLLITTNPYDYPFVSQGEISV 323
Cdd:cd14895 155 FVRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGGQCYQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 324 AS--IDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVA----------------- 384
Cdd:cd14895 235 RNdgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqh 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 385 -DKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQY----- 458
Cdd:cd14895 315 lDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 459 ------FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPM 531
Cdd:cd14895 395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 532 GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKvvKGKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGL 611
Cdd:cd14895 474 GIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 612 YQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGGKKKGS-SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAM 690
Cdd:cd14895 551 LGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVlSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQF 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 691 EHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASaipegQFIDSKKASEkLLASIDIDHTQykFGHTKVF 770
Cdd:cd14895 631 DMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAA-----KNASDATASA-LIETLKVDHAE--LGKTRVF 702
|
..
gi 153791586 771 FK 772
Cdd:cd14895 703 LR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
100-772 |
9.21e-124 |
|
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: 405.53 E-value: 9.21e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRG-KKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 179 GESGAGKTVNTKRVIQYFATiavtgekKKEEITSGKIQgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS-------AKSGNMDLRIQ----TAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 259 GKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGEISVASIDDQEELMATDSA 338
Cdd:cd14876 150 GGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLG-LKEYKFLNPKCLDVPGIDDVADFEEVLES 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 339 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQ-----AEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEY 413
Cdd:cd14876 229 LKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 414 VTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14876 309 IEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 494 HHMFVLEQEEYKKEGI-----EWTfidfgmDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSANFQ 567
Cdd:cd14876 389 DIVFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSNGKFK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 568 KPKVvkgKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGgakkggkkkg 647
Cdd:cd14876 462 PAKV---DSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKG---------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 648 ssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 727
Cdd:cd14876 529 ---SLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQ 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 153791586 728 YKVLNAsAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14876 606 FKFLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
100-772 |
1.43e-119 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 393.38 E-value: 1.43e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIavtgEKKKEEITSGKIQGTLedqiisanPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 259
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----YQDQTEDRLRQPEDVL--------PILESFGHAKTILNANASRFGQVLRLHL-QHG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEI-SVASIDDQEELMATDSA 338
Cdd:cd14896 148 VIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 339 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQ---AEPDGTEVADKAAYLQSlnSADLLKALCYPRVKVGN-EYV 414
Cdd:cd14896 227 LQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevaAVSSWAEIHTAARLLQV--PPERLEGAVTHRVTETPyGRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 415 TKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYF--IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 492
Cdd:cd14896 305 SRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 493 NHHMFVLEQEEYKKEGIEWTFIDfGMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKV 571
Cdd:cd14896 385 SQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 572 vkgkAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGakkggkkkgssfq 651
Cdd:cd14896 463 ----PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP------------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 652 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 731
Cdd:cd14896 526 TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL 605
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 153791586 732 NASAIPEgqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14896 606 GSERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-731 |
5.17e-113 |
|
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: 374.96 E-value: 5.17e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVTAYRGKKR-QEAPPHIFSISDNAYQFMLTDRE--NQSILI 177
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 178 TGESGAGKTVNTKRVIQYFATIAVTgekkKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 257
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAAS----PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 258 TGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSN-KKPELIEMLLitTNPYDYPFVSQGEISVasidDQEELMATD 336
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGaSADERLQWHL--PEGAAFSWLPNPERNL----EEDCFEVTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 337 SAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQA---EPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEY 413
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 414 VT--KGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPR-QYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 490
Cdd:cd14880 313 QVfkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 491 FFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKP 569
Cdd:cd14880 393 HFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 570 KVVKgkaEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQtaegegAGGGAKKGGKKKGSS 649
Cdd:cd14880 472 KLSR---EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANP------EEKTQEEPSGQSRAP 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 650 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 729
Cdd:cd14880 543 VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
..
gi 153791586 730 VL 731
Cdd:cd14880 623 LL 624
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-734 |
2.52e-108 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 363.53 E-value: 2.52e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVTAYRGKKR-QEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFatIAVTGEKKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTT 258
Cdd:cd14906 83 ESGSGKTEASKTILQYL--INTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 259 GKLASADIETYLLEKSRVVFQL-KAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQ-------- 329
Cdd:cd14906 161 GKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFKSQssnknsnh 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 330 -------EELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQ---REEQAEPDGTEVADKAAYLQSLNSADLL 399
Cdd:cd14906 241 nnktesiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 400 KALCYPRVKVGNE--YVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARIN----QQLDTKQPRQY-------FIGVLDIA 466
Cdd:cd14906 321 QALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINrkfnQNTQSNDLAGGsnkknnlFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 467 GFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPK 545
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 546 ATDTSFKNKLYDQHLGKSANFQKPkvvkgKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFS 625
Cdd:cd14906 480 GSEQSLLEKYNKQYHNTNQYYQRT-----LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 626 GAQTaegegagggAKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVL 705
Cdd:cd14906 555 QQIT---------STTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVL 625
|
650 660
....*....|....*....|....*....
gi 153791586 706 EGIRICRKGFPSRILYADFKQRYKVLNAS 734
Cdd:cd14906 626 NTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
101-729 |
3.59e-108 |
|
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: 363.26 E-value: 3.59e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVTAY----------RGKKRQEAPPHIFSISDNAYQFMLTD 169
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKI-----QGTLEDQIISANPLLEAFGNAKTVRNDNS 244
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPpaspsRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 245 SRFGKFIRIHF-GTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNK----KPELIEMLLITTNPYDYPFVSQG 319
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 320 EISVA--SIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQ--KQREEQAEPDGTEVA----------D 385
Cdd:cd14899 242 LCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 386 KAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQL--------------- 450
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 451 DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-K 529
Cdd:cd14899 402 DDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 530 PMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVV 609
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 610 GLYQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGGKKKGSSFQTVSAL-----FRENLNKLMTNLRSTHPHFVRCIIPNET 684
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVsvgtqFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 153791586 685 KTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 729
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-772 |
9.59e-105 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 351.42 E-value: 9.59e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 102 VLYNLKERYAAWMI-YTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEA-PPHIFSISDNAY-QFMLTDRENQSILIT 178
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 179 GESGAGKTVNTKRVIQYFAtiavtgeKKKEEITSGKIQGTLEDQIIS----ANPLLEAFGNAKTVRNDNSSRFGKFIRIH 254
Cdd:cd14875 83 GESGSGKTENAKMLIAYLG-------QLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 255 F-GTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISV------ASID 327
Cdd:cd14875 156 FdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 328 DQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQsLNSADLLKalCYpRV 407
Cdd:cd14875 236 DAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFLTACRLLQ-LDPAKLRE--CF-LV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 408 KVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQ----QLDTKQPRqyFIGVLDIAGFEIFDFNSLEQLCINF 483
Cdd:cd14875 312 KSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNAsitpQGDCSGCK--YIGLLDIFGFENFTRNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 484 TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGK 562
Cdd:cd14875 390 ANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 563 SANFQKPkvvKGKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGagggakkg 642
Cdd:cd14875 469 SPYFVLP---KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRK-------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 643 gkkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 722
Cdd:cd14875 538 --------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIE 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 153791586 723 DF-KQRYKVLNASAIPEGQFIDSKKASEKLLAS----IDIDHTQYKFGHTKVFFK 772
Cdd:cd14875 610 QFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
106-772 |
3.41e-102 |
|
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: 343.41 E-value: 3.41e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVTAYRGKKRQ-----EAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYFATIAVTGEKKkeeitsgkiqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTD------------VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYdYPFVSQGEISVA-SIDDQEELMATDSA 338
Cdd:cd14886 155 GLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASKCYDApGIDDQKEFAPVRSQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 339 IDILgFTNEEKVSIYKLTGAVMHYGNLKFKQKQR---EEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 415
Cdd:cd14886 234 LEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETII 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 416 KGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 495
Cdd:cd14886 313 SPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 496 MFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLyDQHLgKSANFqkpkvVKG 574
Cdd:cd14886 393 VFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF-----IPG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 575 K-AEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGggakkggkkkgssfQTV 653
Cdd:cd14886 465 KgSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKG--------------KFL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 654 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL-- 731
Cdd:cd14886 531 GSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILis 610
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 153791586 732 -NASAIPEGQfiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14886 611 hNSSSQNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-772 |
2.25e-100 |
|
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: 339.67 E-value: 2.25e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 182 GAGKTVNTKRVIQYFATIAVTGEKKkeeITSGKIQgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAGSVGGV---LSVEKLN--------AALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 262 ASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFvsqGEISVASIDD----QEELMATDS 337
Cdd:cd01386 152 ASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF---GIVPLQKPEDkqkaAAAFSKLQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 338 AIDILGFTNEEKVSIYKLTGAVMHYGN---LKFKQKQREEQAEPdgtEVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 414
Cdd:cd01386 229 AMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 415 TKGQTVEQVSN------------AVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 476
Cdd:cd01386 306 TTSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrgaTF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---------------PMGIFSILEEEC 541
Cdd:cd01386 386 EDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLDEEA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 542 MFPKATDTSFKNKLYdQHLGKSANFQKPKVVKgKAEA--HFALIHYAGV--VDYNITGWLEKNK-DPLNETVVGLYQKSA 616
Cdd:cd01386 466 LYPGSSDDTFLERLF-SHYGDKEGGKGHSLLR-RSEGplQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQESQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 617 MKTLAQLFSGaqtaegegagggakkggkkkgssfqtVSALFRENLNKLMTNLRSTHPHFVRCIIPN------ETKTPGAM 690
Cdd:cd01386 544 KETAAVKRKS--------------------------PCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPA 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 691 EHELVLH------QLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL----NASAIPEGQFIDSKKASEKLLASIDIDHT 760
Cdd:cd01386 598 AGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLapplTKKLGLNSEVADERKAVEELLEELDLEKS 677
|
730
....*....|..
gi 153791586 761 QYKFGHTKVFFK 772
Cdd:cd01386 678 SYRIGLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
101-772 |
1.30e-92 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 315.99 E-value: 1.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYR---GKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 177
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 178 TGESGAGKTVNTKRVIQYFATiavtgekkkeeiTSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 257
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTC------------RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 258 TGK-LASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGE----ISVASIDDQEEL 332
Cdd:cd14878 150 RKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTMredvSTAERSLNREKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 333 MATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNE 412
Cdd:cd14878 229 AVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 413 YVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARIN----QQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14878 309 MIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclqSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 489 QQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQ 567
Cdd:cd14878 389 HHYINEVLFLQEQTECVQEGVTMeTAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 568 KPKVVKGKAE-------AHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFsgaqtaegegagggak 640
Cdd:cd14878 469 YSPMKDGNGNvalkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF---------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 641 kggkkkGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 720
Cdd:cd14878 533 ------QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLS 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 153791586 721 YADFKQRYKVLnASAIPEGQfidsKKASEKLLASIDIDHTQ---YKFGHTKVFFK 772
Cdd:cd14878 607 FSDFLSRYKPL-ADTLLGEK----KKQSAEERCRLVLQQCKlqgWQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
101-735 |
5.94e-91 |
|
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: 308.36 E-value: 5.94e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvykpEVVTAYRGKKRQE-----APPHIFSISDNAYQFMLTdRENQSI 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPY--------ETIYGAGAMKAYLknyshVEPHVYDVAEASVQDLLV-HGNQTI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 176 LITGESGAGKTVNTKRVIQYFatiaVTGEKKKEEItsgkiqgtlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14898 73 VISGESGSGKTENAKLVIKYL----VERTASTTSI---------EKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 256 gtTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKpeliemLLITTNPYDYPFVSQGEISVasIDDQEELMAT 335
Cdd:cd14898 140 --DGKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 336 DSAIDILGFTNEEkvSIYKLTGAVMHYGNLKFKQkqrEEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 415
Cdd:cd14898 210 CSAMKSLGIANFK--SIEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 416 KGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQyfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 495
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 496 MFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKAT--DTSFKNKLYDQHLgksanfqkpkvVK 573
Cdd:cd14898 363 MFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNGF-----------IN 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 574 GKAEAHFALIHYAGVVDYNITGWLEKNKdplnetvvglyQKSAMKTLAQLFsgaqtaegegagggakkggKKKGSSFQTV 653
Cdd:cd14898 431 TKARDKIKVSHYAGDVEYDLRDFLDKNR-----------EKGQLLIFKNLL-------------------INDEGSKEDL 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 654 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 733
Cdd:cd14898 481 VKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI 560
|
..
gi 153791586 734 SA 735
Cdd:cd14898 561 TL 562
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-772 |
3.41e-89 |
|
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: 305.40 E-value: 3.41e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEvvtaYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 182 GAGKTVNTKRVIQYFatiaVTGEKKKEEITSgkiqgTLEDqiisANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14937 79 GSGKTEASKLVIKYY----LSGVKEDNEISN-----TLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 262 ASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPyDYPFVSQGEISVASIDDQEELMATDSAIDI 341
Cdd:cd14937 146 VSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 342 LGFTNEEKVSIYKLTGAVMhYGNLKFKQ-----KQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd14937 225 MNMHDMKDDLFLTLSGLLL-LGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 417 GQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 497 FVLEQEEYKKEGIEWTFIDFGMDlAACIELIEKPMGIFSILEEECMFPKATDTSfknkLYDQHLGKSANFQKPKVVKGKA 576
Cdd:cd14937 384 YEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKYASTKKDI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 577 EAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGggakkggkkkgssfQTVSAL 656
Cdd:cd14937 459 NKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK--------------NLITFK 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 657 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRIcRKGFPSRILYADFKQRYKVLNASAI 736
Cdd:cd14937 525 YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTS 603
|
650 660 670
....*....|....*....|....*....|....*.
gi 153791586 737 PEGQFIDSKKASEKLLASIDIDhtQYKFGHTKVFFK 772
Cdd:cd14937 604 KDSSLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
100-772 |
1.17e-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: 303.49 E-value: 1.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAA--------WMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRE 171
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 172 NQSILITGESGAGKTVNTKRVIQYFAtiAVTGEKKkeeitsGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 251
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLA--AVSDRRH------GADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKML 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 252 RIHFGTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITtnpYDYPFVSqgeisvasidDQEE 331
Cdd:cd14887 153 LLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAG---EGDPEST----------DLRR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 332 LMATDSAIDILGFTNEEkvsIYKLTGAVMHYGNLKFKQKQREEQAEPDGT--------EVADK---AAYLQSLNS----- 395
Cdd:cd14887 220 ITAAMKTVGIGGGEQAD---IFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADrshSSEVKCLSSglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 396 -------ADLLKALCYPRVKVGNEYV------------TKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPR 456
Cdd:cd14887 297 easrkhlKTVARLLGLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 457 QY--------------FIGVLDIAGFEIF---DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFI----D 515
Cdd:cd14887 377 SEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsafP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 516 FGMDLAAC--------IELIEKP--------------MGIFSILEEE-CMFPKATDTSFKNKLYDQHLGK----SANFQK 568
Cdd:cd14887 457 FSFPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKN 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 569 PKVVKGKAEAHFALIHYAGVVDYNITGWLEKNKDPLNEtvvglyqksamkTLAQLFSGAQTaEGEGAGGGAKKGGKKKGS 648
Cdd:cd14887 537 ITPALSRENLEFTVSHFACDVTYDARDFCRANREATSD------------ELERLFLACST-YTRLVGSKKNSGVRAISS 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 649 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 728
Cdd:cd14887 604 RRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRY 683
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 153791586 729 KVLNASAIPEgqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 772
Cdd:cd14887 684 ETKLPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
106-771 |
7.46e-84 |
|
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: 289.84 E-value: 7.46e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 106 LKERYAAWMIYTY---SGLfcVTVNPYKWLPVYKPEVVTAYR-------GKKRQEAPPHIFSISDNAYQFMLTDRENQSI 175
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 176 LITGESGAGKTVNTKRVIQYFATIAVTGekKKEEITSGKIQgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSSHS--KKGTKLSSQIS--------AAEFVLDSFGNAKTLTNPNASRFGRYTELQF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 256 GTTGKLASADIETYLLEKSRVVfQLKA-ERSYHIFYQITSNKKPELIEMLLITTNP-YDYPFVSQG--EISVASIDDQE- 330
Cdd:cd14879 158 NERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGLDDPSdYALLASYGChpLPLGPGSDDAEg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 331 --ELMAtdsAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQ--REEQAEPDGTEVADKAAYLQSLNSADLLKALCYPR 406
Cdd:cd14879 237 fqELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 407 VKVGNEYVTkgqtveqVS-NAVGA------LAKAVYEKMFLWMVARINQQL-DTKQPRQYFIGVLDIAGFEIFD---FNS 475
Cdd:cd14879 314 KLVRKELCT-------VFlDPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSstgGNS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 476 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEEC-MFPKATDTSFKN 553
Cdd:cd14879 387 LDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDEQMLE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 554 KLYDQHLGKSANFQKPKVVKGKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVglyqksamktlaQLFSGAQTaege 633
Cdd:cd14879 466 ALRKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFV------------NLLRGATQ---- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 634 gagggakkggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRK 713
Cdd:cd14879 530 -----------------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRV 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791586 714 GFPSRILYADFKQRYKvlnasaiPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFF 771
Cdd:cd14879 587 EYVVSLEHAEFCERYK-------STLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
100-720 |
2.03e-76 |
|
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: 269.47 E-value: 2.03e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVTAYRGKKRQEA-------PPHIFSISDNAYQFMLTDRE 171
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 172 NQSILITGESGAGKTVNTKRVIQYFatiavtgekkkEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 251
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYF-----------HYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRIN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 252 RIHFGT---------TGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGE-- 320
Cdd:cd14884 150 LLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEsh 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 321 ----------ISVASIDDQEELMATDSA-----IDILGFTNEEKVSI---YKLTGAVMHYGNLKFKQkqreeqaepdgte 382
Cdd:cd14884 230 qkrsvkgtlrLGSDSLDPSEEEKAKDEKnfvalLHGLHYIKYDERQInefFDIIAGILHLGNRAYKA------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 383 vadkAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARIN---------QQLDTK 453
Cdd:cd14884 297 ----AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekDESDNE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 454 QPRQY---FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDfgmdLAACIELIEKP 530
Cdd:cd14884 373 DIYSIneaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDV----APSYSDTLIFI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 531 MGIFSILEEECMFP----KATDTSFKNKLYD----QHLGK--SANFQKPKVVKGKAEAH------FALIHYAGVVDYNIT 594
Cdd:cd14884 449 AKIFRRLDDITKLKnqgqKKTDDHFFRYLLNnerqQQLEGkvSYGFVLNHDADGTAKKQnikkniFFIRHYAGLVTYRIN 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 595 GWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTaegegagggakkggkkkgSSFQTVSALFRENLNKLMTNLRSTHPH 674
Cdd:cd14884 529 NWIDKNSDKIETSIETLISCSSNRFLREANNGGNK------------------GNFLSVSKKYIKELDNLFTQLQSTDMY 590
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 153791586 675 FVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 720
Cdd:cd14884 591 YIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
101-754 |
9.01e-68 |
|
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: 242.33 E-value: 9.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPvyKPEVVTAYRGKKRQeapPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 181 SGAGKTVNTKRVI-QYFatiavtgekkkeEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 259
Cdd:cd14881 77 SGSGKTYASMLLLrQLF------------DVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKP-ELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSA 338
Cdd:cd14881 144 ALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQeERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 339 IDILG--FTNeekvsIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLqSLNSADLLKALcYPRVKVgneyvTK 416
Cdd:cd14881 224 LGILGipFLD-----VVRVLAAVLLLGNVQFIDGGGLEVDVKGETELKSVAALL-GVSGAALFRGL-TTRTHN-----AR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 417 GQTVEQV-----SNAV-GALAKAVYEKMFLWMVARINQQLD-----TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd14881 292 GQLVKSVcdanmSNMTrDALAKALYCRTVATIVRRANSLKRlgstlGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 486 EKLQQFFNHHMFVLEQEEYKKEGIEwTFIDFG-MDLAACIELIEK-PMGIFSILEEECMfPKATDTSFKNKLYDQHLGkS 563
Cdd:cd14881 372 ETMQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQ-N 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 564 ANFQKPKVVKGKAeahFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKtlaqlFsgaqtaegegagggakkgg 643
Cdd:cd14881 449 PRLFEAKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCN-----F------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 644 kkkgsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 723
Cdd:cd14881 502 -----GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKA 576
|
650 660 670
....*....|....*....|....*....|.
gi 153791586 724 FKQRYKVLnASAIPEGQFIDSKKASEKLLAS 754
Cdd:cd14881 577 FNARYRLL-APFRLLRRVEEKALEDCALILQ 606
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
102-772 |
1.44e-65 |
|
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: 236.18 E-value: 1.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 182 GAGKTVNTKRVIQYfatIAVTGEKKKEeiTSGKIQgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14882 83 YSGKTTNARLLIKH---LCYLGDGNRG--ATGRVE--------SSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 262 ASADIETYLLEKSRVVFQLKAERSYHIFYQI--TSNKKPELIEMLLITTNPYDY----PFVSQGEISVASIDDQEELMAT 335
Cdd:cd14882 150 SGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFydFIEAQNRLKEYNLKAGRNYRYlripPEVPPSKLKYRRDDPEGNVERY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 336 DSAIDIL---GFTNEEKVSIYKLTGAVMHYGNLKFKQKQREeqAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNE 412
Cdd:cd14882 230 KEFEEILkdlDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 413 YVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTkqPR-----QYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd14882 308 AERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVNTLNEQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 488 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEecmfpKATDTSFKNKLYDQHLGKSANFQ 567
Cdd:cd14882 386 MQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKEKHSQFV 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 568 KPkvvkgkAEAH-FALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEgegagggakkggkkk 646
Cdd:cd14882 461 KK------HSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQVRN--------------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 647 gssFQTVSALFR----ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 722
Cdd:cd14882 520 ---MRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQ 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 153791586 723 DFKQRYKVLnasAIPEGQFIDSKKASEKLLAsIDIDHTQYKFGHTKVFFK 772
Cdd:cd14882 597 EFLRRYQFL---AFDFDETVEMTKDNCRLLL-IRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
101-731 |
7.29e-65 |
|
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: 233.61 E-value: 7.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYrgkkrqeappHIFSISDNAYQFMLTDREN-QSILITG 179
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 180 ESGAGKTVNTKRVIQYfatiaVTGEKKKeeitsgKIQGTLEDQIISanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14874 72 ESGSGKSYNAFQVFKY-----LTSQPKS------KVTTKHSSAIES---VFKSFGCAKTLKNDEATRFGCSIDLLYKRNV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 260 KLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14874 138 LTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLEDAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKqREEQAEPDGTEVADKA-----AYLQSLNSADLLKALCyPRVKVGNEYv 414
Cdd:cd14874 217 HVLGFSDDHCISIYKIISTILHIGNIYFRTK-RNPNVEQDVVEIGNMSevkwvAFLLEVDFDQLVNFLL-PKSEDGTTI- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 415 tkgqTVEQVSNAVGALAKAVYEKMFLWMVARINQQLdtKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14874 294 ----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHL--KCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 494 HHMFVLEQEEYKKEGIEwtfIDFGM----DLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSAnFQK 568
Cdd:cd14874 368 KHSFHDQLVDYAKDGIS---VDYKVpnsiENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 569 pkvVKGKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFsgaqtaegegagggaKKGGKKKGS 648
Cdd:cd14874 444 ---ARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLF---------------ESYSSNTSD 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 649 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 728
Cdd:cd14874 506 MIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQY 585
|
...
gi 153791586 729 KVL 731
Cdd:cd14874 586 RCL 588
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
103-729 |
1.15e-64 |
|
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: 235.64 E-value: 1.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQ----------EAPPHIFSISDNAYQFMLTDREN 172
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 173 QSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIR 252
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 253 IHFGTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKK--PELIEMLLITTNPYDYPFVSQG--EISVASID- 327
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFALDa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 328 -DQEELMATDSAIDIlgfTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDG--TEVADKAAYL-----QSLNSADLL 399
Cdd:cd14893 244 rDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGAnsTTVSDAQSCAlkdpaQILLAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 400 KAlcYPRV------------KVGNEYVT--KGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQL----DTKQPRQYFIG 461
Cdd:cd14893 321 EV--EPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVIN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 462 -----VLDIAGFEIFD--FNSLEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEG--IEWTFIDFGMDLAACIELI 527
Cdd:cd14893 399 sqgvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 528 E-KPMGIFSILEEECMFPKATDTSFKNKLY--DQHLG------KSANFQKPKVVKGKA-EAHFALIHYAGVVDYNITGWL 597
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFsgNEAVGglsrpnMGADTTNEYLAPSKDwRLLFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 598 EKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGGKKKGSSFQTVSALFRENLN--------------K 663
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadA 638
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791586 664 LMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 729
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
106-715 |
2.91e-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: 2.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVTAYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 184
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 185 KTVNTKRVIQYFATIAVTGEKkkeeitsgkiqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASA 264
Cdd:cd14905 85 KSENTKIIIQYLLTTDLSRSK------------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 265 DIETYLLEKSRVVFQLKAERSYHIFYQ----ITSNKKPeliEMLLITTNPYDYpFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd14905 153 KLYSYFLDENRVTYQNKGERNFHIFYQflkgITDEEKA---AYQLGDINSYHY-LNQGGSISVESIDDNRVFDRLKMSFV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 341 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREeqaepdgTEVADKaAYLQSLNsadllKALCYPRVKVGNEYVT-KGQT 419
Cdd:cd14905 229 FFDFPSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDR-TLIESLS-----HNITFDSTKLENILISdRSMP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 420 VEQVSNAVGALAKAVYEKMFLWMVARINQQLdtkQPRQY--FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14905 296 VNEAVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 498 VLEQEEYKKEGIEW-TFIDFgMDLAACIELIEKpmgIFSILEEECMFPKATDTSFKNKLydqhlgksANFQKPKVVKGKA 576
Cdd:cd14905 373 KQEQREYQTERIPWmTPISF-KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 577 EAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMK----------------TLAQLFSGAQTAEGEGAGGGAK 640
Cdd:cd14905 441 PNKFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKylfsrdgvfninatvaELNQMFDAKNTAKKSPLSIVKV 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 641 KGGKKKG-----------------------------SSFQTVSAlfrenLNKLMTNlRSTHPHFVRCIIPNETKTPGAME 691
Cdd:cd14905 521 LLSCGSNnpnnvnnpnnnsgggggggnsgggsgsggSTYTTYSS-----TNKAINN-SNCDFHFIRCIKPNSKKTHLTFD 594
|
650 660
....*....|....*....|....
gi 153791586 692 HELVLHQLRCNGVLEGIRICRKGF 715
Cdd:cd14905 595 VKSVNEQIKSLCLLETTRIQRFGY 618
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
122-253 |
1.90e-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: 207.97 E-value: 1.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 122 FCVTVNPYKWLPVYKPEVV-TAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIA 200
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791586 201 VTGEKKKEEITS---GKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 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 ... |
100-770 |
1.29e-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: 171.56 E-value: 1.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYR-GKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 179 GESGAGKTVNTKRVIQYFA-----------TIAVTGEKKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAyqvkgsrrlptNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 248 GKFIRIHFGTTgKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASID 327
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFL-KNIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 328 DQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGN-------------LKFKQKQRE----------EQAEPDGTEVA 384
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 385 DKAAYLQS-LNSADLLKALCYPRVK-VGNEYV-TKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYF-- 459
Cdd:cd14938 319 VKNLLLACkLLSFDIETFVKYFTTNyIFNDSIlIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININtn 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 460 -IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM--GIFSI 536
Cdd:cd14938 399 yINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFSL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 537 LEEECMfPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAhFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSA 616
Cdd:cd14938 479 LENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 617 MKTLAQLFSG---------AQTAEGEGAGGGAKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTP 687
Cdd:cd14938 557 NEYMRQFCMFynydnsgniVEEKRRYSIQSALKLFKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKRE 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 688 -GAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAsaipegqfiDSKKASEKLLASIDIDHTQYKFGH 766
Cdd:cd14938 637 lCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMIGN 707
|
....
gi 153791586 767 TKVF 770
Cdd:cd14938 708 NMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1179-1932 |
3.80e-32 |
|
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: 137.50 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1179 KMRRdlEEATLQHEATAATLrKKHADSVAELGEQIDNLQRVKQKLEKEKsEMKMEIDDLASNVETVSKakgnlekmcRTL 1258
Cdd:TIGR02168 171 KERR--KETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERYK-ELKAELRELELALLVLRL---------EEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1259 EDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEeikaknalaha 1338
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI----------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1339 LQSSRHDcdlLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKK------LAQRLQAAEEHVEA 1412
Cdd:TIGR02168 307 LRERLAN---LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaeleeLESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1413 VNAKCASLEKTKQRLQNEVEDLMLDVERtnaacaaLDKKQRNFDKILAEWKQKCEEthAELEASQKEARSLGTELFKIKN 1492
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLER-------LEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1493 AYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEA----------SLEHEEG 1562
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlseLISVDEG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1563 KILRIQLEL------------NQVKSEVD----------RKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRL 1620
Cdd:TIGR02168 535 YEAAIEAALggrlqavvvenlNAAKKAIAflkqnelgrvTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1621 KKKMEGDLNEMEI--QLNHANRMAAEALRNYRNtqgILKDTQIHLDDALRSQEDLKEQLAMVERRAnllqaEIEELRATL 1698
Cdd:TIGR02168 615 RKALSYLLGGVLVvdDLDNALELAKKLRPGYRI---VTLDGDLVRPGGVITGGSAKTNSSILERRR-----EIEELEEKI 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1699 EQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKE 1778
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1779 QDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTY 1858
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKE--------ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791586 1859 QTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSRE 1932
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
846-1595 |
1.92e-29 |
|
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: 128.65 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 846 LKSAETEKEMAtmkEEFQKIKDELAKSEAKrkELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKI 925
Cdd:TIGR02169 200 LERLRREREKA---ERYQALLKEKREYEGY--ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 926 KEVTERAED--EEEINA------ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAK 997
Cdd:TIGR02169 275 EELNKKIKDlgEEEQLRvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 998 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIEN 1077
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1078 EKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLS----------- 1146
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEervrggravee 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1147 -------------RELEEISER----LEEAGGA------------TSAQIEMNKKREA------EFQKMRRDLEEATLQH 1191
Cdd:TIGR02169 515 vlkasiqgvhgtvAQLGSVGERyataIEVAAGNrlnnvvveddavAKEAIELLKRRKAgratflPLNKMRDERRDLSILS 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1192 EATAAtlrkKHADSVAELGEQIDNLQR-------VKQKLEKEKSEM---KM-----EIDDLASNVETVSKAKGNLEKMCR 1256
Cdd:TIGR02169 595 EDGVI----GFAVDLVEFDPKYEPAFKyvfgdtlVVEDIEAARRLMgkyRMvtlegELFEKSGAMTGGSRAPRGGILFSR 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1257 TLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALA 1336
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1337 HALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQAAEEHVEAVNAK 1416
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL---SKLEEEVSRIEARLREIEQKLNRLTLE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1417 CASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEE 1496
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1497 SLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIK------KQVEQEKCELQAALEEAE-----ASLEHEEGKIL 1565
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEpvnmlAIQEYEEVLKR 987
|
810 820 830
....*....|....*....|....*....|.
gi 153791586 1566 RIQLELNQVKSEVDRK-IAEKDEEIDQLKRN 1595
Cdd:TIGR02169 988 LDELKEKRAKLEEERKaILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
850-1754 |
5.25e-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: 127.09 E-value: 5.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 850 ETEKEMATMKEEFQKIKDELAKSEAKRKELE------EKMVTLLKEKNDLQLQV-----QAEAEGLADAEERCDQLIKTK 918
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 919 IQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKL 998
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 999 TKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENE 1078
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1079 KQQLDEKLKKKEFEISNLQskIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLE- 1157
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDs 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1158 --------EAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAelgeqIDNLQRVKQKLEKEKSE 1229
Cdd:TIGR02168 494 lerlqenlEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVV-----VENLNAAKKAIAFLKQN 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1230 MKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQ-----TESGEFSRQLDEKEALV 1304
Cdd:TIGR02168 569 ELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvddlDNALELAKKLRPGYRIV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1305 SQ----------LSRGKQAFTQQIEELKRQLEEeikaknalahalqssrhdcdlLREQYEEEQESKAELQRALSKANTEv 1374
Cdd:TIGR02168 649 TLdgdlvrpggvITGGSAKTNSSILERRREIEE---------------------LEEKIEELEEKIAELEKALAELRKE- 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1375 aqwrtkyetdaiqrTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKqrn 1454
Cdd:TIGR02168 707 --------------LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER--- 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1455 fdkiLAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEK 1534
Cdd:TIGR02168 770 ----LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1535 IKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRnhiriVESMQSTLDAEIRSR 1614
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE-----LESKRSELRRELEEL 920
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1615 NDAIrlkKKMEGDLNEMEIQLNHANRMAAEalrnyrntqgilkDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEEL 1694
Cdd:TIGR02168 921 REKL---AQLELRLEGLEVRIDNLQERLSE-------------EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1695 -RATLEqtersrkiAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEA 1754
Cdd:TIGR02168 985 gPVNLA--------AIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDT 1037
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
982-1800 |
2.57e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 124.78 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 982 KNLTEEMAGldetIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLR--------MD 1053
Cdd:TIGR02168 158 RAIFEEAAG----ISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRelelallvLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1054 LERAKRKLE---GDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEA 1130
Cdd:TIGR02168 234 LEELREELEelqEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1131 ERASRAKAEKQRSDLSR---ELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKhadsVA 1207
Cdd:TIGR02168 314 LERQLEELEAQLEELESkldELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK----VA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1208 ELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKmcRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQ 1287
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEELR 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1288 TESGEFSRQLDEKEALVSQLsRGKQAFTQQIEELKRQLEEEIKakNALAHALQSSRHDcDLLREQYEEEQESKAELQRAL 1367
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSEGVK--ALLKNQSGLSGIL-GVLSELISVDEGYEAAIEAAL 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1368 SKANTEVAqwrTKYETDAIQRTEELEEAKK--------------KLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVED 1433
Cdd:TIGR02168 544 GGRLQAVV---VENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSY 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1434 LMLDV----------------------------------------ERTNAACAALDKKQRNFDKILAEWKQKCEETHAEL 1473
Cdd:TIGR02168 621 LLGGVlvvddldnalelakklrpgyrivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKAL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1474 EASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEA 1553
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1554 EASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRiVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEI 1633
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1634 QLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELL 1713
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1714 DASERVQLLHTQNTSLINTKK-KLETDISQMQGEMEDIlqearnaeEKAKKAITDAAMMA-EELKKEQDTSAHLERMKKN 1791
Cdd:TIGR02168 940 NLQERLSEEYSLTLEEAEALEnKIEDDEEEARRRLKRL--------ENKIKELGPVNLAAiEEYEELKERYDFLTAQKED 1011
|
....*....
gi 153791586 1792 MEQTVKDLQ 1800
Cdd:TIGR02168 1012 LTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1318-1937 |
1.44e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 119.01 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1318 IEELKRQLEE-EIKAKNALA-HALQS--SRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETdAIQRTEELE 1393
Cdd:TIGR02168 195 LNELERQLKSlERQAEKAERyKELKAelRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1394 EAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAEL 1473
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1474 EASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEA 1553
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1554 EASLEHEEGKILRIQLE--------LNQVKSEVDRKIAEKDEEIDQLKRNH------IRIVESMQ--------------- 1604
Cdd:TIGR02168 434 ELKELQAELEELEEELEelqeelerLEEALEELREELEEAEQALDAAERELaqlqarLDSLERLQenlegfsegvkallk 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1605 -------------------------------STLDAEIRSRNDAIR-----LKKKMEGDLNEMEIQLNHANRMAA---EA 1645
Cdd:TIGR02168 514 nqsglsgilgvlselisvdegyeaaieaalgGRLQAVVVENLNAAKkaiafLKQNELGRVTFLPLDSIKGTEIQGndrEI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1646 LRNYRNTQGILKD-----TQIH---------------LDDALRSQEDLKEQLAMV------------------ERRANLL 1687
Cdd:TIGR02168 594 LKNIEGFLGVAKDlvkfdPKLRkalsyllggvlvvddLDNALELAKKLRPGYRIVtldgdlvrpggvitggsaKTNSSIL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1688 --QAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAI 1765
Cdd:TIGR02168 674 erRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1766 TDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKG 1845
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1846 LRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNK 1925
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
730
....*....|..
gi 153791586 1926 LRVKSREVHTKV 1937
Cdd:TIGR02168 913 LRRELEELREKL 924
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
846-1594 |
2.84e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 118.24 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 846 LKSAETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKI 925
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 926 KEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKAL 1005
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1006 QEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEK----KLRMDLERAKRK-LEGDLKLAQESIMDIENEKQ 1080
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQqeieELLKKLEEAELKeLQAELEELEEELEELQEELE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1081 QLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISER----- 1155
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDegyea 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1156 -LEEAGGATSAQIEMNKKREAefqkmrRDLEEATLQHEATAATL----RKKHADSVAELGEQIDNLQRVKQ---KLEKEK 1227
Cdd:TIGR02168 538 aIEAALGGRLQAVVVENLNAA------KKAIAFLKQNELGRVTFlpldSIKGTEIQGNDREILKNIEGFLGvakDLVKFD 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1228 SEMKMEIDDLASNVetvskakgnleKMCRTLEDQLsELKSKEEEQQRLI---NDLTAQRGRL-----QTESGEFSRQ--L 1297
Cdd:TIGR02168 612 PKLRKALSYLLGGV-----------LVVDDLDNAL-ELAKKLRPGYRIVtldGDLVRPGGVItggsaKTNSSILERRreI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1298 DEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQY---EEEQESKAELQRALSKANTEV 1374
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLarlEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1375 AQWRTKYETDAIQRTEELEEAKKKLAQRlqaaEEHVEAVNAKCASLEKTKQRLQNEVEDLmldvertNAACAALDKKQRN 1454
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEEL----EAQIEQLKEELKALREALDELRAELTLL-------NEEAANLRERLES 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1455 FDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEK 1534
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1535 IKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELN-----------QVKSEVDRKIAEKDEEIDQLKR 1594
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeeysltleeaeALENKIEDDEEEARRRLKRLEN 979
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
923-1809 |
4.57e-25 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 114.39 E-value: 4.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 923 AKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKdIDDLELTLAKVE-----KEKHATENKVKNLTEEMAGLDETIAK 997
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 998 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAK-IKLEQQVDDLEGSLEQekklrmdlerakrkLEGDLKLAQESIMDIE 1076
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAEIAS--------------LERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1077 NEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERL 1156
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1157 EEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKhADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDD 1236
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1237 lasnvetvskakgnlekmcrtLEDQLSELKSKEEEqqrlindLTAQRGRLQTESGEFSRQLDEKEA-------LVSQLSR 1309
Cdd:TIGR02169 481 ---------------------VEKELSKLQRELAE-------AEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1310 GKQAFtqqieelkrQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKA---------ELQRALSKANTEVAqwrTK 1380
Cdd:TIGR02169 533 VGERY---------ATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRAtflplnkmrDERRDLSILSEDGV---IG 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1381 YETDAIQRTEELEEAKKK------LAQRLQAAEEHVeaVNAKCASLEKtkqrlqneveDLmldVERTNAACAALDKKQRN 1454
Cdd:TIGR02169 601 FAVDLVEFDPKYEPAFKYvfgdtlVVEDIEAARRLM--GKYRMVTLEG----------EL---FEKSGAMTGGSRAPRGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1455 FDKILAEwKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEK 1534
Cdd:TIGR02169 666 ILFSRSE-PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1535 IKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR-KIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRS 1613
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1614 RNDAIRLKKKMEGDLNEM-EIQLNHANRMAAEAlrnyrNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIE 1692
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRiDLKEQIKSIEKEIE-----NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1693 ELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLET------DISQMQGEMEDILQEARNAEEKAKKAIT 1766
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelSLEDVQAELQRVEEEIRALEPVNMLAIQ 979
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 153791586 1767 DAAMMAEELKKEQDTSAHLERMKknmeqtvKDLQLRLDEAEQL 1809
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAKLEEER-------KAILERIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
930-1869 |
1.10e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 112.85 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 930 ERAEDEEEIN--AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEkhatenkVKNLTEEmagldetiaKLTKEK-KALQ 1006
Cdd:TIGR02169 154 ERRKIIDEIAgvAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQ-------LERLRRE---------REKAERyQALL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1007 EAHQQTLDDLQAEEdkVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDI-ENEKQQLDEK 1085
Cdd:TIGR02169 218 KEKREYEGYELLKE--KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1086 LKKKEFEISNLQSKIEDEQALGIQLQKKikelqarieeleeeieaerasRAKAEKQRSDLSRELEEISERLEEAGGATSA 1165
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEER---------------------LAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1166 QIEMNKKREAEFQKMRRDLEEAtlqhEATAATLRKKHADSVAELGE----------QIDNLQRVKQKLEKEKSEMKMEID 1235
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEV----DKEFAETRDELKDYREKLEKlkreinelkrELDRLQEELQRLSEELADLNAAIA 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1236 DLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFT 1315
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1316 QQIEELK----------RQL----EEEIKA-KNALAHALQSSRHDCDLLREQYEEEQESKaELQRA----LSKANTEVAQ 1376
Cdd:TIGR02169 511 AVEEVLKasiqgvhgtvAQLgsvgERYATAiEVAAGNRLNNVVVEDDAVAKEAIELLKRR-KAGRAtflpLNKMRDERRD 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1377 WRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNakcaSLEkTKQRLQNEVEDLMLD---VERTNAACAALDKKQR 1453
Cdd:TIGR02169 590 LSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVE----DIE-AARRLMGKYRMVTLEgelFEKSGAMTGGSRAPRG 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1454 NFDKILAEwKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELE 1533
Cdd:TIGR02169 665 GILFSRSE-PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1534 KIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR-KIAEKDEEIDQLKRNHIRIVESMQStLDAEIR 1612
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRIEARLRE-IEQKLN 822
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1613 SRNdairlkkkMEGDLNEMEIQlnhanrmaaealrnyrntqgilkdtqihldDALRSQEDLKEQLAMVERRANLLQAEIE 1692
Cdd:TIGR02169 823 RLT--------LEKEYLEKEIQ------------------------------ELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1693 ELRATLEQTersrkiaEQELLDASERvqllhtqntslintKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMA 1772
Cdd:TIGR02169 865 ELEEELEEL-------EAALRDLESR--------------LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1773 EELKKEQDTSAHLERMKKNMEQtvkdlqlrlDEAEQLALKGGKKQIQKLEARVRELEG-------EVESEQKRNAEAVKG 1845
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEE---------IPEEELSLEDVQAELQRVEEEIRALEPvnmlaiqEYEEVLKRLDELKEK 994
|
970 980
....*....|....*....|....*..
gi 153791586 1846 LRKHERR---VKELTYQTEEDRKNILR 1869
Cdd:TIGR02169 995 RAKLEEErkaILERIEEYEKKKREVFM 1021
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
854-1435 |
1.23e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.72 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 854 EMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAE 933
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 934 DEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTL 1013
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1014 DDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEI 1093
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1094 SNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQR---------SDLSRELEEISERLEEAGGATS 1164
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavliGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1165 AQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDnlqRVKQKLEKEKSEMKMEIDDLASNVETV 1244
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD---LVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1245 SKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQ 1324
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1325 LEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVaqwrtkYETDAIQRteELEEAKKKLaQRL- 1403
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP------PDLEELER--ELERLEREI-EALg 780
|
570 580 590
....*....|....*....|....*....|....*
gi 153791586 1404 ---QAAEEHVEAVNAKCASLEKTKQRLQNEVEDLM 1435
Cdd:COG1196 781 pvnLLAIEEYEELEERYDFLSEQREDLEEARETLE 815
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1316-1917 |
3.35e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.18 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1316 QQIEELKRQ---------LEEEIKAKNALAHALQSsrhdcDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYEtdai 1386
Cdd:COG1196 200 RQLEPLERQaekaeryreLKEELKELEAELLLLKL-----RELEAELEELEAELEELEAELEELEAELAELEAELE---- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1387 qrteELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKC 1466
Cdd:COG1196 271 ----ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1467 EETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCEL 1546
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1547 QAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRsRNDAIRLKKKMEG 1626
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-LLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1627 DLNE------------------MEIQLNHANRMAAEALRNYRNTQGILKDTQihldDALRSQEDLKEQLAmveRRANLLQ 1688
Cdd:COG1196 506 FLEGvkaalllaglrglagavaVLIGVEAAYEAALEAALAAALQNIVVEDDE----VAAAAIEYLKAAKA---GRATFLP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1689 AEIEELRATLEQTERSRKIAEQELLDASERVQLLHT----QNTSLINTkkkLETDISQMQGEMEDILQEARNAEEKAKKA 1764
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARyyvlGDTLLGRT---LVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1765 ITDAAMMAEELKKEQDTSahLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVK 1844
Cdd:COG1196 656 GSAGGSLTGGSRRELLAA--LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1845 GLRKHERRVKELTYQTEEDRKNILRLQDLvDKLQAKVKSYKRQAEE-------AEEqsntnlakfrklqhELEEAEERAD 1917
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDL-EELERELERLEREIEAlgpvnllAIE--------------EYEELEERYD 798
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1125-1915 |
1.74e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 109.00 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1125 EeeieaerasrAKAEKQRsdlsRELEEISERLEEaggatsAQIEMNKKREaEFQKMRRDLEEAtlqhEATAATLRKKHAD 1204
Cdd:TIGR02169 169 D----------RKKEKAL----EELEEVEENIER------LDLIIDEKRQ-QLERLRREREKA----ERYQALLKEKREY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1205 SVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQ-QRLINDLTAQR 1283
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1284 GRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAEL 1363
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1364 QRALSKANTEVaqwrtkyeTDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVErtna 1443
Cdd:TIGR02169 384 RDELKDYREKL--------EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK---- 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1444 acaALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLgtelfkiknayEESLDQLETLKRENKNLQQEISDLTEQIA 1523
Cdd:TIGR02169 452 ---KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL-----------QRELAEAEAQARASEERVRGGRAVEEVLK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1524 EGGKRIHELekiKKQVEQEKCELQAALEEAEAS------LEHEEGKILRIQ------------LELNQVKSE-VDRKIAE 1584
Cdd:TIGR02169 518 ASIQGVHGT---VAQLGSVGERYATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrrkagratfLPLNKMRDErRDLSILS 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1585 KDE---------EIDQLKRNHIR-------IVESMQS-----------TLDAEI-----------RSRNDAIRLKKKMEG 1626
Cdd:TIGR02169 595 EDGvigfavdlvEFDPKYEPAFKyvfgdtlVVEDIEAarrlmgkyrmvTLEGELfeksgamtggsRAPRGGILFSRSEPA 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1627 DLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRK 1706
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1707 IAEQELLDASERVQLLHTQNTSLINTKKKLETDIS-----QMQGEMEDILQE-------ARNAEEKAKKAITDAAMMAEE 1774
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEvsriearLREIEQKLNRLTLEKEYLEKE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1775 LKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVK 1854
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1855 ELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSnTNLAKFRKLQHELEEAEER 1915
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP-EEELSLEDVQAELQRVEEE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1147-1936 |
1.77e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 109.00 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1147 RELEEISERLEEAggatsaQIEMNKKREaEFQKMRRDLEEAtlqhEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKE 1226
Cdd:TIGR02169 177 EELEEVEENIERL------DLIIDEKRQ-QLERLRREREKA----ERYQALLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1227 KSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQ-QRLINDLTAQRGRLQTESGEFSRQLDEKEALVS 1305
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1306 QLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVaqwrtkyeTDA 1385
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL--------EKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1386 IQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVErtnaacaALDKKQRNFDKILAEWKQK 1465
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK-------KQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1466 CEETHAELEASQKEARSLgtelfkiknayEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELekiKKQVEQEKCE 1545
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKL-----------QRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGT---VAQLGSVGER 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1546 LQAALEEAEAS------LEHEEGKILRIQ------------LELNQVKSE-VDRKIAEKDE---------EIDQLKRNHI 1597
Cdd:TIGR02169 537 YATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrrkagratfLPLNKMRDErRDLSILSEDGvigfavdlvEFDPKYEPAF 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1598 R-------IVESMQSTldaeiRSRNDAIRLKKkMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQ 1670
Cdd:TIGR02169 617 KyvfgdtlVVEDIEAA-----RRLMGKYRMVT-LEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1671 EDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVqllhtqntslintkKKLETDISQMQGEMEdi 1750
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL--------------EELEEDLSSLEQEIE-- 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1751 lqearNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKnmEQTVKDLQLRLDEAEqlalkggkKQIQKLEARVRELEG 1830
Cdd:TIGR02169 755 -----NVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLE--------EEVSRIEARLREIEQ 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1831 EVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELE 1910
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
810 820
....*....|....*....|....*.
gi 153791586 1911 EAEERADIAESQVNKLRVKSREVHTK 1936
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1141-1754 |
4.30e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.72 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1141 QRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHAdSVAELGEQIDNLQRVK 1220
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA-ELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1221 QKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEK 1300
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1301 EALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTK 1380
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1381 YETDA---IQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVE---------RTNAACAAL 1448
Cdd:COG1196 472 AALLEaalAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEaayeaaleaALAAALQNI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1449 DKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKR 1528
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1529 IHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLD 1608
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1609 AEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEalrnyrntqgilkdtqihLDDALRSQEDLKEQLAMVERRANLLQ 1688
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEEL------------------LEEEALEELPEPPDLEELERELERLE 773
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1689 AEIEEL-----RAtleqtersrkiaEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEA 1754
Cdd:COG1196 774 REIEALgpvnlLA------------IEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLET 832
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
842-1434 |
6.58e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.94 E-value: 6.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 842 IKPLLKSAETEKEMATMKEEFQKIKDELAKseAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLiktKIQL 921
Cdd:COG1196 202 LEPLERQAEKAERYRELKEELKELEAELLL--LKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL---RLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 922 EAKIKEVTERAEDEEEINAELtakkRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKE 1001
Cdd:COG1196 277 EELELELEEAQAEEYELLAEL----ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1002 KKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQ 1081
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1082 LDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAeKQRSDLSRELEEISERLEEAGG 1161
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-AARLLLLLEAEADYEGFLEGVK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1162 ATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNV 1241
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1242 E---TVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQI 1318
Cdd:COG1196 592 LargAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1319 EELKRQLEEEIKAKNALAHALQSSRHdcDLLREQYEEEQESKAELQRALSKANTEVAQwRTKYETDAIQRTEELEEAkkk 1398
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEE--ALLAEEEEERELAEAEEERLEEELEEEALE-EQLEAEREELLEELLEEE--- 745
|
570 580 590
....*....|....*....|....*....|....*.
gi 153791586 1399 LAQRLQAAEEHVEAVNAkcASLEKTKQRLQNEVEDL 1434
Cdd:COG1196 746 ELLEEEALEELPEPPDL--EELERELERLEREIEAL 779
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
223-717 |
6.69e-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: 106.75 E-value: 6.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 223 IISANPLLEAFGNAKTVRNDNSSRFGKF--IRIHFGTTG---KLASADIETYLLEKSRVVFQL------KAERSYHIFYQ 291
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 292 ITS--NKKPEL----IEMLLITTNPYDYPFVSQGEISVASIDDQEELMATD--------SAIDILGFTNEEKVSIYKLTG 357
Cdd:cd14894 329 MVAgvNAFPFMrllaKELHLDGIDCSALTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 358 AVMHYGNLKFKQKQREEQAEPDGT---EVADKAAYLQSLNSADLL-KALCYPRVKVGNEYVTKGQTVE--QVSNAVGALA 431
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLeRMLMTKSVSLQSTSETFEVTLEkgQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 432 KAVYEKMFLWMVARINQ--------------QLDTKQPRQYFIGVL---DIAGFEIFDFNSLEQLCINFTNEKLqqFFNH 494
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEatkmsalstdgnkhQMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINYLSEKL--YARE 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 495 HMFVLEQEEYKKEGIEWtfiDFGMDLaacIELIEKPMGIFSILEEECMFPKATDTSF-----KNKLYDQHL--GKSANFQ 567
Cdd:cd14894 567 EQVIAVAYSSRPHLTAR---DSEKDV---LFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIydRNSSRLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 568 KPKVVKGKAEAH---------FALIHYAGVVDYNITGWLEKNKDPL-NETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGG 637
Cdd:cd14894 641 EPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLNESSQLGWSPNTNR 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 638 GAKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPS 717
Cdd:cd14894 721 SMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNSSSS 800
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
860-1602 |
2.95e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 105.61 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 860 EEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEIN 939
Cdd:PTZ00121 1191 EELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 940 AELTAKKRKLED-ECSELKKDIDDLEltlaKVEKEKHATENKVKnlTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQA 1018
Cdd:PTZ00121 1271 AIKAEEARKADElKKAEEKKKADEAK----KAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1019 EEdkvntltKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQS 1098
Cdd:PTZ00121 1345 AE-------AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1099 KIEDEQALGIQLQKKIKELQARIEELEeeieaerasRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEfq 1178
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEEAK---------KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-- 1486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1179 KMRRDLEEATLQ-HEATAATLRKKHADSVAELGEQidnlqrvKQKLEKEKSEMKMEIDDlASNVETVSKAkgnlEKMCRT 1257
Cdd:PTZ00121 1487 EAKKKAEEAKKKaDEAKKAAEAKKKADEAKKAEEA-------KKADEAKKAEEAKKADE-AKKAEEKKKA----DELKKA 1554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1258 LEDQLSELKSKEEEQQRlindlTAQRGRLQTESGEFSRQLDEKEaLVSQLSRGKQAFTQQIEELKRQLEEEIKAKNalAH 1337
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKK-----AEEDKNMALRKAEEAKKAEEAR-IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE--LK 1626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1338 ALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAiQRTEEL---EEAKKKLAQRLQAAEEH---VE 1411
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaEEDEKKAAEALKKEAEEakkAE 1705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1412 AVNAKCASLEKTKQRLQNEVEDLMLDVERTnaacaaldKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIK 1491
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1492 NAY-EESLDQLETLKR-ENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQA-----ALEEAEASLEHEEGKi 1564
Cdd:PTZ00121 1778 EAViEEELDEEDEKRRmEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVAdsknmQLEEADAFEKHKFNK- 1856
|
730 740 750
....*....|....*....|....*....|....*...
gi 153791586 1565 lriqlelNQVKSEVDRKIAEKDEEIDQLKRNHIRIVES 1602
Cdd:PTZ00121 1857 -------NNENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
849-1538 |
1.09e-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: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 849 AETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMvtllkekNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV 928
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRL-------EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 929 TERAEDEEEINAELtaKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKE---KKAL 1005
Cdd:TIGR02168 413 EDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaqLQAR 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1006 QEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAkrkLEGDLklaQESIMDIENEKQQLDEK 1085
Cdd:TIGR02168 491 LDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA---LGGRL---QAVVVENLNAAKKAIAF 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1086 LKKKEFEISNLqskIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSD-LSRELeeISERLEEA----- 1159
Cdd:TIGR02168 565 LKQNELGRVTF---LPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYlLGGVL--VVDDLDNAlelak 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1160 ------------------GGATSAQIEmnkKREAEFQKMRRDLEEATLQHEATAATLRKKHAdSVAELGEQIDNLQRVKQ 1221
Cdd:TIGR02168 640 klrpgyrivtldgdlvrpGGVITGGSA---KTNSSILERRREIEELEEKIEELEEKIAELEK-ALAELRKELEELEEELE 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1222 KLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQrlindltAQRGRLQTESGEFSRQLDEKE 1301
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE-------ERLEEAEEELAEAEAEIEELE 788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1302 ALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKY 1381
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1382 ETdAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKK-QRNFDKILA 1460
Cdd:TIGR02168 869 EE-LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRiDNLQERLSE 947
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1461 EWK-------QKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELE 1533
Cdd:TIGR02168 948 EYSltleeaeALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
....*
gi 153791586 1534 KIKKQ 1538
Cdd:TIGR02168 1028 REARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1434 |
3.71e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 101.29 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 847 KSAETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQ----------AEAEGLADAEERCDQLIK 916
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnneierleARLERLEDRRERLQQEIE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 917 T--KIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV---KNLTEEMAGL 991
Cdd:TIGR02168 425 EllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQENLEGF 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 992 DETIAKLTKEKK-------------------------ALQEAHQQTL-DDLQAEEDKVNTLTKAKIKL------------ 1033
Cdd:TIGR02168 505 SEGVKALLKNQSglsgilgvlselisvdegyeaaieaALGGRLQAVVvENLNAAKKAIAFLKQNELGRvtflpldsikgt 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1034 EQQVDDLEGSLEQEKKLRM--DLERAKRKLEGDLK--LAQESIMDIENEKQQLDEKLKKKE---------FEISNLQSKI 1100
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVakDLVKFDPKLRKALSylLGGVLVVDDLDNALELAKKLRPGYrivtldgdlVRPGGVITGG 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1101 EDEQALGIQ-LQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAEFQK 1179
Cdd:TIGR02168 665 SAKTNSSILeRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL--------------SRQISA 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1180 MRRDLEEATLQHEATAATLRKKHADsVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLE 1259
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1260 DQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHAL 1339
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1340 QSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCAS 1419
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
650
....*....|....*
gi 153791586 1420 LEKTKQRLQNEVEDL 1434
Cdd:TIGR02168 970 ARRRLKRLENKIKEL 984
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1007-1830 |
4.43e-21 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 101.35 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1007 EAHQQTLDDLQAEEDKVNTL-TKAKIKLEQQVDDLEGSLEQ---EKKLRMDLERAKRKLEGDLK-LAQESIMDIENEKQQ 1081
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLRnQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1082 LDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAEraSRAKAEKQRSDLSRELEEISERLEEAGG 1161
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSM--STMHFRSLGSAISKILRELDTEISYLKG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1162 AT--------SAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKME 1233
Cdd:pfam15921 239 RIfpvedqleALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1234 IDDLASnveTVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLdekEALVSQLSRGKQA 1313
Cdd:pfam15921 319 LSDLES---TVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL---QKLLADLHKREKE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1314 FTQQIEELKRQLEEEIKAKNALAHalqssrhdcdllreqyeeeqeskaeLQRALSKANTEVaqwrtkyetdaiQRTEELE 1393
Cdd:pfam15921 393 LSLEKEQNKRLWDRDTGNSITIDH-------------------------LRRELDDRNMEV------------QRLEALL 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1394 EAKKKLAQ--------RLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLmldvertNAACAALDKKQRNFDKILAEWKQK 1465
Cdd:pfam15921 436 KAMKSECQgqmerqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTVSDLTASLQEK 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1466 ceethaeleasQKEARSLGTELFKIKNAYEESLDQLETLKREN---KNLQQEISDLTEQIAEGGKRIhelEKIKKQVEQ- 1541
Cdd:pfam15921 509 -----------ERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEKDKVI---EILRQQIENm 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1542 -----EKCELQAALEEAEASLEHE-EGKILRIQlELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLdaeiRSRN 1615
Cdd:pfam15921 575 tqlvgQHGRTAGAMQVEKAQLEKEiNDRRLELQ-EFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERL----RAVK 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1616 DairLKKKMEGDLNEMEIQLNHANRMAAE---ALRNYRNTQGILKDTQIHLDDALRSQedlkeqlamverranllQAEIE 1692
Cdd:pfam15921 650 D---IKQERDQLLNEVKTSRNELNSLSEDyevLKRNFRNKSEEMETTTNKLKMQLKSA-----------------QSELE 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1693 ELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMA 1772
Cdd:pfam15921 710 QTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMA 789
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1773 EELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQ-KLEAR--VRELEG 1830
Cdd:pfam15921 790 GELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRlKLQHTldVKELQG 850
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1206-1834 |
7.03e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.40 E-value: 7.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1206 VAELGEQIDNLQR----------VKQKL-EKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQR 1274
Cdd:COG1196 195 LGELERQLEPLERqaekaeryreLKEELkELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1275 LINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYE 1354
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1355 EEQESKAELQRALSKANTEVAQWRtkyetdaiqrtEELEEAKKKLAQRLQAAEEhveavnakcasLEKTKQRLQNEVEDL 1434
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAE-----------EELEELAEELLEALRAAAE-----------LAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1435 MLDVERTNAACAALDKKQrnfdkilaewkqkcEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQE 1514
Cdd:COG1196 413 LERLERLEEELEELEEAL--------------AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1515 ISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRiqlelnqvkseVDRKIAEKDEEIDQLKR 1594
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI-----------GVEAAYEAALEAALAAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1595 NHIRIVESMQSTLDAeirsrndAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLK 1674
Cdd:COG1196 548 LQNIVVEDDEVAAAA-------IEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1675 EQLAMVERRANLLQAeiEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEA 1754
Cdd:COG1196 621 TLLGRTLVAARLEAA--LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1755 RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVES 1834
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
836-1441 |
7.57e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.52 E-value: 7.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 836 MKLFFKIKPLLKSAETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAeercdqlI 915
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA-------A 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 916 KTKIQLEAKIKEVTERAEDEEEINAELTAKKRKL-EDECSELKKDIDDLEltlAKVEKEKHATENKVKnlTEEMAGLDET 994
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEAKKKADAAK---KKAEEKKKADEAKKK--AEEDKKKADE 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 995 IAKLTKEKKALQEAHQqtlddlQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKlrmdLERAKRKLEgdlklaqesimd 1074
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKK------KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK----AEEAKKKAE------------ 1467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1075 ienEKQQLDEKLKKKEFEISNLQSKIEDEQAlgiqlQKKIKELQarieeleeeieAERASRAKAEKQRSDLSRELEEISE 1154
Cdd:PTZ00121 1468 ---EAKKADEAKKKAEEAKKADEAKKKAEEA-----KKKADEAK-----------KAAEAKKKADEAKKAEEAKKADEAK 1528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1155 RLEEAGGATSAQIEMNKKREAEFQKMR--RDLEEATLQHEATAATLRKKHADSVAELGEQIDNlQRVKQKLEKEKSEMKM 1232
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE-ARIEEVMKLYEEEKKM 1607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1233 EIDDLASNVETVSKAKgnlekmcrtledqlsELKsKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQ 1312
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAE---------------ELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1313 AFTQQIEELKRQLEEEIKAKNALAHALQSSRhDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAiQRTEEL 1392
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEA 1749
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 153791586 1393 ---EEAKKKLAQRLQAAEEHVEAVNAKCASLekTKQRLQNEVEDLMLDVERT 1441
Cdd:PTZ00121 1750 kkdEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKK 1799
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
969-1869 |
5.16e-19 |
|
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: 94.27 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 969 KVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAhqqtlDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEK 1048
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEET-----ENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1049 KLRmdLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEI 1128
Cdd:pfam02463 218 KLE--LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1129 EAERASRAKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAE 1208
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKA----EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1209 LGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQT 1288
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1289 ESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALS 1368
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1369 KANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEhVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAAL 1448
Cdd:pfam02463 532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT-ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1449 DKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNA-----YEESLDQLETLKRENKNLQQEISDLTEQIA 1523
Cdd:pfam02463 611 ATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEeglaeKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1524 EGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESM 1603
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1604 QstldaeirsrnDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERR 1683
Cdd:pfam02463 771 L-----------KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1684 ANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDisqmQGEMEDILQEARNAEEKAKK 1763
Cdd:pfam02463 840 LELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKE----KEEKKELEEESQKLNLLEEK 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1764 AITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAV 1843
Cdd:pfam02463 916 ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDEL 995
|
890 900
....*....|....*....|....*.
gi 153791586 1844 KGLRKHERRVKELTYQTEEDRKNILR 1869
Cdd:pfam02463 996 EKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1139-1917 |
7.60e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.05 E-value: 7.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1139 EKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREaefQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQR 1218
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAE---EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1219 VKQKLEKEKSEMKMEiddlASNVETVSKAkgnlEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRlQTESGEFSRQLD 1298
Cdd:PTZ00121 1160 AEDARKAEEARKAED----AKKAEAARKA----EEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVK 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1299 EKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWR 1378
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1379 TKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAAcaaldKKQRNFDKI 1458
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-----KKKADAAKK 1385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1459 LAEWKQKCEETHAELEASQKEARSLgtelfKIKNAYEESLDQLETLKRENKNlqqeiSDLTEQIAEGGKRIHELEKikKQ 1538
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADEL-----KKAAAAKKKADEAKKKAEEKKK-----ADEAKKKAEEAKKADEAKK--KA 1453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1539 VEQEKCElqaaleeaEASLEHEEGKilriqlelnqvKSEVDRKIAEKDEEIDQLKRNhirivesmqstldAEiRSRNDAI 1618
Cdd:PTZ00121 1454 EEAKKAE--------EAKKKAEEAK-----------KADEAKKKAEEAKKADEAKKK-------------AE-EAKKKAD 1500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1619 RLKKKMEGDLNEMEIQLNHANRMAAEALR--NYRNTQGILKDTQIHLDDALRSQEDLKEqlAMVERRANLLQAEIEELRA 1696
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKKAEEAKKADEAKKaeEAKKADEAKKAEEKKKADELKKAEELKK--AEEKKKAEEAKKAEEDKNM 1578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1697 TLEQTERSRKIAEqelldaservqllhtqntslintkKKLETDISQMQGEMEDILQEARNAEEKAKKAitdaammaEELK 1776
Cdd:PTZ00121 1579 ALRKAEEAKKAEE------------------------ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--------EELK 1626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1777 KEQDTSAHLERMKKNMEQTVKDL-QLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKE 1855
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAeELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791586 1856 LTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAE---EQSNTNLAKFRKLQHELEEAEERAD 1917
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
843-1380 |
8.32e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 93.59 E-value: 8.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 843 KPLLKSAETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLqlqvQAEAEGLADAEERCDQLIKTKIQLE 922
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL----EELKEEIEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 923 AKIKEVTERAEDEEEINAELTAKKRKLE------DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIA 996
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 997 KLTKEKKALQEahqqTLDDLQAEEDKVNTLTKAKIKLEQ--QVDDLEGSLEQEKKLRM--DLERAKRKLEGDLKLAQESI 1072
Cdd:PRK03918 339 RLEELKKKLKE----LEKRLEELEERHELYEEAKAKKEEleRLKKRLTGLTPEKLEKEleELEKAKEEIEEEISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1073 MDIENEKQQLD---EKLKKKEFEISNLQSKIEDEQALGIqLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRE- 1148
Cdd:PRK03918 415 GELKKEIKELKkaiEELKKAKGKCPVCGRELTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEs 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1149 ----LEEISERLEEAGGATSA-QIEMNKKREAEFQKMRRDLEEATLQHEATaatlrKKHADSVAELGEQIDNLQRVKQKL 1223
Cdd:PRK03918 494 elikLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSL-----KKELEKLEELKKKLAELEKKLDEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1224 EKEKSEMKMEIDDLA-SNVETVSKAKGNLEKMCR---TLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDE 1299
Cdd:PRK03918 569 EEELAELLKELEELGfESVEELEERLKELEPFYNeylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1300 KEALVSQLSRGKQaftQQIEELKRQLEEEIKAKNALAHALQSSRH----DCDLLREQYEEEQESKAELQRaLSKANTEVA 1375
Cdd:PRK03918 649 LEELEKKYSEEEY---EELREEYLELSRELAGLRAELEELEKRREeikkTLEKLKEELEEREKAKKELEK-LEKALERVE 724
|
....*
gi 153791586 1376 QWRTK 1380
Cdd:PRK03918 725 ELREK 729
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1628-1929 |
1.58e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.69 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1628 LNEMEIQLNHANRMAAEALRnYRNTQGILKDTQIHLddALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKI 1707
Cdd:COG1196 195 LGELERQLEPLERQAEKAER-YRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1708 AEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1787
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1788 MKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEgEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNI 1867
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791586 1868 LRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVK 1929
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
849-1461 |
2.21e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 92.44 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 849 AETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV 928
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 929 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN-------LTEEMAGLDETIAKLTKE 1001
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGgraveevLKASIQGVHGTVAQLGSV 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1002 K----KALQEAHQQTLDDLQAEED--------------------------KVNTLTKAKIKLEQQVDDLEGSLEQEKKLR 1051
Cdd:TIGR02169 534 GeryaTAIEVAAGNRLNNVVVEDDavakeaiellkrrkagratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPKYE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1052 -------------MDLERAKR--------KLEGDL--------------KLAQESIMDIENEKQQLDEKLKKKEFEISNL 1096
Cdd:TIGR02169 614 pafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGELfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1097 QSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqIEMNKKREAE 1176
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV-------KSELKELEAR 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1177 FQKMRRDLEEATLQHEATAATLRkkhadsvaelGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCR 1256
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLS----------HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1257 TLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEeikaknala 1336
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE--------- 907
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1337 halqssrhdcdlLREQYEEEQESKAELQRALSKANTEVAQ-----WRTKYETDAIQRTEELEEAKKKLAQRLQA------ 1405
Cdd:TIGR02169 908 ------------LEAQIEKKRKRLSELKAKLEALEEELSEiedpkGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnm 975
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791586 1406 -AEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTN-----AACAALDKKQRNFDKILAE 1461
Cdd:TIGR02169 976 lAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEkkkreVFMEAFEAINENFNEIFAE 1037
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
855-1706 |
2.90e-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: 91.96 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 855 MATMKEEFQKIKDELA----KSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTE 930
Cdd:pfam02463 147 IAMMKPERRLEIEEEAagsrLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 931 RAEDEEEINAE---LTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAG-LDETIAKLTKEKKALQ 1006
Cdd:pfam02463 227 LYLDYLKLNEEridLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKlLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1007 EAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAK---RKLEGDLKLAQESIMDIENEKQQLD 1083
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEeelEKLQEKLEQLEEELLAKKKLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1084 EKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGAT 1163
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1164 SAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASN--- 1240
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVais 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1241 ------VETVSKAKGNLEKMCRTLEDQLSEL--------KSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQ 1306
Cdd:pfam02463 547 taviveVSATADEVEERQKLVRALTELPLGArklrllipKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1307 LSRGKQAFTQQIEELKRQLEEEIKAKnALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAI 1386
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGV-SLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1387 QRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVErtnaacaALDKKQRNFDKILAEWKQKC 1466
Cdd:pfam02463 706 QREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK-------KEEKEEEKSELSLKEKELAE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1467 EETHAELEASQKEARSLGTEL-FKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCE 1545
Cdd:pfam02463 779 EREKTEKLKVEEEKEEKLKAQeEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELER 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1546 LQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKR--NHIRIVESMQSTLDAEIRSRNDAIRLKKK 1623
Cdd:pfam02463 859 LEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQklNLLEEKENEIEERIKEEAEILLKYEEEPE 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1624 MEGDLNEMEIQLNHANRMAAEaLRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTER 1703
Cdd:pfam02463 939 ELLLEEADEKEKEENNKEEEE-ERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
...
gi 153791586 1704 SRK 1706
Cdd:pfam02463 1018 RLK 1020
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
885-1431 |
3.27e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 91.64 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 885 TLLKEKNDLQLQVQAEAEGLADAEercdqLIKTKIQLEAKIKEVTERAE--DEEEINAELT--------AKKRKLEDECS 954
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEKD-----LHERLNGLESELAELDEEIEryEEQREQARETrdeadevlEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 955 ELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKkALQEAHQQTLDDLQAEedkvntltkakikLE 1034
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA-GLDDADAEAVEARREE-------------LE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1035 QQVDDLEGSLEQEkklRMDLERAKRKLEGdlklAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKI 1114
Cdd:PRK02224 321 DRDEELRDRLEEC---RVAAQAHNEEAES----LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1115 KELqarieeleeeieaerasrakaEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEA-TLQHEA 1193
Cdd:PRK02224 394 EEL---------------------RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAeALLEAG 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1194 TAATLRKK-----HADSVAELGEQIDnlqrvkqKLEKEKSEMKMEIDDLASNVETVSKAKgNLEKMCRTLEDQLSELKSK 1268
Cdd:PRK02224 453 KCPECGQPvegspHVETIEEDRERVE-------ELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEEL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1269 EEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEE---EIKAKNALAHALQssrhd 1345
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAElkeRIESLERIRTLLA----- 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1346 cdlLREQYEEEQESKAELQRALSKANTEvaqwRTKYETDAIQRTEELEE-----AKKKLAQRLQAAEEHVEAVNAKCASL 1420
Cdd:PRK02224 600 ---AIADAEDEIERLREKREALAELNDE----RRERLAEKRERKRELEAefdeaRIEEAREDKERAEEYLEQVEEKLDEL 672
|
570
....*....|.
gi 153791586 1421 EKTKQRLQNEV 1431
Cdd:PRK02224 673 REERDDLQAEI 683
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1015-1799 |
3.55e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.13 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1015 DLQAEEDKVNTLT--KAKIKLEQQVDDLEGSLEQEKKLrmdlERAKRKLEgDLKLAQESIMdiENEKQQLDEKLKKKEFE 1092
Cdd:PTZ00121 1080 DFDAKEDNRADEAteEAFGKAEEAKKTETGKAEEARKA----EEAKKKAE-DARKAEEARK--AEDARKAEEARKAEDAK 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1093 ISNLQSKIED----EQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEK-QRSDLSRELEEISERLEEAGGATSAQI 1167
Cdd:PTZ00121 1153 RVEIARKAEDarkaEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAaRKAEEERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1168 EMNKKREAEFQKMR--RDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQR---VKQKLEKEKSEMKMEIDDLASNVE 1242
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEeeRNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeeKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1243 TVSKAKgNLEKMCRTLEDQLSELKSKEEEQQRLINdltAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQaftqQIEELK 1322
Cdd:PTZ00121 1313 EAKKAD-EAKKKAEEAKKKADAAKKKAEEAKKAAE---AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK----KADAAK 1384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1323 RQLEEEIKAKNALAHAlQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAiqrteelEEAKKKLAQR 1402
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKA-EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA-------DEAKKKAEEA 1456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1403 LQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKilAEWKQKCEETHAELEASQKEARS 1482
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK--ADEAKKAEEAKKADEAKKAEEAK 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1483 LGTELFKIknayEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEK--IKKQVEQEKCELQAALEEAEASLEHE 1560
Cdd:PTZ00121 1535 KADEAKKA----EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1561 EGKilriQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDlnemeiqlnhanR 1640
Cdd:PTZ00121 1611 EAK----KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED------------K 1674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1641 MAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSrkiAEQElldaservq 1720
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE---AEED--------- 1742
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791586 1721 llhtqntslintKKKLEtDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmkknMEQTVKDL 1799
Cdd:PTZ00121 1743 ------------KKKAE-EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME-----VDKKIKDI 1803
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
850-1333 |
3.64e-18 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 91.24 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 850 ETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQL------IKTKIQ--- 920
Cdd:TIGR04523 135 ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLelllsnLKKKIQknk 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 921 -LEAKI-----------KEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKekhaTENKVKNLTEEM 988
Cdd:TIGR04523 215 sLESQIselkkqnnqlkDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ----NNKKIKELEKQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 989 AGLDETIAKLTKEKKalQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLA 1068
Cdd:TIGR04523 291 NQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1069 QESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRE 1148
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1149 LEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQheataatlrkkhadsVAELGEQIDNLQRVKQKLEKEKS 1228
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE---------------LKSKEKELKKLNEEKKELEEKVK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1229 EMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQL---------SELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDE 1299
Cdd:TIGR04523 514 DLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQ 593
|
490 500 510
....*....|....*....|....*....|....
gi 153791586 1300 KEALVSQLSRGKQAFTQQIEELKRQLeEEIKAKN 1333
Cdd:TIGR04523 594 KEKEKKDLIKEIEEKEKKISSLEKEL-EKAKKEN 626
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
978-1636 |
7.20e-18 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 90.08 E-value: 7.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 978 ENKVKNLTEEMAGLDETIAKLTKEKKALQEahqqtlDDLQAEEDKVNTLTKAKIkLEQQVDDLEGSLEQEKKLRMDLERA 1057
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDK------NLNKDEEKINNSNNKIKI-LEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1058 KRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAK 1137
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1138 AEKQRSDLSRELEEISERLeeaggatsAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQ 1217
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLL--------SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1218 RVKQKLEKEKSEMKMEIDDLASNVETVSkakgNLEKMCRTLEDQLSELKSkeEEQQRLINDLTAQRGRLQTESGEFSRQL 1297
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELEQNNKKIK----ELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1298 DEKEALVSQLsrgkqafTQQIEELKRQLEEeikaknalahalqsSRHDCDLLREQYEEEQESKAELQRALSKANTEVaqw 1377
Cdd:TIGR04523 331 SQNNKIISQL-------NEQISQLKKELTN--------------SESENSEKQRELEEKQNEIEKLKKENQSYKQEI--- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1378 rtkyetdaiqrtEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDK 1457
Cdd:TIGR04523 387 ------------KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1458 ILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKK 1537
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1538 QVEQEKCELQAALEEAEASLEHE--EGKILRIQLELNQVKSE---VDRKIAEKDEEIDQLKRNhIRIVESMQSTLDAEIR 1612
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTqksLKKKQEEKQELIDQKEKE-KKDLIKEIEEKEKKIS 613
|
650 660
....*....|....*....|....
gi 153791586 1613 SRNDAIRLKKKMEGDLNEMEIQLN 1636
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIK 637
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
850-1639 |
1.10e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.20 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 850 ETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQlEAKIKEVT 929
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAE-DARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 930 ERAEDEEEINAeltAKKRKLEDECSELKKDIDDLELTLA-KVEKEKHATENKV---KNLTEEMAGLDETIAKLTKEKKAL 1005
Cdd:PTZ00121 1170 RKAEDAKKAEA---ARKAEEVRKAEELRKAEDARKAEAArKAEEERKAEEARKaedAKKAEAVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1006 QEAHQQTLDDLQAEEDKVNTLTKAKIKLEQ--QVDDLEGSLEQEKKLRMDLERAKRKLEgDLKLAQESIMDIENEKQQLD 1083
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEarKADELKKAEEKKKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAE 1325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1084 EKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAE--KQRSDLSRELEEISERLEEagg 1161
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaaKKKAEEKKKADEAKKKAEE--- 1402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1162 aTSAQIEMNKKREAEFQK---MRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKsemkmEIDDLA 1238
Cdd:PTZ00121 1403 -DKKKADELKKAAAAKKKadeAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK-----KADEAK 1476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1239 SNVETVSKAKgNLEKMCRTLEDQLSELKSKEEEQQRlindltaqrgrlqtesGEFSRQLDEKealvsqlsrgKQAFTQQI 1318
Cdd:PTZ00121 1477 KKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKK----------------ADEAKKAEEA----------KKADEAKK 1529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1319 EELKRQLEEEIKAKnalahalqssrhdcdllREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEEL---EEA 1395
Cdd:PTZ00121 1530 AEEAKKADEAKKAE-----------------EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkkaEEA 1592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1396 KKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEA 1475
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1476 SQKEARSLgtelfkiKNAYEESLDQLETLKREnknlqqeisdlteqiAEGGKRIHELEKIKKQVEQEKCELQAALEEAEA 1555
Cdd:PTZ00121 1673 DKKKAEEA-------KKAEEDEKKAAEALKKE---------------AEEAKKAEELKKKEAEEKKKAEELKKAEEENKI 1730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1556 SLEHeegkiLRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQL 1635
Cdd:PTZ00121 1731 KAEE-----AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
|
....
gi 153791586 1636 NHAN 1639
Cdd:PTZ00121 1806 NFAN 1809
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1079-1855 |
3.56e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 88.25 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1079 KQQLDEKLKKKEFEISNLQSKIEDEQAL----GIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISE 1154
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELhekqKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1155 RLEeagGATSAQIEMNKKREAEFQKMRRDLeeatLQHEATAATLRKKHADSVAELGEQI---DNLQRVK-QKLEKEKSEM 1230
Cdd:pfam15921 153 ELE---AAKCLKEDMLEDSNTQIEQLRKMM----LSHEGVLQEIRSILVDFEEASGKKIyehDSMSTMHfRSLGSAISKI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1231 KMEIDdlasnvETVSKAKGNLekmcRTLEDQLSELKSKEEEQQRLIndltaqrgrLQTESGEFSRQLDEKEALVSQLSRG 1310
Cdd:pfam15921 226 LRELD------TEISYLKGRI----FPVEDQLEALKSESQNKIELL---------LQQHQDRIEQLISEHEVEITGLTEK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1311 KQAFTQQIEELKRQLE---EEIKAKNALahalqSSRHDCDL----------LREQYEEEQESKAELQRALSKANTEVAQW 1377
Cdd:pfam15921 287 ASSARSQANSIQSQLEiiqEQARNQNSM-----YMRQLSDLestvsqlrseLREAKRMYEDKIEELEKQLVLANSELTEA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1378 RTKYETDAiQRTEELEEAKKKLAQRLQAAEEHVeavnakcaSLEKTKQR---------------LQNEVEDLMLDVERTN 1442
Cdd:pfam15921 362 RTERDQFS-QESGNLDDQLQKLLADLHKREKEL--------SLEKEQNKrlwdrdtgnsitidhLRRELDDRNMEVQRLE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1443 AACAALDKK-QRNFDKILAEWKQKCEethaeleaSQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQ 1521
Cdd:pfam15921 433 ALLKAMKSEcQGQMERQMAAIQGKNE--------SLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1522 IAEGGKRIH----ELEKIKKQVEQEKCELQaaleeaeaSLEHEEGKILRIQLELNQVKSEvdrkIAEKDEEIDQLKRNhi 1597
Cdd:pfam15921 505 LQEKERAIEatnaEITKLRSRVDLKLQELQ--------HLKNEGDHLRNVQTECEALKLQ----MAEKDKVIEILRQQ-- 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1598 riVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEalrnyrntqgilKDTQIHLDDALRSQEDLkEQL 1677
Cdd:pfam15921 571 --IENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDK------------KDAKIRELEARVSDLEL-EKV 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1678 AMVERRANLLQAeIEELRATLEQTERSRKIAEQELLDASERVQLL----HTQNTSLINTKKKLETDISQMQGEMEDILQE 1753
Cdd:pfam15921 636 KLVNAGSERLRA-VKDIKQERDQLLNEVKTSRNELNSLSEDYEVLkrnfRNKSEEMETTTNKLKMQLKSAQSELEQTRNT 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1754 ARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQlrldeAEQLALKGGKKQIQKlearvrELEgEVE 1833
Cdd:pfam15921 715 LKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNAN-----KEKHFLKEEKNKLSQ------ELS-TVA 782
|
810 820
....*....|....*....|..
gi 153791586 1834 SEQKRNAEAVKGLRKHERRVKE 1855
Cdd:pfam15921 783 TEKNKMAGELEVLRSQERRLKE 804
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1036-1594 |
2.31e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 85.50 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1036 QVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlaqeSIMDIENEKQQLDEKLKKKEFEISNLQSKIEdeqalgiQLQKKIK 1115
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIK----RTENIEELIKEKEKELEEVLREINEISSELP-------ELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1116 ELQARIEELEEEIEAErasrAKAEKQRSDLSRELEEISERLEEaggaTSAQIEMNKKREAEFQKMRRDLEEAtlqheata 1195
Cdd:PRK03918 225 KLEKEVKELEELKEEI----EELEKELESLEGSKRKLEEKIRE----LEERIEELKKEIEELEEKVKELKEL-------- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1196 atlrKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAK---GNLEKMCRTLEDQLSELKSKEEEQ 1272
Cdd:PRK03918 289 ----KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELY 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1273 QRlINDLTAQRGRLQTESGEFSrqLDEKEALVSQLSRGKQAFTQQIEEL---KRQLEEEIKAKNALAHALQSSRHDC--- 1346
Cdd:PRK03918 365 EE-AKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAKGKCpvc 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1347 ----------DLLREQYEEEQESKAELQRA------LSKANTEVAQWRTKYETDAIQRT--EELEEAKKKL----AQRLQ 1404
Cdd:PRK03918 442 grelteehrkELLEEYTAELKRIEKELKEIeekerkLRKELRELEKVLKKESELIKLKElaEQLKELEEKLkkynLEELE 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1405 AAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLG 1484
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1485 TELFKIKNA---YEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKI-----KKQVEQEKCELQAALEEAEAS 1556
Cdd:PRK03918 602 NEYLELKDAekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAE 681
|
570 580 590
....*....|....*....|....*....|....*...
gi 153791586 1557 LEHEEGKILRIQLELNQVKSEVDrKIAEKDEEIDQLKR 1594
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEK 718
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1214-1913 |
2.90e-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: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1214 DNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLiNDLTAQRGRLQTESGEF 1293
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1294 SRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEikaknALAHALQSSRhdcdllrEQYEEEQESKAELQRALSKANTE 1373
Cdd:TIGR00618 266 RARIEELRAQEAVLEETQERINRARKAAPLAAHIK-----AVTQIEQQAQ-------RIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1374 VAQwrtkyetdaiqrtEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTK-------QRLQNEVEDLMLDVERTNAACA 1446
Cdd:TIGR00618 334 VKQ-------------QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIScqqhtltQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1447 ALDKKQRNFDKILAE------WKQKCEETHAELEASQKEARSLgtelfkiKNAYEESLDQLETLKRENKNLQQEISDLTE 1520
Cdd:TIGR00618 401 ELDILQREQATIDTRtsafrdLQGQLAHAKKQQELQQRYAELC-------AAAITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1521 QIAEGgKRIHELEKIKKQVEQEKCELQAALE-EAEASLEHEEGK-------------ILRIQLELNQVKSEVDRKIAEKD 1586
Cdd:TIGR00618 474 QLQTK-EQIHLQETRKKAVVLARLLELQEEPcPLCGSCIHPNPArqdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1587 EEIDQLKRNHIRIVESMQSTLDAEI---RSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHL 1663
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1664 DDALRSQEDLKEQLAMVERRANLLQAEIEE-LRATLEQTERSRKIAEQELLDASERVQllhtqntSLINTKKKLETDISQ 1742
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTQERVREhALSIRVLPKELLASRQLALQKMQSEKE-------QLTYWKEMLAQCQTL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1743 MQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQ---IQ 1819
Cdd:TIGR00618 706 LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELshlAA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1820 KLEARVRELEGEVESEQKRNAEaVKGLRKHERRVKELT-YQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTN 1898
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAE-IGQEIPSDEDILNLQcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQL 864
|
730
....*....|....*
gi 153791586 1899 LAKFRKLQHELEEAE 1913
Cdd:TIGR00618 865 TQEQAKIIQLSDKLN 879
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
871-1590 |
3.39e-16 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 84.69 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 871 KSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLE 950
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 951 DECSELKKDIDDLELTLAKVEKEKHATE-------NKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKV 1023
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1024 NTLTKAKIKLEQQVDDLEGSLEQEKKLR---MDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKkkefEISNLQSKI 1100
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNKSLEsqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN----QLKDEQNKI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1101 EDeqalgiQLQKKIKELQarieeleeeieaerasraKAEKQRSDLSRELEEISERLEEAGgaTSAQIEMNKKREAEFQKM 1180
Cdd:TIGR04523 266 KK------QLSEKQKELE------------------QNNKKIKELEKQLNQLKSEISDLN--NQKEQDWNKELKSELKNQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1181 RRDLEEATLQheataatlRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLED 1260
Cdd:TIGR04523 320 EKKLEEIQNQ--------ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1261 QLSELKSKEEEQQRLINDLTAQRGRLQTesgefsrqldEKEALVSQLSRGKQAFTQQIEELKRqLEEEIKAKNALAHALQ 1340
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLQQ----------EKELLEKEIERLKETIIKNNSEIKD-LTNQDSVKELIIKNLD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1341 SSRhdcdllreqyeEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASL 1420
Cdd:TIGR04523 461 NTR-----------ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1421 EKTKQRLQNEVEDLMLDVErtnaacaaldkkqrnfdkilaewKQKCEETHAELEasqKEARSLGTELFKIKNAYEESLDQ 1500
Cdd:TIGR04523 530 ESEKKEKESKISDLEDELN-----------------------KDDFELKKENLE---KEIDEKNKEIEELKQTQKSLKKK 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1501 LETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVK---SE 1577
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRnkwPE 663
|
730
....*....|...
gi 153791586 1578 VDRKIAEKDEEID 1590
Cdd:TIGR04523 664 IIKKIKESKTKID 676
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1139-1631 |
7.28e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.94 E-value: 7.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1139 EKQRSDLSRELEEISERLEEAG---GATSAQIEMNKKREAEFQKMRRDLEEATlqhEATAATLRKKhadsvAELGEQIDN 1215
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARetrDEADEVLEEHEERREELETLEAEIEDLR---ETIAETERER-----EELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1216 LQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSR 1295
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1296 QLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVA 1375
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1376 QWRTKYE-------------TDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTK------QRLQNEVEDL-- 1434
Cdd:PRK02224 444 EAEALLEagkcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaedriERLEERREDLee 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1435 MLD-----VERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEeSLDQLETLKRENK 1509
Cdd:PRK02224 524 LIAerretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERIRTLLAAIA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1510 NLQQEISDLTEQIAEggkrIHELEKIKKQVEQEKCELQAALEEA--EASLEHEEGKILRIQLELNQVKSEVDRKIAEKDE 1587
Cdd:PRK02224 603 DAEDEIERLREKREA----LAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLDELREERDD 678
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791586 1588 ----------EIDQLKR-------------------NHIRIVESMQSTLDAEIRSRNDAirlkkKMEGDLNEM 1631
Cdd:PRK02224 679 lqaeigavenELEELEElrerrealenrvealealyDEAEELESMYGDLRAELRQRNVE-----TLERMLNET 746
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
903-1540 |
1.25e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.19 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 903 GLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLED---ECSELKKDIDDLELTLAKVEKEKhateN 979
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrEINEISSELPELREELEKLEKEV----K 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 980 KVKNLTEEMAGLDETIAKLTKEKKALQEahqqtldDLQAEEDKVNTLTKAKIKLEQQVDDLEgSLEQEKKLRMDLERAKR 1059
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEE-------KIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1060 KLEgdlklaqesimdienekqqldEKLKKKEFEISNLQSKIEDeqalgiqLQKKIKELqarieeleeeieaerasrakae 1139
Cdd:PRK03918 304 EYL---------------------DELREIEKRLSRLEEEING-------IEERIKEL---------------------- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1140 kqrSDLSRELEEISERLEEAggatsaqiemnKKREAEFQKMRRDLEEAtLQHEATAATLRKKHAD-SVAELGEQIDNLQR 1218
Cdd:PRK03918 334 ---EEKEERLEELKKKLKEL-----------EKRLEELEERHELYEEA-KAKKEELERLKKRLTGlTPEKLEKELEELEK 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1219 VKQKLEKE-------KSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEdqlselkskEEEQQRLINDLTAQRGRLQTESG 1291
Cdd:PRK03918 399 AKEEIEEEiskitarIGELKKEIKELKKAIEELKKAKGKCPVCGRELT---------EEHRKELLEEYTAELKRIEKELK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1292 EFSRQLD----EKEALVSQLSRGKQAFTQ-----QIEELKRQLE----EEIKAKNALAHALQSS----RHDCDLLREQYE 1354
Cdd:PRK03918 470 EIEEKERklrkELRELEKVLKKESELIKLkelaeQLKELEEKLKkynlEELEKKAEEYEKLKEKliklKGEIKSLKKELE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1355 EEQE---SKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAqrlQAAEEHVEAVNAkcaslEKTKQRLQNEV 1431
Cdd:PRK03918 550 KLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE---PFYNEYLELKDA-----EKELEREEKEL 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1432 EDLMLDVERTNAACAALDKKQRNFDKILAEWKQK-CEETHAELEasqKEARSLGTELFKIKNAYEESLDQLETLKRENKN 1510
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKySEEEYEELR---EEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
650 660 670
....*....|....*....|....*....|
gi 153791586 1511 LQQEIsdltEQIAEGGKRIHELEKIKKQVE 1540
Cdd:PRK03918 699 LKEEL----EEREKAKKELEKLEKALERVE 724
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1223-1700 |
2.54e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.01 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1223 LEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRL-----------------INDLTAQRGR 1285
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLretiaeterereelaeeVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1286 LQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQR 1365
Cdd:PRK02224 291 LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1366 ALSKANTEVAQWRTKYE------TDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQN---EVEDLM- 1435
Cdd:PRK02224 371 ELEEAREAVEDRREEIEeleeeiEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARErveEAEALLe 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1436 --------LDVERTNAACAALDKKQRNFDkiLAEWKQKCEETHAELEASQKEARSLgtelfkiknayEESLDQLETLKRE 1507
Cdd:PRK02224 451 agkcpecgQPVEGSPHVETIEEDRERVEE--LEAELEDLEEEVEEVEERLERAEDL-----------VEAEDRIERLEER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1508 NKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR------- 1580
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESlerirtl 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1581 --KIAEKDEEIDQL--KRNHIRIVESMQSTLDAEIRSRndairlKKKMEGDLNEMEIQLNHANRMAAEA--------LRN 1648
Cdd:PRK02224 598 laAIADAEDEIERLreKREALAELNDERRERLAEKRER------KRELEAEFDEARIEEAREDKERAEEyleqveekLDE 671
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791586 1649 YRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERR----------ANLLQAEIEELRATLEQ 1700
Cdd:PRK02224 672 LREERDDLQAEIGAVENELEELEELRERREALENRvealealydeAEELESMYGDLRAELRQ 733
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
910-1601 |
1.48e-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: 79.63 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 910 RCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAT----ENKVKNLT 985
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERkqvlEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 986 EEMAGLDETIAKLTKEKKALQEAH--QQTLDDLQAEEDKVNTLTKA------KIKLEQQVDDLEGSLEQEKKLRMDLERA 1057
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAVleetqeRINRARKAAPLAAHIKAVTQIEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1058 KRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQAlgIQLQKKIKELQARIEELEEEIEAERASRAK 1137
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA--HEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1138 AEKQRSDLSRELEEISERLEEAGGATSAQIEMNK-----KREAEFQKMRRDLEEATLQHEATAATLRKKHADSVA----E 1208
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGqlahaKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAqslkE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1209 LGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSK----------AKGNLEKMCRTLEDQLSELKSKEEEQQRLIND 1278
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGscihpnparqDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1279 LTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQA---FTQQIEELKRQLEEEIKAKNALAhalqssrhdcDLLREQYEE 1355
Cdd:TIGR00618 551 LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDipnLQNITVRLQDLTEKLSEAEDMLA----------CEQHALLRK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1356 EQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLm 1435
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML- 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1436 ldvERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEA-------SQKEARSLG-TELFKIKNAYEESLDQLETLKRE 1507
Cdd:TIGR00618 700 ---AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAredalnqSLKELMHQArTVLKARTEAHFNNNEEVTAALQT 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1508 NKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR---KIAE 1584
Cdd:TIGR00618 777 GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHqllKYEE 856
|
730
....*....|....*..
gi 153791586 1585 KDEEIDQLKRNHIRIVE 1601
Cdd:TIGR00618 857 CSKQLAQLTQEQAKIIQ 873
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
902-1839 |
1.74e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 79.63 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 902 EGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAEL-TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHatenk 980
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL----- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 981 vknlteemagLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRK 1060
Cdd:pfam02463 235 ----------NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1061 LEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEK 1140
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1141 QRSDLSRELEEISERLEEaggatsaqiemnKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVK 1220
Cdd:pfam02463 385 RLSSAAKLKEEELELKSE------------EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1221 QKLEKEKSEMKMEIDDLASNvetvskakgnlekmcrtledqlsELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEK 1300
Cdd:pfam02463 453 LEKQELKLLKDELELKKSED-----------------------LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1301 EALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALqssrhdCDLLREQYEEEQESKAELQRALSKANTEVAQWRTK 1380
Cdd:pfam02463 510 KVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTA------VIVEVSATADEVEERQKLVRALTELPLGARKLRLL 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1381 YETDaiqRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILA 1460
Cdd:pfam02463 584 IPKL---KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAE 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1461 EwkqkceethAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVE 1540
Cdd:pfam02463 661 K---------SEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1541 QEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRsRNDAIRL 1620
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL-RALEEEL 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1621 KKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQ 1700
Cdd:pfam02463 811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES 890
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1701 TERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAItdaamMAEELKKEQD 1780
Cdd:pfam02463 891 KEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK-----EEEEERNKRL 965
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791586 1781 TSAHLERMKKNMEQtvkDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRN 1839
Cdd:pfam02463 966 LLAKEELGKVNLMA---IEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1316-1915 |
2.01e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.19 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1316 QQIEELKRQLE--EEIKAKNALAHALQSSRHDCDLLRE--QYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEE 1391
Cdd:COG4913 242 EALEDAREQIEllEPIRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1392 LEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMldvERTNAACAALDKKQRNFDKILAEWKQKCEETHA 1471
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---ALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1472 ELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEG-GKRIHEL----EKIkkQVEQEKCEL 1546
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlGLDEAELpfvgELI--EVRPEEERW 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1547 QAALEEAEASLEheegkiLRIQLElnqvksevDRKIAEKDEEIDQLK-RNHIRIvESMQSTLDAEIRSRNDAIRLKKKME 1625
Cdd:COG4913 477 RGAIERVLGGFA------LTLLVP--------PEHYAAALRWVNRLHlRGRLVY-ERVRTGLPDPERPRLDPDSLAGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1626 GDLNEMEIQLNH--ANRMA------AEALRNYRntQGILKDTQIH-------LDDALRSQEDL------KEQLAMVERRA 1684
Cdd:COG4913 542 FKPHPFRAWLEAelGRRFDyvcvdsPEELRRHP--RAITRAGQVKgngtrheKDDRRRIRSRYvlgfdnRAKLAALEAEL 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1685 NLLQAEIEELRATLEQTERSRKiAEQELLDASERVQLLHTQntslintkkklETDISQMQGEMEDiLQEARNAEEKAKKA 1764
Cdd:COG4913 620 AELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWD-----------EIDVASAEREIAE-LEAELERLDASSDD 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1765 ITDAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEVESEQKRNAEAVK 1844
Cdd:COG4913 687 LAALEEQLEELEAELEE---LEEELDELKGEIGRLEKELEQAEE--------ELDELQDRLEAAEDLARLELRALLEERF 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1845 GLRKHERRVKELTYQTEEDRKNIL-RLQDLVDKLQAKVKSYKRQAEEAEEQSNTNL-------AKFRKLQHE-LEEAEER 1915
Cdd:COG4913 756 AAALGDAVERELRENLEERIDALRaRLNRAEEELERAMRAFNREWPAETADLDADLeslpeylALLDRLEEDgLPEYEER 835
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1390-1924 |
2.99e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.80 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1390 EELEEAKKKLaQRLQAAEEHVEAVNAKCASLEKTKQRLQ-NEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEE 1468
Cdd:COG4913 235 DDLERAHEAL-EDAREQIELLEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1469 THAELEASQKEARSLgtelfkiKNAYEES-LDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQ 1547
Cdd:COG4913 314 LEARLDALREELDEL-------EAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1548 AALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNhirivesmQSTLDAEIRSRNDAIR--LKKKME 1625
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR--------KSNIPARLLALRDALAeaLGLDEA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1626 -----GDLneMEIQLNHAN-RMAAE-ALRNYRNTqgILKDTQiHLDDALR--SQEDLKEQLamverranllqaeieelra 1696
Cdd:COG4913 459 elpfvGEL--IEVRPEEERwRGAIErVLGGFALT--LLVPPE-HYAAALRwvNRLHLRGRL------------------- 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1697 tleQTERSRKIAEQELLDASERVQLLHtqntslintkkKLETDISQMQGEMEDILQE------ARNAEE--KAKKAITDA 1768
Cdd:COG4913 515 ---VYERVRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLEAELGRrfdyvcVDSPEElrRHPRAITRA 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1769 AMMAeelkkeQDTSAHlermKKNMEQTVK-DLQLRLDEAEQLALKggKKQIQKLEARVRELEGEVE---------SEQKR 1838
Cdd:COG4913 581 GQVK------GNGTRH----EKDDRRRIRsRYVLGFDNRAKLAAL--EAELAELEEELAEAEERLEaleaeldalQERRE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1839 NAEAVKGLRKHERRVKELTY---QTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEER 1915
Cdd:COG4913 649 ALQRLAEYSWDEIDVASAEReiaELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
....*....
gi 153791586 1916 ADIAESQVN 1924
Cdd:COG4913 729 LDELQDRLE 737
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
846-1420 |
3.21e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 78.68 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 846 LKSAETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQaEAEGLADAEERCDQLIKTKI-QLEAK 924
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ-DTQELLQEETRQKLNLSTRLrQLEDE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 925 IKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKA 1004
Cdd:pfam01576 498 RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1005 LQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQ------------------------------------------------- 1035
Cdd:pfam01576 578 LQQELDDLLVDLDHQRQLVSNLEKKQKKFDQmlaeekaisaryaeerdraeaeareketralslaraleealeakeeler 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1036 -------QVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIE-DEQALG 1107
Cdd:pfam01576 658 tnkqlraEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFErDLQARD 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1108 IQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEA 1187
Cdd:pfam01576 738 EQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEA 817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1188 TLQHEATAATLR---KKHADSVAE---LGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQ 1261
Cdd:pfam01576 818 RASRDEILAQSKeseKKLKNLEAEllqLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEE 897
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1262 LSELKSKEE-----------EQQRLINDLTAQRGRLQTESG----------EFSRQLDEKEALV-SQLSRGKQAFTQQIE 1319
Cdd:pfam01576 898 LEEEQSNTEllndrlrkstlQVEQLTTELAAERSTSQKSESarqqlerqnkELKAKLQEMEGTVkSKFKSSIAALEAKIA 977
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1320 ELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYEtDAIQRTEELEEAKKKL 1399
Cdd:pfam01576 978 QLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE-EAEEEASRANAARRKL 1056
|
650 660
....*....|....*....|.
gi 153791586 1400 AQRLQAAEEHVEAVNAKCASL 1420
Cdd:pfam01576 1057 QRELDDATESNESMNREVSTL 1077
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
33-77 |
3.43e-14 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 68.23 E-value: 3.43e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 153791586 33 DAKTSVFVAEPKESFVKGTIQSREGGKVTVKTEGGATLTVKDDQV 77
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
841-1277 |
4.70e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.26 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 841 KIKPLLKSAETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQlqvqaEAEGLADAEERCDQLIKTKIQ 920
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK-----KAEEAKKAEEDKNMALRKAEE 1585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 921 L----EAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDiddlELTLAKVEKEKHATENKVKNLTEEMAGLDETIA 996
Cdd:PTZ00121 1586 AkkaeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 997 KLTKEKKALQEAHQQTLDDLQAEEDKVntltkakiKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIE 1076
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEK--------KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1077 NEKQQLDEKLKKKEfeisnlQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEI---S 1153
Cdd:PTZ00121 1734 EAKKEAEEDKKKAE------EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIfdnF 1807
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1154 ERLEEAGGATSAQIEMNKKRE-------AEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKE 1226
Cdd:PTZ00121 1808 ANIIEGGKEGNLVINDSKEMEdsaikevADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1227 KSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLIN 1277
Cdd:PTZ00121 1888 DEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1038-1632 |
8.93e-14 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 77.07 E-value: 8.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1038 DDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQldeKLKKKEFEISNLQSKIEDEQALGIQLQKKIKEL 1117
Cdd:pfam05483 190 NNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLEES 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1118 QARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqIEMNKKREAEFQKMRRDLEEATLQHEATAAT 1197
Cdd:pfam05483 267 RDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRS-------MSTQKALEEDLQIATKTICQLTEEKEAQMEE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1198 LRK---KHADSVAELGEQIDNLQRV----KQKLEKEKSEMK---MEIDDLASNVETVSKAKGNLEKMCRTLEDQLSE--- 1264
Cdd:pfam05483 340 LNKakaAHSFVVTEFEATTCSLEELlrteQQRLEKNEDQLKiitMELQKKSSELEEMTKFKNNKEVELEELKKILAEdek 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1265 LKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEiKAKNALAHAlqssrh 1344
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKE-KLKNIELTA------ 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1345 DCDLLREQYEEEQESKAELQRALSKANTEVAQWRtKYETDAIQRTEELEEAKKKLAQRLQAAEEHV----EAVNAKCASL 1420
Cdd:pfam05483 493 HCDKLLLENKELTQEASDMTLELKKHQEDIINCK-KQEERMLKQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1421 EKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILaewkqkcEETHAELEASQKEARSLGTELfkikNAYEESLDQ 1500
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI-------EELHQENKALKKKGSAENKQL----NAYEIKVNK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1501 LETLKRENKNLQQEISDLTEQIAEgGKRIHElEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR 1580
Cdd:pfam05483 641 LELELASAKQKFEEIIDNYQKEIE-DKKISE-EKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDK 718
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 153791586 1581 KIAEKDEEIDqLKRNHIRIVESMQSTLDAEIRS-RNDAIRLKKKMEGDLNEME 1632
Cdd:pfam05483 719 IIEERDSELG-LYKNKEQEQSSAKAALEIELSNiKAELLSLKKQLEIEKEEKE 770
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
849-1615 |
1.05e-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: 76.93 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 849 AETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV 928
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 929 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEA 1008
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1009 HQ--QTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKL 1086
Cdd:pfam02463 435 EEesIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1087 KKKEFEISNLQSKIEDEQALGIQLQKkiKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQ 1166
Cdd:pfam02463 515 LIKDGVGGRIISAHGRLGDLGVAVEN--YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLK 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1167 IEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQ--IDNLQRVKQKLEKEKSEMKMEIDDLASNVETV 1244
Cdd:pfam02463 593 SIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKesAKAKESGLRKGVSLEEGLAEKSEVKASLSELT 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1245 SKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQ 1324
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1325 LEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQ 1404
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1405 AAEEHVEAVnakcaSLEKTKQRLQNEVEDLMLDVERTNAACAA---LDKKQRNFDKILAEWKQKCEETHAELEASQKEAR 1481
Cdd:pfam02463 833 EELEELALE-----LKEEQKLEKLAEEELERLEEEITKEELLQellLKEEELEEQKLKDELESKEEKEKEEKKELEEESQ 907
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1482 SLGTELFKIKnaYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIH--ELEKIKKQVEQEKCELQAALEEAEASLEH 1559
Cdd:pfam02463 908 KLNLLEEKEN--EIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNkeEEEERNKRLLLAKEELGKVNLMAIEEFEE 985
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791586 1560 EEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRN 1615
Cdd:pfam02463 986 KEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLE 1041
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1032-1627 |
1.06e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.88 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1032 KLEQQVDDLEGSLEQEKKLRMDLERAKRKLE--GDLKLAQESIMDIENEKQQLDEklkkkefeisnLQSKIEDEQAlgiq 1109
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEY-----------LRAALRLWFA---- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1110 lQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIE-----MNKKRE------AEFQ 1178
Cdd:COG4913 287 -QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEreierLERELEererrrARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1179 KMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGN----LEKM 1254
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNiparLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1255 CRTLEDQLS-------------ELKSKEEEQQ----RLINDltaQRGRLQTEsgefSRQLDEKEALVSQLSRGKQAFTQQ 1317
Cdd:COG4913 446 RDALAEALGldeaelpfvgeliEVRPEEERWRgaieRVLGG---FALTLLVP----PEHYAAALRWVNRLHLRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1318 IEELKRQLEEEIKAKNALAHALQSSRHDC-DLLREQYEEEQ-----ESKAELQRAlSKANTE---VAQWRTKYE------ 1382
Cdd:COG4913 519 VRTGLPDPERPRLDPDSLAGKLDFKPHPFrAWLEAELGRRFdyvcvDSPEELRRH-PRAITRagqVKGNGTRHEkddrrr 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1383 --------TDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQN--EVEDLMLDVERTNAACAALdkkq 1452
Cdd:COG4913 598 irsryvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL---- 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1453 rnfdkilaewkqkcEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHEL 1532
Cdd:COG4913 674 --------------EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1533 EKIKKQVEQEKCELQAALEEAEASLEheegkilRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIR 1612
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAVER-------ELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLE 812
|
650
....*....|....*
gi 153791586 1613 SRNDAIRLKKKMEGD 1627
Cdd:COG4913 813 SLPEYLALLDRLEED 827
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1316-1920 |
1.10e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.88 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1316 QQIEELKRQLEEEIKAKNALAHALQssrhdcdlLREQYEEEQESKAELQRALSKANTEVAQwrTKYETdAIQRTEELEEA 1395
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRE--------LAERYAAARERLAELEYLRAALRLWFAQ--RRLEL-LEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1396 KKKLAQRLQAAEEHVEAVNAKCASLEKtkQRLQN---EVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAE 1472
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEA--QIRGNggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1473 LEASQKEARSLGTELFKIKNAYEESLDQLETLKREnknLQQEISDLTEQIAEggkriheLEKIKKQVEQEkceLQAALEE 1552
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIAS-------LERRKSNIPAR---LLALRDA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1553 AEASLEHEEGKiLRIQLELNQVKSE--------------------VD-RKIAEKDEEIDQLK-RNHIRIvESMQSTLDAE 1610
Cdd:COG4913 449 LAEALGLDEAE-LPFVGELIEVRPEeerwrgaiervlggfaltllVPpEHYAAALRWVNRLHlRGRLVY-ERVRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1611 IRSRNDAIRLKKKMEGDLNEMEIQLNH--ANRMA------AEALRNYRntQGILKDTQIHLDDALRS---QEDLKEQLAM 1679
Cdd:COG4913 527 ERPRLDPDSLAGKLDFKPHPFRAWLEAelGRRFDyvcvdsPEELRRHP--RAITRAGQVKGNGTRHEkddRRRIRSRYVL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1680 ---VERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHtqntslintkkkletDISQMQGEMEDILQEARN 1756
Cdd:COG4913 605 gfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ---------------RLAEYSWDEIDVASAERE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1757 AEEKAkkaitdaammaEELKKEQDTSAHLERMkknmEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEVES-- 1834
Cdd:COG4913 670 IAELE-----------AELERLDASSDDLAAL----EEQLEELEAELEELEE--------ELDELKGEIGRLEKELEQae 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1835 -EQKRNAEAVKGLRkhERRVKELTYQTEEDRKNIL---RLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKlQHELE 1910
Cdd:COG4913 727 eELDELQDRLEAAE--DLARLELRALLEERFAAALgdaVERELRENLEERIDALRARLNRAEEELERAMRAFNR-EWPAE 803
|
650
....*....|
gi 153791586 1911 EAEERADIAE 1920
Cdd:COG4913 804 TADLDADLES 813
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1279-1809 |
5.24e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 74.69 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1279 LTAQRGRLqtesGEFSRQLDEKEA--LVSQLSRGKQAFTQQIEELKRQLEEEIKAKnalahalqSSRHDCDLLREQYEEE 1356
Cdd:PRK02224 182 LSDQRGSL----DQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQAR--------ETRDEADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1357 QESKAELQRALSKANTEVAQWRTKYET------DAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNE 1430
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREElaeevrDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1431 VEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEARS-------LGTELFKIKNAYEESLDQLET 1503
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDrreeieeLEEEIEELRERFGDAPVDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1504 LKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQ--------------EKCELQAALEEAEASLEHEEGKILRIQL 1569
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1570 ELNQVKSEVDR--KIAEKDEEIDQLKRNHIRIVESMqSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALR 1647
Cdd:PRK02224 490 EVEEVEERLERaeDLVEAEDRIERLEERREDLEELI-AERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1648 NYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERranlLQAEIEELRATLEQ-----TERSRKIAEQelldaSERVQLL 1722
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLERIRTLLAAIAD----AEDEIERLREKREAlaelnDERRERLAEK-----RERKREL 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1723 HTQN-----TSLINTKKKLETDISQMQGEMEDiLQEARNAEEKAKKAITDAAMMAEELKKEQDTsahlermkknMEQTVK 1797
Cdd:PRK02224 640 EAEFdeariEEAREDKERAEEYLEQVEEKLDE-LREERDDLQAEIGAVENELEELEELRERREA----------LENRVE 708
|
570
....*....|..
gi 153791586 1798 DLQLRLDEAEQL 1809
Cdd:PRK02224 709 ALEALYDEAEEL 720
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
852-1546 |
6.16e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 74.62 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 852 EKEMATMKEEFQKIKDELAKSEAKRKELEEKMV--TLLKEKNDLQLQVQAEAEGLADAEERCDQLIKtKIQLEAKIKEVT 929
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYLTQKREAQEEQLKkqQLLKQLRARIEELRAQEAVLEETQERINRARK-AAPLAAHIKAVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 930 ERAEDEEEINAELTAKKRKLEDE---CSELKKDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQ 1006
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLlmkRAAHVKQQSSIE-EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1007 EAHQQtlddLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQldekL 1086
Cdd:TIGR00618 383 TLQQQ----KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQC----E 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1087 KKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERleeagGATSAQ 1166
Cdd:TIGR00618 455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNP-----GPLTRR 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1167 IEMNKKREAEFQKmrrdlEEATLQHEATAATLRkkhadsVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSK 1246
Cdd:TIGR00618 530 MQRGEQTYAQLET-----SEEDVYHQLTSERKQ------RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1247 AKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLE 1326
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1327 EeikaknALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETdaiqRTEELEEAKKKLAQRLQAA 1406
Cdd:TIGR00618 679 Q------LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSS----LGSDLAAREDALNQSLKEL 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1407 EEhvEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAAcAALDKKQRNFDKILAEWKQKCEEThaeleasQKEARSLGTE 1486
Cdd:TIGR00618 749 MH--QARTVLKARTEAHFNNNEEVTAALQTGAELSHLA-AEIQFFNRLREEDTHLLKTLEAEI-------GQEIPSDEDI 818
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1487 LFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCEL 1546
Cdd:TIGR00618 819 LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1378-1891 |
7.74e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 7.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1378 RTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVN-------AKCASLEKTKQRLQ---NEVEDLMLDVERTNAACAA 1447
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISselpelrEELEKLEKEVKELEelkEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1448 LDKKQRNFDKILAEWKQKCEETHaELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGK 1527
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1528 RIHELEKIKKQVEqekcELQAALEEAEASLEHEEgKILRIQLELNQVKSEV-DRKIAEKDEEIDQLKR------NHIRIV 1600
Cdd:PRK03918 336 KEERLEELKKKLK----ELEKRLEELEERHELYE-EAKAKKEELERLKKRLtGLTPEKLEKELEELEKakeeieEEISKI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1601 ESMQSTLDAEIRSRNDAI-----------------------RLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILK 1657
Cdd:PRK03918 411 TARIGELKKEIKELKKAIeelkkakgkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1658 DtqihlDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQT--ERSRKIAEQ--ELLDASERVQLLHTQNTSLINTK 1733
Cdd:PRK03918 491 K-----ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKlkEKLIKLKGEikSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1734 KKLETDISQMQGEMEDI--------------LQEARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTVKDL 1799
Cdd:PRK03918 566 DELEEELAELLKELEELgfesveeleerlkeLEPFYNEYLELKDAEKELEREEKELKKLEEE---LDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1800 QLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDL------ 1873
Cdd:PRK03918 643 EELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLekaler 722
|
570
....*....|....*...
gi 153791586 1874 VDKLQAKVKSYKRQAEEA 1891
Cdd:PRK03918 723 VEELREKVKKYKALLKER 740
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
852-1430 |
1.02e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 852 EKEMATMKEEFQKIKDELAKSEAKRKELEEkmvtLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTER 931
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARETRDEADE----VLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 932 AEDEEEINAELTAK-------KRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKA 1004
Cdd:PRK02224 288 LEELEEERDDLLAEaglddadAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1005 LQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDD----LEGSLEQEKKLRMDLERAKRK---LEGDLKLAQESImdieN 1077
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDapvdLGNAEDFLEELREERDELREReaeLEATLRTARERV----E 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1078 EKQQLDEKLKKKEFEisnlQSKIEDEQALGIqlqkkikelqarieeleeeiEAERASRAKAEKQRSDLSRELEEISERLE 1157
Cdd:PRK02224 444 EAEALLEAGKCPECG----QPVEGSPHVETI--------------------EEDRERVEELEAELEDLEEEVEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1158 EAGGATSAQIEMNKKREAefqkmRRDLEEATLQHEATaatlrkkhadsVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDL 1237
Cdd:PRK02224 500 RAEDLVEAEDRIERLEER-----REDLEELIAERRET-----------IEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1238 ASNVETVSKAKGNLEKMCRTLEDQLSELKsKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSrgkqaftqq 1317
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR--------- 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1318 ieELKRQLEEEIKAKnalahALQSSRHDcdllREQYEEEQESKAELQRALSKANTEVaQWRTKYETDAIQRTEELEEAKK 1397
Cdd:PRK02224 634 --ERKRELEAEFDEA-----RIEEARED----KERAEEYLEQVEEKLDELREERDDL-QAEIGAVENELEELEELRERRE 701
|
570 580 590
....*....|....*....|....*....|...
gi 153791586 1398 KLAQRLQAaeehVEAVNAKCASLEKTKQRLQNE 1430
Cdd:PRK02224 702 ALENRVEA----LEALYDEAEELESMYGDLRAE 730
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1261-1927 |
1.61e-12 |
|
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: 73.29 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1261 QLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQ-----------------LSRGKQAFTQQIEELKR 1323
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQlqaetelcaeaeemrarLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1324 QLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQraLSKANTEVAQwrTKYETDAI---QRTEELEEAKKKLA 1400
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQ--LEKVTTEAKI--KKLEEDILlleDQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1401 QRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEA 1480
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1481 RSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHE 1560
Cdd:pfam01576 239 AKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1561 EGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANR 1640
Cdd:pfam01576 319 QELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1641 MAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMverranlLQAEIEELRATLEQTERSRKIAEQELLDASERVQ 1720
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK-------LQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1721 LLHTQNTSLINTKKKLETDISQMQGEmEDILQEARNAEEKAKKAITdaammaeelKKEQDTSAHLERMKKNMEQTVKDLQ 1800
Cdd:pfam01576 472 DTQELLQEETRQKLNLSTRLRQLEDE-RNSLQEQLEEEEEAKRNVE---------RQLSTLQAQLSDMKKKLEEDAGTLE 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1801 lrldeaeqlALKGGKKQIQklearvRELEGEVESEQKRnAEAVKGLRKHERRVKE----LTYQTEEDRKNILRL---QDL 1873
Cdd:pfam01576 542 ---------ALEEGKKRLQ------RELEALTQQLEEK-AAAYDKLEKTKNRLQQelddLLVDLDHQRQLVSNLekkQKK 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791586 1874 VDKLQAKVKS----YKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLR 1927
Cdd:pfam01576 606 FDQMLAEEKAisarYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLR 663
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1247-1911 |
1.63e-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: 73.23 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1247 AKGNLEKMCRTLEDQLSELKSKEEEQQRLINDltaQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLE 1326
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEK---QKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1327 ---EEIKAKNALAH-ALQSSRHDCDLLREQYEEEQESKAELQRALskANTEVAQWRTKYETDAIQRT------------- 1389
Cdd:pfam15921 149 ntvHELEAAKCLKEdMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL--VDFEEASGKKIYEHDSMSTMhfrslgsaiskil 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1390 EELEEAKKKLAQRLQAAEEHVEAVNAKCAS-LEKTKQRLQNEVEDLMLDVErtnAACAALDKKQrnfdkilAEWKQKCEE 1468
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEALKSESQNkIELLLQQHQDRIEQLISEHE---VEITGLTEKA-------SSARSQANS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1469 THAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNL-QQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQ 1547
Cdd:pfam15921 297 IQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1548 AALE---------EAEASLEHEEGKILRIQLELNQVK-SEVDRKIAEKDEEIDQLKRnhirIVESMQSTLDAEIRSRNDA 1617
Cdd:pfam15921 377 DQLQklladlhkrEKELSLEKEQNKRLWDRDTGNSITiDHLRRELDDRNMEVQRLEA----LLKAMKSECQGQMERQMAA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1618 IRLKKKMEGDLNEMEIQLNHANRMAAEALRNyrntqgiLKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRAT 1697
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEMLRKVVEE-------LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1698 LEqtersrkIAEQELldaservQLLHTQNTSLINTKKKLETDISQMQGE---MEDILQEARNaeekakkaitdaamMAEE 1774
Cdd:pfam15921 526 VD-------LKLQEL-------QHLKNEGDHLRNVQTECEALKLQMAEKdkvIEILRQQIEN--------------MTQL 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1775 LKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLAlkggkkqiQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVK 1854
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILK--------DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVK 649
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1855 ELTYQTE----EDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEE 1911
Cdd:pfam15921 650 DIKQERDqllnEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1075-1941 |
2.03e-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: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1075 IENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEeieaeRASRAKAEKQRSDLSRELEEISE 1154
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEEL-----KLQELKLKEQAKKALEYYQLKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1155 RLEEAGGATSAQIEmnkKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKS------ 1228
Cdd:pfam02463 219 LELEEEYLLYLDYL---KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKllakee 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1229 -EMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQL 1307
Cdd:pfam02463 296 eELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1308 SRGKQAFTQQIEELKRQLEEEikaknaLAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQ 1387
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEE------LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1388 RTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTkqrlQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCE 1467
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ----LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRII 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1468 ETHAELE--ASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCE 1545
Cdd:pfam02463 526 SAHGRLGdlGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1546 LQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKME 1625
Cdd:pfam02463 606 AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1626 GDLNEMEIQLNHANRMAAEALRNYRNTQgILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSR 1705
Cdd:pfam02463 686 ESELAKEEILRRQLEIKKKEQREKEELK-KLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1706 KIAEQELLDASERVQLLHTQNTSLINTKKKLET--------DISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKK 1777
Cdd:pfam02463 765 EKSELSLKEKELAEEREKTEKLKVEEEKEEKLKaqeeelraLEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1778 EQDTSAHLERMKK--NMEQTVKDLQLRLDEAEQLALKGGKKQ-IQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVK 1854
Cdd:pfam02463 845 EQKLEKLAEEELErlEEEITKEELLQELLLKEEELEEQKLKDeLESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIK 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1855 ELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSREVH 1934
Cdd:pfam02463 925 EEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEK 1004
|
....*..
gi 153791586 1935 TKVISEE 1941
Cdd:pfam02463 1005 KKLIRAI 1011
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1212-1933 |
3.64e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.10 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1212 QIDNLQRVKQKLEKEKSEMKMEIDDLASNV--ETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTE 1289
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRadEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAED 1138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1290 SGEFSRQLDEKEALVSQLSRgkqaftqQIEElKRQLEEEIKAKNAlaHALQSSRHDCDLLREQYEEEQESKAELQRALSK 1369
Cdd:PTZ00121 1139 ARKAEEARKAEDAKRVEIAR-------KAED-ARKAEEARKAEDA--KKAEAARKAEEVRKAEELRKAEDARKAEAARKA 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1370 ANTEVAQWRTKYETDA-IQRTEELEEAKKKlaqrlqaAEEhveavnAKCASLEKTKQRLQNEVEDLMLDVERTNAACAAL 1448
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKkAEAVKKAEEAKKD-------AEE------AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1449 DKKQrnfdkilAEWKQKCEETHAELEASQKEARSLGTELfkiKNAYEEsldqletlKRENKNLQQEISDLTEQIAEGGKR 1528
Cdd:PTZ00121 1276 EARK-------ADELKKAEEKKKADEAKKAEEKKKADEA---KKKAEE--------AKKADEAKKKAEEAKKKADAAKKK 1337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1529 IhelEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLElnQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLD 1608
Cdd:PTZ00121 1338 A---EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA--KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK 1412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1609 AEiRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEqlAMVERRANLLQ 1688
Cdd:PTZ00121 1413 AA-AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK--AEEAKKADEAK 1489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1689 AEIEELRatlEQTERSRKIAEQelldaservqllhtqntslintKKKLEtdiSQMQGEMEDILQEARNAEEKAKkaiTDA 1768
Cdd:PTZ00121 1490 KKAEEAK---KKADEAKKAAEA----------------------KKKAD---EAKKAEEAKKADEAKKAEEAKK---ADE 1538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1769 AMMAEELKKEQDTSaHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKglRK 1848
Cdd:PTZ00121 1539 AKKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--KA 1615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1849 HERRVK-ELTYQTEEDRKNILRLQDLVDKLQAKVKSYkRQAEEAEEQSNTNLAKF----RKLQHELEEAEERADIAESQV 1923
Cdd:PTZ00121 1616 EEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEEL-KKAEEENKIKAAEEAKKaeedKKKAEEAKKAEEDEKKAAEAL 1694
|
730
....*....|
gi 153791586 1924 NKLRVKSREV 1933
Cdd:PTZ00121 1695 KKEAEEAKKA 1704
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
852-1765 |
3.81e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 72.00 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 852 EKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKekndlqlqvqaeaegladaeercdqliktkiqLEAKIKEVTER 931
Cdd:TIGR00606 230 EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMK--------------------------------LDNEIKALKSR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 932 AEDEEEINAELTAKKRKLEDECSELKKDIDdleltlakvekekHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAH-- 1009
Cdd:TIGR00606 278 KKQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKte 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1010 ---QQTLDDLQAEEDKVNTLTKAKIKLEQQ----VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQL 1082
Cdd:TIGR00606 345 llvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1083 DEKLKKKEFEISNLQSKIEDEQalgIQLQKKIKELQARIEELEeeieaerasraKAEKQRSDLSRELEEISERLEEAGGA 1162
Cdd:TIGR00606 425 QEQADEIRDEKKGLGRTIELKK---EILEKKQEELKFVIKELQ-----------QLEGSSDRILELDQELRKAERELSKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1163 -TSAQIEMNKKREAEFQKMRRDLEEaTLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNV 1241
Cdd:TIGR00606 491 eKNSLTETLKKEVKSLQNEKADLDR-KLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYF 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1242 ETVskakgnlekmcRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSR------GKQAFT 1315
Cdd:TIGR00606 570 PNK-----------KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcGSQDEE 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1316 QQIEELKRQLEEEIKAKNALAHALQssrhdcdlLREQYEEEQESKaelqralSKANTEVAQwrtkyetDAIQRTEELEEA 1395
Cdd:TIGR00606 639 SDLERLKEEIEKSSKQRAMLAGATA--------VYSQFITQLTDE-------NQSCCPVCQ-------RVFQTEAELQEF 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1396 KKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELE- 1474
Cdd:TIGR00606 697 ISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGt 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1475 --ASQKEARSLGTELFKIKNAYEEsldqletLKRENKNLQQEISDLteQIAEGGKRIHELEKIKKQVEQEKCELQAALEE 1552
Cdd:TIGR00606 777 imPEEESAKVCLTDVTIMERFQME-------LKDVERKIAQQAAKL--QGSDLDRTVQQVNQEKQEKQHELDTVVSKIEL 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1553 AEASLEHEEGKILRIQLELNQVKSEvDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEME 1632
Cdd:TIGR00606 848 NRKLIQDQQEQIQHLKSKTNELKSE-KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1633 IQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKE-QLAMVERRANLLQAEIEELRATLEQTERSRKIAEQE 1711
Cdd:TIGR00606 927 ELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDdYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQD 1006
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791586 1712 LLDASERVQLLHTQNTSLI--NTKKKLETDISQMQGEM-EDILQEARNAEEKAKKAI 1765
Cdd:TIGR00606 1007 IDTQKIQERWLQDNLTLRKreNELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENI 1063
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1043-1940 |
3.97e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 72.00 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1043 SLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKiEDEQALGIQLQKKIKELQARIE 1122
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY-ENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1123 ELEeeieAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREA-EFQKMRRDLEEATLQHEATAATLRKK 1201
Cdd:TIGR00606 266 KLD----NEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1202 HADSVAELGE-----QIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQ-------LSELKSKE 1269
Cdd:TIGR00606 342 KTELLVEQGRlqlqaDRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEaktaaqlCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1270 EEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLL 1349
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1350 REQYeeEQESKAELQRALSKANTEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQAAE-EHVEAVNAKCA------SLEK 1422
Cdd:TIGR00606 502 EVKS--LQNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQIRKIKsRHSDELTSLLGyfpnkkQLED 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1423 TKQRLQNEVEDLMLDVERTNAACAALDKKQ---RNFDKILAEWKQKCEETHAELEASQKEARSLGtelfKIKNAYEESLD 1499
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELASLEQNKnhiNNELESKEEQLSSYEDKLFDVCGSQDEESDLE----RLKEEIEKSSK 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1500 QLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQV----- 1574
Cdd:TIGR00606 654 QRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglap 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1575 --KSEVDRKIAEKDEEIDQLK---------RNHIRIVESMQSTLDAEIRSRND-----AIRLKKKMEGDLNEMEIQLNHA 1638
Cdd:TIGR00606 734 grQSIIDLKEKEIPELRNKLQkvnrdiqrlKNDIEEQETLLGTIMPEEESAKVcltdvTIMERFQMELKDVERKIAQQAA 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1639 NRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEEL---RATLEQTERSRKIAEQELLDA 1715
Cdd:TIGR00606 814 KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELkseKLQIGTNLQRRQQFEEQLVEL 893
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1716 SERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQearNAEEKAKKAITDAAMMAEELKK--------EQDTSAHLER 1787
Cdd:TIGR00606 894 STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS---SKETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDD 970
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1788 MKKNMEQTVKDLQLRLDEAEQlalkgGKKQIQKlEARVRELEGEVESEQKRNAEAVKGLRKHERRVKEL-----TYQTEE 1862
Cdd:TIGR00606 971 YLKQKETELNTVNAQLEECEK-----HQEKINE-DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVeeelkQHLKEM 1044
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1863 DRKNILRLQDLVDKLQAKVKSYKR-------QAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSREVHT 1935
Cdd:TIGR00606 1045 GQMQVLQMKQEHQKLEENIDLIKRnhvlalgRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYY 1124
|
....*
gi 153791586 1936 KVISE 1940
Cdd:TIGR00606 1125 KTLDQ 1129
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1249-1904 |
6.37e-12 |
|
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: 70.94 E-value: 6.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1249 GNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQL-------DEKEALVSQLSrGKQAFTQQIEEL 1321
Cdd:pfam07111 59 QALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAvaekagqAEAEGLRAALA-GAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1322 KRQLEEEIKA--KNALAHALQSSRHDCDLLREQYE--EEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKK 1397
Cdd:pfam07111 138 SQRELEEIQRlhQEQLSSLTQAHEEALSSLTSKAEglEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1398 KLAQRLQ--AAEEHVEAVNAKCASLEKtkQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILA----EWKQKCEETHA 1471
Cdd:pfam07111 218 TLVESLRkyVGEQVPPEVHSQTWELER--QELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLAlqeeELTRKIQPSDS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1472 ELEASQKEARSLgtelfkIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEggkrihELEKIKKQvEQEKCELQAALE 1551
Cdd:pfam07111 296 LEPEFPKKCRSL------LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAE------LQEQVTSQ-SQEQAILQRALQ 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1552 EAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKrnhiRIVESMQSTldaeirsrndAIRLKKKMeGDLNEM 1631
Cdd:pfam07111 363 DKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLK----FVVNAMSST----------QIWLETTM-TRVEQA 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1632 EIQLNHANRMAAEALRNYRNTQGILKD----TQIHLDDALRSQE------DLKEQLAMVERRANLLQAEIeELRATLEQT 1701
Cdd:pfam07111 428 VARIPSLSNRLSYAVRKVHTIKGLMARkvalAQLRQESCPPPPPappvdaDLSLELEQLREERNRLDAEL-QLSAHLIQQ 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1702 ERSRKIAEQElldaSERVQllhtqntsLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQdt 1781
Cdd:pfam07111 507 EVGRAREQGE----AERQQ--------LSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQ-- 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1782 sahlERMKKNMEQTVKDLQLRLDEaeqlalkggkkQIQKLEARVRElegevesEQKRNAEAVKGLRKHERRVKeltyQTE 1861
Cdd:pfam07111 573 ----EIYGQALQEKVAEVETRLRE-----------QLSDTKRRLNE-------ARREQAKAVVSLRQIQHRAT----QEK 626
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 153791586 1862 EDRKNILRLQDLVDKLQAkvKSYKRQAEEAEEQSNTNLAKFRK 1904
Cdd:pfam07111 627 ERNQELRRLQDEARKEEG--QRLARRVQELERDKNLMLATLQQ 667
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1390-1929 |
6.80e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 70.92 E-value: 6.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1390 EELEEAKKKLAQRLQAAEE-HveavnakcaslEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEE 1468
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNElH-----------EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1469 THAELEAsqkeARSLGTELFKIKNAyeeSLDQLETLKRENKNLQQEISDLTEQIAEG-GKRIHELEKIKK-QVEQEKCEL 1546
Cdd:pfam15921 150 TVHELEA----AKCLKEDMLEDSNT---QIEQLRKMMLSHEGVLQEIRSILVDFEEAsGKKIYEHDSMSTmHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1547 QAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIaekdeeiDQLKRNHirivesmqstldaeirsrndairlKKKMEG 1626
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALKSESQNKI-------ELLLQQH------------------------QDRIEQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1627 DLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQihlddalrsqEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRK 1706
Cdd:pfam15921 272 LISEHEVEITGLTEKASSARSQANSIQSQLEIIQ----------EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1707 IAEQELldaservqllhTQNTSLINTkkkletDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLE 1786
Cdd:pfam15921 342 DKIEEL-----------EKQLVLANS------ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1787 RMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKn 1866
Cdd:pfam15921 405 DRDTGNSITIDHLRRELDDRNM--------EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE- 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791586 1867 ilRLQDLVDKLQAkvksyKRQAEEAEEQSNTNLAKfrklqhELEEAEERADIAESQVNKLRVK 1929
Cdd:pfam15921 476 --MLRKVVEELTA-----KKMTLESSERTVSDLTA------SLQEKERAIEATNAEITKLRSR 525
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
841-1333 |
8.67e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 8.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 841 KIKPLLKSAETEKEMATMKEEFQKIKDElaksEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLiKTKIQ 920
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKAD----AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA-KKKAE 1428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 921 LEAKIKEVTERAEDEEEinAELTAKKRKLEDECSELKKdiddleltlaKVEKEKHATENKVKnlTEEMAGLDETIAKLTK 1000
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKK--ADEAKKKAEEAKKAEEAKK----------KAEEAKKADEAKKK--AEEAKKADEAKKKAEE 1494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1001 EKKALQEAHQQTLDDLQAEEDKvntltkaKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgDLKLAQEsiMDIENEKQ 1080
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAK-------KAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD-ELKKAEE--LKKAEEKK 1564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1081 QLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDlsrelEEISERLEEAg 1160
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKKVEQL- 1638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1161 gatsaqiemnKKREAEFQKMRRDLEEATLQHEATAATLRKKHADS--VAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLA 1238
Cdd:PTZ00121 1639 ----------KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1239 SNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGrlqtESGEFSRQLDEKEALVSQLSRGKQAFTQQ- 1317
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE----EKKKIAHLKKEEEKKAEEIRKEKEAVIEEe 1784
|
490
....*....|....*...
gi 153791586 1318 --IEELKRQLEEEIKAKN 1333
Cdd:PTZ00121 1785 ldEEDEKRRMEVDKKIKD 1802
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1065-1756 |
1.05e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 70.64 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1065 LKLAQESimdieNEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAekQRSD 1144
Cdd:pfam12128 244 TKLQQEF-----NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSA--ADAA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1145 LSRELEEIsERLEEAGGA-TSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKL 1223
Cdd:pfam12128 317 VAKDRSEL-EALEDQHGAfLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1224 EKEKSEMKMEIDDLASNVEtvskakGNLEKMCRTLEDQLSELKSK-EEEQQRLINDLTAQRGRLQTESGEfSRQLDEKEA 1302
Cdd:pfam12128 396 KDKLAKIREARDRQLAVAE------DDLQALESELREQLEAGKLEfNEEEYRLKSRLGELKLRLNQATAT-PELLLQLEN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1303 LVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRhdcdlLREQYEEEQESK-AELQRALSKA--------NTE 1373
Cdd:pfam12128 469 FDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALR-----QASRRLEERQSAlDELELQLFPQagtllhflRKE 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1374 VAQWRtkyetDAIQRTeeleeAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNevedlmLDVERTNAACAALDKKQR 1453
Cdd:pfam12128 544 APDWE-----QSIGKV-----ISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKR------IDVPEWAASEEELRERLD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1454 NFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISD-LTEQIAEGGKRIHEL 1532
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKaLAERKDSANERLNSL 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1533 EKIKKQVEQEkceLQAALEEA-EASLEHEEGKilriQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEI 1611
Cdd:pfam12128 688 EAQLKQLDKK---HQAWLEEQkEQKREARTEK----QAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDL 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1612 RSRN-DAIRLKKkMEGDLNEMEIQLNHANRMAAEALRN---YRNTQGILKDT-QIHLDDALRSQEDLKEQLAMVERRANL 1686
Cdd:pfam12128 761 ASLGvDPDVIAK-LKREIRTLERKIERIAVRRQEVLRYfdwYQETWLQRRPRlATQLSNIERAISELQQQLARLIADTKL 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1687 LQAEIEELRATLEQTE------------RSRKIAEQELLDASERVQLlhtqntSLINTKKKLETDISQMQGEMEDILQEA 1754
Cdd:pfam12128 840 RRAKLEMERKASEKQQvrlsenlrglrcEMSKLATLKEDANSEQAQG------SIGERLAQLEDLKLKRDYLSESVKKYV 913
|
..
gi 153791586 1755 RN 1756
Cdd:pfam12128 914 EH 915
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1226-1808 |
1.39e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.94 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1226 EKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEdQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQ-LDEKEALV 1304
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAALRLWFAQRrLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1305 SQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHD-CDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYET 1383
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1384 DAiqrtEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVertnaacAALDKKQRNFD----KIL 1459
Cdd:COG4913 378 SA----EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI-------ASLERRKSNIParllALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1460 AEWKQkceethaELEASQKEARSLGtELFKIKNAYEESLDQLETLKRENK-------NLQQEISDLTEQIAEGGK-RIHE 1531
Cdd:COG4913 447 DALAE-------ALGLDEAELPFVG-ELIEVRPEEERWRGAIERVLGGFAltllvppEHYAAALRWVNRLHLRGRlVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1532 LEKIKKQVEQEKCELQAALEEaeasLEHEEGKILR-IQLELNQvksevdRKIAEKDEEIDQLKRNHIRIVESMQSTLDAE 1610
Cdd:COG4913 519 VRTGLPDPERPRLDPDSLAGK----LDFKPHPFRAwLEAELGR------RFDYVCVDSPEELRRHPRAITRAGQVKGNGT 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1611 ---------IRSRN----DAIRLKKKMEGDLNEMEIQLNHANRmAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQL 1677
Cdd:COG4913 589 rhekddrrrIRSRYvlgfDNRAKLAALEAELAELEEELAEAEE-RLEALEAELDALQERREALQRLAEYSWDEIDVASAE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1678 AMVERranlLQAEIEELRAT---LEQTERSRKIAEQELLDASERVQLLHTQntslintKKKLETDISQMQGEMEDILQEA 1754
Cdd:COG4913 668 REIAE----LEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGE-------IGRLEKELEQAEEELDELQDRL 736
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 153791586 1755 RNAEEKAKKAITDAammAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQ 1808
Cdd:COG4913 737 EAAEDLARLELRAL---LEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
835-1880 |
1.64e-11 |
|
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: 70.08 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 835 WMKLFFKIKPLL-----KSAETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTlLKEKNDLQLQVQAEAEGLADAEE 909
Cdd:TIGR01612 556 WKKLIHEIKKELeeeneDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKN-ISDKNEYIKKAIDLKKIIENNNA 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 910 RCDQLIKTKIQleakikEVTERAEDEEEINAELTAKKRKLEDEcselkkDIDDLELTLAKVEKekhatENKVKNlTEEMA 989
Cdd:TIGR01612 635 YIDELAKISPY------QVPEHLKNKDKIYSTIKSELSKIYED------DIDALYNELSSIVK-----ENAIDN-TEDKA 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 990 GLDETIAKLTKEKKALQEAHQQTLD-DLQAEEDKVNTLTKAKIKLEQQVDDlegslEQEKKLRMDLERAKRKlegdLKLA 1068
Cdd:TIGR01612 697 KLDDLKSKIDKEYDKIQNMETATVElHLSNIENKKNELLDIIVEIKKHIHG-----EINKDLNKILEDFKNK----EKEL 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1069 QESIMDIENEKQQLDeKLKKKefeISNLQSKIEDEQALgiqlqKKIKElqarieeleeeieaerasraKAEKQRSDLSRE 1148
Cdd:TIGR01612 768 SNKINDYAKEKDELN-KYKSK---ISEIKNHYNDQINI-----DNIKD--------------------EDAKQNYDKSKE 818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1149 -LEEISERLEEaggaTSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQI--DNLQRVKQKLEK 1225
Cdd:TIGR01612 819 yIKTISIKEDE----IFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEIsdDKLNDYEKKFND 894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1226 EKS---EMKMEIDDLASNVETVSKAKGNLeKMCRTLEDQLSELKSKeeeqQRLINDLTAQRGRLQTESGEFSRQLDEK-- 1300
Cdd:TIGR01612 895 SKSlinEINKSIEEEYQNINTLKKVDEYI-KICENTKESIEKFHNK----QNILKEILNKNIDTIKESNLIEKSYKDKfd 969
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1301 EALVSQLSRGKQAFTQ-QIEELKRQLEEEIKAKNALAHALQSSRHdcDLLREQYEEEQESKAELQRALSKANTEVAQWRT 1379
Cdd:TIGR01612 970 NTLIDKINELDKAFKDaSLNDYEAKNNELIKYFNDLKANLGKNKE--NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEI 1047
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1380 KYETDAIQRTEELEEAKKKLAQRLQaaEEHVEAVNAKCASLEKTKQRLqnevedlmldvertnaacaaldkKQRNFDKIL 1459
Cdd:TIGR01612 1048 AIHTSIYNIIDEIEKEIGKNIELLN--KEILEEAEINITNFNEIKEKL-----------------------KHYNFDDFG 1102
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1460 AEWKQKCEEthaeleasqkEARSLGTELFKIKNAYEESLDQLETLKRENKN----LQQEISDLtEQIAEGGKRIHELEKI 1535
Cdd:TIGR01612 1103 KEENIKYAD----------EINKIKDDIKNLDQKIDHHIKALEEIKKKSENyideIKAQINDL-EDVADKAISNDDPEEI 1171
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1536 KKQVEQ--EKCELQAALEEAEASLEHEEGKILRIQLELNQVKS-------EVDRKIAEKDEEIDQLKRNHIRIVESMQST 1606
Cdd:TIGR01612 1172 EKKIENivTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGinlsygkNLGKLFLEKIDEEKKKSEHMIKAMEAYIED 1251
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1607 LDaEIRSRNDAIRLKKKMEGDLN-EME--------------IQLNHANRMAAEALRNYRNTQG---------ILKDTQIH 1662
Cdd:TIGR01612 1252 LD-EIKEKSPEIENEMGIEMDIKaEMEtfnishdddkdhhiISKKHDENISDIREKSLKIIEDfseesdindIKKELQKN 1330
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1663 LDDALRSQEDLKEQLAMVERRANLLQAE-----IEELRATLEQTERSRKIAEQElLDASERVQLLHTQNTSLINTKKKLE 1737
Cdd:TIGR01612 1331 LLDAQKHNSDINLYLNEIANIYNILKLNkikkiIDEVKEYTKEIEENNKNIKDE-LDKSEKLIKKIKDDINLEECKSKIE 1409
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1738 TD---------ISQMQGEMEDILQEA-------RNAEE-------------------------KAKKAITDAAMMAEELK 1776
Cdd:TIGR01612 1410 STlddkdidecIKKIKELKNHILSEEsnidtyfKNADEnnenvlllfkniemadnksqhilkiKKDNATNDHDFNINELK 1489
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1777 KEQDTS-----------AHLERMKKNMEQTVKDLQLRLDEAEQLALKGG----KKQIQKLEARVRELEGEVESEQKRNAE 1841
Cdd:TIGR01612 1490 EHIDKSkgckdeadknaKAIEKNKELFEQYKKDVTELLNKYSALAIKNKfaktKKDSEIIIKEIKDAHKKFILEAEKSEQ 1569
|
1130 1140 1150
....*....|....*....|....*....|....*....
gi 153791586 1842 AVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAK 1880
Cdd:TIGR01612 1570 KIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENK 1608
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1204-1703 |
2.75e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1204 DSVAELGEQIDNLQRVKQKLEKEKSEMKM--EIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSkeEEQQRLINDLTA 1281
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQRRL--ELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1282 QRGRLQTESGEFSRQLDEKEALVSQLSRGKQAF-TQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESK 1360
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1361 AELQRALSKANTEVAQWRTKYE---TDAIQRTEELEEAKKKLAQRLQAAE-------EHVEAV-NAKCASLEKTKQRL-- 1427
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEealAEAEAALRDLRRELRELEAEIASLErrksnipARLLALrDALAEALGLDEAELpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1428 --------------QNEVE--------DLMLDVERTNAACAALDK---KQR-NFDKIlaewkqkcEETHAELEASQKEAR 1481
Cdd:COG4913 463 vgelievrpeeerwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1482 SLGTELFKIKNAYEESLDQL-------------ETLKRENK--------------------------------------N 1510
Cdd:COG4913 535 SLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRaitragqvkgngtrhekddrrrirsryvlgfdnraklaA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1511 LQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEegkilriqlelnqvksEVDRKIAEKDEEID 1590
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA----------------SAEREIAELEAELE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1591 QLKRNHIRiVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQ 1670
Cdd:COG4913 679 RLDASSDD-LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
570 580 590
....*....|....*....|....*....|...
gi 153791586 1671 EDLKEQLAMVERRanlLQAEIEELRATLEQTER 1703
Cdd:COG4913 758 ALGDAVERELREN---LEERIDALRARLNRAEE 787
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1186-1739 |
3.05e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 68.59 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1186 EATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEiddLASNVETVSKAKGNLEKMCRTLEDQLSEL 1265
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFK---LKEDHEKIQHLEEEYKKEINDKEKQVSLL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1266 KSKEEEQQRLINDLTAqrgrLQTESGEFSRQLDEKEALVS----QLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQ- 1340
Cdd:pfam05483 246 LIQITEKENKMKDLTF----LLEESRDKANQLEEKTKLQDenlkELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQi 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1341 SSRHDCDLLRE---QYEEEQESKAELQRALSKANTEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQAAEEHVEavnakc 1417
Cdd:pfam05483 322 ATKTICQLTEEkeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QRLEKNEDQLKIITMELQKKSSELE------ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1418 aslEKTKQRLQNEVEdlMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEES 1497
Cdd:pfam05483 395 ---EMTKFKNNKEVE--LEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1498 LDQLETLKR---------------------ENKNLQQEISDLT-------EQIAEGGKRIHELEKIKKQVEQEKCELQAA 1549
Cdd:pfam05483 470 LKEVEDLKTelekeklknieltahcdklllENKELTQEASDMTlelkkhqEDIINCKKQEERMLKQIENLEEKEMNLRDE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1550 LEEAEASL--EHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEG- 1626
Cdd:pfam05483 550 LESVREEFiqKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENk 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1627 -------DLNEMEIQLNHANRMAAEALRNYR-----------NTQGILKDTQIHLDDA--------LRSQEDLKEQLAMV 1680
Cdd:pfam05483 630 qlnayeiKVNKLELELASAKQKFEEIIDNYQkeiedkkiseeKLLEEVEKAKAIADEAvklqkeidKRCQHKIAEMVALM 709
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791586 1681 ERRANLLQAEIEELRATLEQTERSRKiaEQELLDASERVQLLHTQNtSLINTKKKLETD 1739
Cdd:pfam05483 710 EKHKHQYDKIIEERDSELGLYKNKEQ--EQSSAKAALEIELSNIKA-ELLSLKKQLEIE 765
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
858-1524 |
5.12e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 67.82 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 858 MKEEFQKIKDELAKSEAKRKELEEKMVTLlkeKNDLQLQVQAEAEGLADAEercdqliKTKIQLEAKIKEVTERAED-EE 936
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDL---NNNIEKMILAFEELRVQAE-------NARLEMHFKLKEDHEKIQHlEE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 937 EINAELTAKKRK---LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTL 1013
Cdd:pfam05483 230 EYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSM 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1014 DDLQAEEDKVNTLTKAKIKL----EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKK 1089
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1090 EFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEM 1169
Cdd:pfam05483 390 SSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1170 NKkreaEFQKMRRDLEEATLQHeataatlrkkhadsvAELGEQIDNLQRVKQKLEKEKSEMKMEiddLASNVETVSKAKG 1249
Cdd:pfam05483 470 LK----EVEDLKTELEKEKLKN---------------IELTAHCDKLLLENKELTQEASDMTLE---LKKHQEDIINCKK 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1250 NLEKMcrtledqLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEalvsqlsrgkqaftqqieELKRQLEEEI 1329
Cdd:pfam05483 528 QEERM-------LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE------------------ENARSIEYEV 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1330 KAKNALAHALQSSrhdCDLLREQYEEEQESKAELQ---RALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAA 1406
Cdd:pfam05483 583 LKKEKQMKILENK---CNNLKKQIENKNKNIEELHqenKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1407 EEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAAC--------AALDKKQRNFDKILAEWKQKCEETHAELEASQK 1478
Cdd:pfam05483 660 QKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCqhkiaemvALMEKHKHQYDKIIEERDSELGLYKNKEQEQSS 739
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 153791586 1479 EARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAE 1524
Cdd:pfam05483 740 AKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
853-1261 |
5.59e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 853 KEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEA--EGLADAEERCDQLIKTKIQLEAKIKEVTE 930
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 931 RAEDEEEINAELTAKKRKLEDEC-----------SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 999
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1000 KEKKALQE-----------AHQQTLDDLQAEEDKV---------------NTLTKAKIKLEQQVDDLEGSLEQEKKLRMD 1053
Cdd:COG4717 241 LEERLKEArlllliaaallALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1054 LERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEfeisnlqskIEDEQALGIQLQKKIKELqarIEELEEEIEAERA 1133
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAE---------ELEEELQLEELEQEIAAL---LAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1134 SRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKR--EAEFQKMRRDLEEATLQHEAtaatLRKKHADSVAELG- 1210
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEE----LREELAELEAELEq 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 153791586 1211 -EQIDNLQRVKQKLEKEKSEMKMEIDDLASNvetvSKAKGNLEKMCRTLEDQ 1261
Cdd:COG4717 465 lEEDGELAELLQELEELKAELRELAEEWAAL----KLALELLEEAREEYREE 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1576-1923 |
7.03e-11 |
|
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: 67.79 E-value: 7.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1576 SEVDRKIAEKDEEIDQLKRNHIRIvesmqSTLDAEIRSRNDaiRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGI 1655
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERL-----DLIIDEKRQQLE--RLRREREKAERYQALLKEKREYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1656 LKDTQIHLDDALRSQEDLKEQL----------------------AMVERRANLLQAEIEELRATLEQTERSRKIAEQELL 1713
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEIselekrleeieqlleelnkkikDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1714 DASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSA----HLERMK 1789
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyreKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1790 KNMEQTVKDLQLRLDEAEQLALKGG--KKQIQKLEARVRELEGEVESEQKRnaeavkgLRKHERRVKELTYQTEEDRKNI 1867
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELAdlNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQEL 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791586 1868 LRLQDLVDKLQAKVksykrqaeeaeeqsntnlakfRKLQHELEEAEERADIAESQV 1923
Cdd:TIGR02169 472 YDLKEEYDRVEKEL---------------------SKLQRELAEAEAQARASEERV 506
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1200-1777 |
7.79e-11 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 67.62 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1200 KKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDdlasnvetvskakgNLEKMCRTLEDQLSELKSKEEEQQRLINDL 1279
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYN--------------NAMDDYNNLKSALNELSSLEDMKNRYESEI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1280 TAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEEL---------KRQLEEEIKAKNALAHALQSSRHDCDLLR 1350
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYfkykndienKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1351 EQYEEEQESKAELQRALSKANTevaqwrtkYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNE 1430
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEG--------YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1431 VEDLMLDVERTNAACAALDKKQRNfdkiLAEWKQKCEETHAELEASQKE---ARSLGTE-LFKIKNAYEESLDQLETLKR 1506
Cdd:PRK01156 411 LNEINVKLQDISSKVSSLNQRIRA----LRENLDELSRNMEMLNGQSVCpvcGTTLGEEkSNHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1507 EnknLQQEISDLTEQIAEGGKRIHELEKikKQVEQEKCELQAaLEEAEASLEHEEGKILRIQlELNQVKSEVDRKIAEKD 1586
Cdd:PRK01156 487 E---IEIEVKDIDEKIVDLKKRKEYLES--EEINKSINEYNK-IESARADLEDIKIKINELK-DKHDKYEEIKNRYKSLK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1587 EEIDQLKRNHIRIVESMQSTLDAE-IRSRNDAIRLK-KKMEGDLNEMEIQLNHAN-------RMAAEALRNYRNTQGILK 1657
Cdd:PRK01156 560 LEDLDSKRTSWLNALAVISLIDIEtNRSRSNEIKKQlNDLESRLQEIEIGFPDDKsyidksiREIENEANNLNNKYNEIQ 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1658 DTQIHLDDALRSQEDLKEQLAMVERRanllQAEIEELRATLEQTERSRKIAEQELLDAServqllhTQNTSLINTKKKLE 1737
Cdd:PRK01156 640 ENKILIEKLRGKIDNYKKQIAEIDSI----IPDLKEITSRINDIEDNLKKSRKALDDAK-------ANRARLESTIEILR 708
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 153791586 1738 TDISQMQGEMEDIlQEARNAEEKAKKAITDAAMMAEELKK 1777
Cdd:PRK01156 709 TRINELSDRINDI-NETLESMKKIKKAIGDLKRLREAFDK 747
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
849-1278 |
8.28e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 8.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 849 AETEKEMATMKEEFQKIK--------------DELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQL 914
Cdd:PRK02224 268 AETEREREELAEEVRDLRerleeleeerddllAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 915 IKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDET 994
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 995 IAKLT----------KEKKALQEA--------------HQQTLDDlqaEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKL 1050
Cdd:PRK02224 428 EAELEatlrtarervEEAEALLEAgkcpecgqpvegspHVETIEE---DRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1051 RmDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEA 1130
Cdd:PRK02224 505 V-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1131 ERASRAKAEKQRSDLSrELEEISERLEEAGGATSAQIEMNKKRE---AEFQKMRRDLE--------EATLQHEATAATLR 1199
Cdd:PRK02224 584 LKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDERRerlAEKRERKRELEaefdeariEEAREDKERAEEYL 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1200 KKHADSVAELGEQIDNLQR----VKQKLEkEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQ-QR 1274
Cdd:PRK02224 663 EQVEEKLDELREERDDLQAeigaVENELE-ELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETlER 741
|
....
gi 153791586 1275 LIND 1278
Cdd:PRK02224 742 MLNE 745
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
897-1608 |
1.18e-10 |
|
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: 67.17 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 897 VQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRkledecSELKKDIDDLELTLAKVEKEKHA 976
Cdd:pfam12128 239 IRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 977 TENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAE-----------EDKVNTLT------KAKIKlEQQVDD 1039
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSElenleerlkalTGKHQDVTakynrrRSKIK-EQNNRD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1040 LEGSLEQEKKLRMDLERAKRKLEGDLKlAQESIMDIENEKQQLDEKLKKKEFE--ISNLQSKIEDEQA---LGIQLQKKI 1114
Cdd:pfam12128 392 IAGIKDKLAKIREARDRQLAVAEDDLQ-ALESELREQLEAGKLEFNEEEYRLKsrLGELKLRLNQATAtpeLLLQLENFD 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1115 KEL---QARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRR----DLEEA 1187
Cdd:pfam12128 471 ERIeraREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRkeapDWEQS 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1188 TLQHEATAATLRKK-HADSVAELGEQIDNLQRVKQKLEK-EKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSEL 1265
Cdd:pfam12128 551 IGKVISPELLHRTDlDPEVWDGSVGGELNLYGVKLDLKRiDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1266 KSKEEEQQRlinDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAknalahalqssrhd 1345
Cdd:pfam12128 631 NGELEKASR---EETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ-------------- 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1346 cdLLREQyeeeQESKAELQRALSKANTEVAQWRtkyetdaiqrtEELEEAKKKLAQRLQAAEEHVEaVNAKcASLEKTKQ 1425
Cdd:pfam12128 694 --LDKKH----QAWLEEQKEQKREARTEKQAYW-----------QVVEGALDAQLALLKAAIAARR-SGAK-AELKALET 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1426 RLQNEVEDLMLDVERtnaacaaldkkqrnfdkiLAEWKQKCEETHAELEASQKEaRSLGTELFKIKNayEESLDQLETLK 1505
Cdd:pfam12128 755 WYKRDLASLGVDPDV------------------IAKLKREIRTLERKIERIAVR-RQEVLRYFDWYQ--ETWLQRRPRLA 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1506 RENKNLQQEISDLTEQIAeggKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRI-QLELNQVKSEVDRKIAE 1584
Cdd:pfam12128 814 TQLSNIERAISELQQQLA---RLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLaTLKEDANSEQAQGSIGE 890
|
730 740
....*....|....*....|....
gi 153791586 1585 KDEEIDQLKRNHIRIVESMQSTLD 1608
Cdd:pfam12128 891 RLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1203-1419 |
2.08e-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: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1203 ADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELkskEEEQQRLINDLTAQ 1282
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1283 RGRLQTESGEFSRQL---------DEKEALVS-----QLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDL 1348
Cdd:COG4942 96 RAELEAQKEELAELLralyrlgrqPPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1349 LREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCAS 1419
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1495-1936 |
2.35e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1495 EESLDQLETL--KRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEheegkilriqleln 1572
Cdd:PRK02224 186 RGSLDQLKAQieEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-------------- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1573 qvksevdrKIAEKDEEIDQLkRNHIRIVESMQSTLDAEIRSRndairlkkkmegdlnemeiqlnhanRMAAEALRNYRNt 1652
Cdd:PRK02224 252 --------ELETLEAEIEDL-RETIAETEREREELAEEVRDL-------------------------RERLEELEEERD- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1653 qGILKDTQihLDDAlrSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINT 1732
Cdd:PRK02224 297 -DLLAEAG--LDDA--DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1733 KKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLaLK 1812
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-LE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1813 GGK---------------------KQIQKLEARVRELEGEVESEQKRnAEAVKGLRKHERRVKELtyqtEEDRKNilrLQ 1871
Cdd:PRK02224 451 AGKcpecgqpvegsphvetieedrERVEELEAELEDLEEEVEEVEER-LERAEDLVEAEDRIERL----EERRED---LE 522
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791586 1872 DLVDKLQAKVKSYKRQAEEAEEQSNtnlakfrKLQHELEEAEERADIAESQVNKLRVKSREVHTK 1936
Cdd:PRK02224 523 ELIAERRETIEEKRERAEELRERAA-------ELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1217-1902 |
2.38e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.81 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1217 QRVKQKLEKEKSEMK---MEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEF 1293
Cdd:TIGR04523 36 KQLEKKLKTIKNELKnkeKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1294 SRQLDEKEALVSQLSRGKQaftqQIEELKRQLEEEIKAKNALahaLQSSRHDCDLLREQYEEEQESKAELQRALSKANTE 1373
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKK----ENKKNIDKFLTEIKKKEKE---LEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1374 VAQWRTKYetdaiQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQR 1453
Cdd:TIGR04523 189 IDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1454 NFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQleTLKRENKNLQQEISDLTEQIAEGGKRIHELE 1533
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQNQISQNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1534 KIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLE----------LNQVKSEVDRKIaEKDEEIDQLKRNHIRIVESM 1603
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEnqsykqeiknLESQINDLESKI-QNQEKLNQQKDEQIKKLQQE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1604 QSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNhanrmaaealrnyrntqgilkdtqIHLDDALRSQEDLKEQLAMVERr 1683
Cdd:TIGR04523 421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKE------------------------LIIKNLDNTRESLETQLKVLSR- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1684 anllqaEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKK 1763
Cdd:TIGR04523 476 ------SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1764 aitdaamMAEELKKEQdtsahLERMKKNMEQTVKDLqlrldeaeqlalkggKKQIQKLEARVRELEGEVESEQKRNAEAV 1843
Cdd:TIGR04523 550 -------DDFELKKEN-----LEKEIDEKNKEIEEL---------------KQTQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791586 1844 KGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKF 1902
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
920-1120 |
3.76e-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: 64.01 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 920 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 999
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1000 KEKK----ALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDI 1075
Cdd:COG4942 104 EELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 153791586 1076 ENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQAR 1120
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1473-1920 |
4.27e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1473 LEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEe 1552
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1553 aeasleheegkilriQLELNQVKSEVDRKIAEKDEEIDQLKRnhirivesmqstldaEIRSRNDAIRLKKKMEGDLNEME 1632
Cdd:COG4717 127 ---------------LLPLYQELEALEAELAELPERLEELEE---------------RLEELRELEEELEELEAELAELQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1633 IQLNHANRMAAEALRNYrntqgiLKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQEL 1712
Cdd:COG4717 177 EELEELLEQLSLATEEE------LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1713 LDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELK--KEQDTSAHLERMKK 1790
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEelEEEELEELLAALGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1791 NMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGE---------VESEQK--RNAEAVKGLRKHERRVKELTYQ 1859
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaallaeagVEDEEElrAALEQAEEYQELKEELEELEEQ 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791586 1860 TEEDRKNILRLQDLVDK--LQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAE 1920
Cdd:COG4717 411 LEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1232-1705 |
4.46e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1232 MEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGK 1311
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1312 QAFT--QQIEELKRQLEEEIKAKNALAHALQSSRHdcdlLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRT 1389
Cdd:COG4717 126 QLLPlyQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1390 EELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQ--NEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKC- 1466
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1467 ---------EETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKK 1537
Cdd:COG4717 282 vlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1538 QVEQEKCELQAALEEAEASLEHEEGkiLRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQ-STLDAEIRSRND 1616
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVEDEEE--LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeEELEEELEELEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1617 AIRLKKKMEGDLNEMEIQLNHANRMAAEALRnyrntqgilkdtqihLDDALRSQEDLKEQLAMVERRANLLQAEIEELRA 1696
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEEDGE---------------LAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
....*....
gi 153791586 1697 TLEQTERSR 1705
Cdd:COG4717 505 AREEYREER 513
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
912-1547 |
4.77e-10 |
|
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: 65.14 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 912 DQLIKTKIQLEAKIKEVTERAEDE-EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEkhaTENKVKNLTEEMAG 990
Cdd:pfam15921 245 DQLEALKSESQNKIELLLQQHQDRiEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 991 LDETIAKLTKEkkaLQEAHQQTlddlqaeEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQE 1070
Cdd:pfam15921 322 LESTVSQLRSE---LREAKRMY-------EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1071 SIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELE 1150
Cdd:pfam15921 392 ELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1151 EISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHAdsvaelgeqidnlqRVKQKLEkEKSEM 1230
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRS--------------RVDLKLQ-ELQHL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1231 KMEIDDLaSNVETVSKAKgnleKMCRTLEDQLSE-LKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSR 1309
Cdd:pfam15921 537 KNEGDHL-RNVQTECEAL----KLQMAEKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKI 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1310 GKQAFTQQIEELKRQLE----EEIKAKNALAHALQSSRhDCDLLREQ-YEEEQESKAELQRALSKANTEVAQWRTKyetd 1384
Cdd:pfam15921 612 LKDKKDAKIRELEARVSdlelEKVKLVNAGSERLRAVK-DIKQERDQlLNEVKTSRNELNSLSEDYEVLKRNFRNK---- 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1385 aiqrTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAewkq 1464
Cdd:pfam15921 687 ----SEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMT---- 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1465 kceETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKC 1544
Cdd:pfam15921 759 ---NANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESV 835
|
...
gi 153791586 1545 ELQ 1547
Cdd:pfam15921 836 RLK 838
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1178-1928 |
5.34e-10 |
|
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: 64.86 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1178 QKMRRDLEEATLQHEATAATLRKKHadSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRT 1257
Cdd:pfam12128 217 RLNRQQVEHWIRDIQAIAGIMKIRP--EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRT 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1258 LEDQLSELKSkeeeqqrlindltAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAftqQIEELKRQLEEEIKAKNALah 1337
Cdd:pfam12128 295 LDDQWKEKRD-------------ELNGELSAADAAVAKDRSELEALEDQHGAFLDA---DIETAAADQEQLPSWQSEL-- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1338 ALQSSRHDCdLLREQYEEEQESKAELQRALSKANTEVAqwRTKYETDAIQRTEELEEAKKKLAqrLQAAEEHV-EAVNAK 1416
Cdd:pfam12128 357 ENLEERLKA-LTGKHQDVTAKYNRRRSKIKEQNNRDIA--GIKDKLAKIREARDRQLAVAEDD--LQALESELrEQLEAG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1417 CASLEKTKQRLQNEVEDLMLdveRTNAACAALDKK--QRNFDkilaewkQKCEETHAELEASQKEARSLGTELFKIKNAY 1494
Cdd:pfam12128 432 KLEFNEEEYRLKSRLGELKL---RLNQATATPELLlqLENFD-------ERIERAREEQEAANAEVERLQSELRQARKRR 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1495 EESLDQLETLKRENKNLQQEISDLTEQ-IAEGGKRIHEL--------EKIKKQVEQE---KCELQAALEEAEASLEHEEG 1562
Cdd:pfam12128 502 DQASEALRQASRRLEERQSALDELELQlFPQAGTLLHFLrkeapdweQSIGKVISPEllhRTDLDPEVWDGSVGGELNLY 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1563 KIlRIQLELNQVKSEVDRKIAEKdEEIDQLKrnhirivesmqSTLDAEiRSRNDAIrlkkkmEGDLNEMEIQLNHANRMA 1642
Cdd:pfam12128 582 GV-KLDLKRIDVPEWAASEEELR-ERLDKAE-----------EALQSA-REKQAAA------EEQLVQANGELEKASREE 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1643 AEALRNYRNTqgilKDTQIHLDDALRSQEDLKEQlamverranllqaeieelratleQTERSRKIAEQELldaservqll 1722
Cdd:pfam12128 642 TFARTALKNA----RLDLRRLFDEKQSEKDKKNK-----------------------ALAERKDSANERL---------- 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1723 htqnTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITD------AAMMAEELKKEQDTSAHLERMKKNMEQTV 1796
Cdd:pfam12128 685 ----NSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGaldaqlALLKAAIAARRSGAKAELKALETWYKRDL 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1797 KDLQLRLDeaeqlalkggkkQIQKLEARVRELEGEVESEQKRNAEAVKGLR----KHERRVKELTYQTEEDRKNILRLQD 1872
Cdd:pfam12128 761 ASLGVDPD------------VIAKLKREIRTLERKIERIAVRRQEVLRYFDwyqeTWLQRRPRLATQLSNIERAISELQQ 828
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791586 1873 LVDKLQAKVKSYKRQAEeaeeqsnTNLAKFRKLQHELEEAEERADIAESQVNKLRV 1928
Cdd:pfam12128 829 QLARLIADTKLRRAKLE-------MERKASEKQQVRLSENLRGLRCEMSKLATLKE 877
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1668-1937 |
8.28e-10 |
|
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: 64.32 E-value: 8.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1668 RSQEDLKEQLAMVERRANLLQAEIEELRATLE--QTERSRKIAEQELLDASERVQLlhtqnTSLINTKKKLETDISQMQG 1745
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKREYEG-----YELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1746 EMEDILQEARNAEEKAkkaitdaammaEELKKEqdtSAHLERMKKNMEQTVKDLqlrlDEAEQLALKGG----KKQIQKL 1821
Cdd:TIGR02169 245 QLASLEEELEKLTEEI-----------SELEKR---LEEIEQLLEELNKKIKDL----GEEEQLRVKEKigelEAEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1822 EARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAK 1901
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
250 260 270
....*....|....*....|....*....|....*.
gi 153791586 1902 FRKLQHELEEAEERADIAESQVNKLRVKSREVHTKV 1937
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
896-1215 |
1.38e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 896 QVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAE--------DEEEINAeltakkRKLEDECSELKKDIDDLELT- 966
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREalqrlaeySWDEIDV------ASAEREIAELEAELERLDASs 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 967 --LAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKikLEQQVDDLEGSl 1044
Cdd:COG4913 685 ddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALGD- 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1045 EQEKKLRMDLERAKRKLEGDLKLAQESIMDIenekqqLDEKLKKKEFEISNLQSKIED------------EQALgIQLQK 1112
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERA------MRAFNREWPAETADLDADLESlpeylalldrleEDGL-PEYEE 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1113 KIKELQARIEELEEEIEAerasrAKAEKQRSDLSRELEEISERLEEA--GGATSAQIEMNKKREAEFQKMRRDLEEATLQ 1190
Cdd:COG4913 835 RFKELLNENSIEFVADLL-----SKLRRAIREIKERIDPLNDSLKRIpfGPGRYLRLEARPRPDPEVREFRQELRAVTSG 909
|
330 340
....*....|....*....|....*
gi 153791586 1191 HEATAATLRKKHADSVAELGEQIDN 1215
Cdd:COG4913 910 ASLFDEELSEARFAALKRLIERLRS 934
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
946-1570 |
1.50e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 946 KRKLEDECSELKKDIDDLELTLAKVEKekhaTENKVKNLtEEMAGLDETIAKLtKEKKALQEAHQQTLDDLQAEEdKVNT 1025
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALED----AREQIELL-EPIRELAERYAAA-RERLAELEYLRAALRLWFAQR-RLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1026 LTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDL-KLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIedeQ 1104
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALL---A 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1105 ALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKR----EAEFQKM 1180
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL----EAEIASLERRksniPARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1181 RRDLEEATLQHEA---------------------------TAAT---LRKKHADSVAELGEQID-----NLQRVKQKLEK 1225
Cdd:COG4913 446 RDALAEALGLDEAelpfvgelievrpeeerwrgaiervlgGFALtllVPPEHYAAALRWVNRLHlrgrlVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1226 EKSeMKMEIDDLASNVET-VSKAKGNLEKM---------CRTLED------------QLSELKSKEEEQ----------- 1272
Cdd:COG4913 526 PER-PRLDPDSLAGKLDFkPHPFRAWLEAElgrrfdyvcVDSPEElrrhpraitragQVKGNGTRHEKDdrrrirsryvl 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1273 ----QRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFtQQIEELK------RQLEEEIKAKNALAHALQSS 1342
Cdd:COG4913 605 gfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSwdeidvASAEREIAELEAELERLDAS 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1343 RHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQAAEEHV------------ 1410
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE----QAEEELDELQDRLEAAEDLARLELralleerfaaal 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1411 --EAVNAKCASLEKTKQRLQNEVEDLMLDVERTnaacaaldkkqrnFDKILAEWKqkceETHAELEASQKEARSLGTELF 1488
Cdd:COG4913 760 gdAVERELRENLEERIDALRARLNRAEEELERA-------------MRAFNREWP----AETADLDADLESLPEYLALLD 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1489 KIKN----AYEESLdqletLKRENKNLQQEISDLTEQIAEggkrihELEKIKKQVEqekcELQAALEEaeasLEHEEGKI 1564
Cdd:COG4913 823 RLEEdglpEYEERF-----KELLNENSIEFVADLLSKLRR------AIREIKERID----PLNDSLKR----IPFGPGRY 883
|
....*.
gi 153791586 1565 LRIQLE 1570
Cdd:COG4913 884 LRLEAR 889
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
858-1308 |
1.62e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 62.92 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 858 MKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLiktkiqlEAKIKEVTERAEDEEE 937
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL-------QTEVDALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 938 INAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQ------ 1011
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalt 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1012 TLDDLQAEEDKVNTLTKAKIKLEQQVDDLEgsLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEF 1091
Cdd:pfam10174 440 TLEEALSEKERIIERLKEQREREDRERLEE--LESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDS 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1092 EISNLQskiedeqalgIQLQKKIKELQARIEELEEEIEAERASRAKAEkqRSDLSRELEEISERLEEAGGATSAQIE--M 1169
Cdd:pfam10174 518 KLKSLE----------IAVEQKKEECSKLENQLKKAHNAEEAVRTNPE--INDRIRLLEQEVARYKEESGKAQAEVErlL 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1170 NKKREAEFQKMRRDLEEATLqhEATAATLRKKHADSVAELgeqidnlqRVKQKLEKEKSEMKMEIDDLASNVETVSKAKG 1249
Cdd:pfam10174 586 GILREVENEKNDKDKKIAEL--ESLTLRQMKEQNKKVANI--------KHGQQEMKKKGAQLLEEARRREDNLADNSQQL 655
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791586 1250 NLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDE-----KEALVSQLS 1308
Cdd:pfam10174 656 QLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEilemkQEALLAAIS 719
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1054-1594 |
1.92e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 63.00 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1054 LERAKRKLEGDLKLAQESIMDIENekqqLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERA 1133
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1134 SR-----------------AKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1196
Cdd:PRK01156 240 ALnelssledmknryeseiKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1197 TLRKKHADSVAELGEQIDNLQRVKQKleKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLI 1276
Cdd:PRK01156 320 EINKYHAIIKKLSVLQKDYNDYIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1277 NDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEE 1356
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1357 ----QESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQ-------------RLQAAEEHVEAVNAKCAS 1419
Cdd:PRK01156 478 ksrlEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESaradledikikinELKDKHDKYEEIKNRYKS 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1420 LEKTKQRLQNEvEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLD 1499
Cdd:PRK01156 558 LKLEDLDSKRT-SWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1500 QLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVkSEVD 1579
Cdd:PRK01156 637 EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRI-NELS 715
|
570
....*....|....*
gi 153791586 1580 RKIAEKDEEIDQLKR 1594
Cdd:PRK01156 716 DRINDINETLESMKK 730
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
837-1510 |
2.26e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 62.76 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 837 KLFFKIKPLLKSAETEKEMATMKEEFQKIKDELAKSE--AKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAE------ 908
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttr 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 909 ERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKV 981
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 982 KNLTEEMAGLDETIAKLTKekkalQEAHQQTLDDLQAEEDKVNT----LTKAKIKLEQQVDDLEGSLEQEKKLRMDLERA 1057
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCG-----SQDEESDLERLKEEIEKSSKqramLAGATAVYSQFITQLTDENQSCCPVCQRVFQT 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1058 KRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELqarieeleeeieaerasRAK 1137
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPEL-----------------RNK 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1138 AEKQRSDLSRELEEISERlEEAGGATSAQIEMNKKREAEFQKMRRdLEEATLQHEataatlrKKHADSVAELgeQIDNLQ 1217
Cdd:TIGR00606 753 LQKVNRDIQRLKNDIEEQ-ETLLGTIMPEEESAKVCLTDVTIMER-FQMELKDVE-------RKIAQQAAKL--QGSDLD 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1218 RVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKS---------------------KEEEQQRLI 1276
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklqigtnlqrrqqfeeqlveLSTEVQSLI 901
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1277 NDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLRE-QYEE 1355
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKEtELNT 981
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1356 EQESKAELQRALSKANTEVAQWRTKYETDAIQ------------RTEELEEAKKKLAQRLQAAEEhveavnAKCASLEKT 1423
Cdd:TIGR00606 982 VNAQLEECEKHQEKINEDMRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELKQHLKEMGQ------MQVLQMKQE 1055
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1424 KQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWK-QKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLE 1502
Cdd:TIGR00606 1056 HQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQfRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFH 1135
|
....*...
gi 153791586 1503 TLKRENKN 1510
Cdd:TIGR00606 1136 SMKMEEIN 1143
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1666-1897 |
4.12e-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: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1666 ALRSQEDLKEQLamvERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQG 1745
Cdd:COG4942 14 AAAAQADAAAEA---EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1746 EMEDILQEARNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNMEQTVKDLQLRLDE--AEQLALKGGKKQIQ 1819
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791586 1820 KLEARVRELEGEVESEQKRNAEAVKglrKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNT 1897
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1464-1932 |
4.18e-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: 61.73 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1464 QKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEIS----DLTEQIAEGGKRIHELEKIKKQV 1539
Cdd:pfam01576 15 QKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAarkqELEEILHELESRLEEEEERSQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1540 EQEKCELQAALEEAEASLEHEEGKILRIQLElnqvKSEVDRKIAEKDEEIdqlkrnhiRIVESMQSTLDAEirsrndair 1619
Cdd:pfam01576 95 QNEKKKMQQHIQDLEEQLDEEEAARQKLQLE----KVTTEAKIKKLEEDI--------LLLEDQNSKLSKE--------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1620 lKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLE 1699
Cdd:pfam01576 154 -RKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1700 QTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQeARNAEEKAKKaitdaammaeelkkeq 1779
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERA-ARNKAEKQRR---------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1780 DTSAHLERMKKNMEQTVKDlqlrldEAEQLALKGgkkqiqKLEARVRELEGEVESEQKRNAEAVKGLR-KHERRVKELTY 1858
Cdd:pfam01576 296 DLGEELEALKTELEDTLDT------TAAQQELRS------KREQEVTELKKALEEETRSHEAQLQEMRqKHTQALEELTE 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791586 1859 QTEEDRKNilrlqdlvdklqakvKSYKRQAEEAEEQSNTNL-AKFRKLQHELEEAEERADIAESQVNKLRVKSRE 1932
Cdd:pfam01576 364 QLEQAKRN---------------KANLEKAKQALESENAELqAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE 423
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1068-1283 |
4.34e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1068 AQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR 1147
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1148 ELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKhadsVAELGEQIDNLQRVKQKLEKEK 1227
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791586 1228 SEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQR 1283
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1137-1757 |
4.42e-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: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1137 KAEKQRSDLsRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAtlrKKHADSVAELGEQIDNL 1216
Cdd:COG4913 246 DAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL---ARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1217 QRVKQKLE--------KEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEdqlSELKSKEEEQQRLINDLTAQRGRLQT 1288
Cdd:COG4913 322 REELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1289 ESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQL----EEEIKAKNALAHALQSSRHD----CDLLrEQYEEEQESK 1360
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEALGLDEAElpfvGELI-EVRPEEERWR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1361 AELQRALskantevAQWRT------KYETDAIQRTEELeeakkKLAQRLQAaeEHVEAVNAKCASLEKTKQRLQNEvedl 1434
Cdd:COG4913 478 GAIERVL-------GGFALtllvppEHYAAALRWVNRL-----HLRGRLVY--ERVRTGLPDPERPRLDPDSLAGK---- 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1435 mLDVERTNAACAALDKKQRNFDKIlaewkqkCEETHAELeasQKEARSLgTELFKIKNAYE------------------E 1496
Cdd:COG4913 540 -LDFKPHPFRAWLEAELGRRFDYV-------CVDSPEEL---RRHPRAI-TRAGQVKGNGTrhekddrrrirsryvlgfD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1497 SLDQLETLKRENKNLQQEISDLTEQIAEggkriheLEKIKKQVEQEKCELQAALEEAEASLEHEEgkilriqlelnqvks 1576
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEA-------LEAELDALQERREALQRLAEYSWDEIDVAS--------------- 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1577 eVDRKIAEKDEEIDQLKRNHirivesmqstldaeirsrndairlkkkmeGDLNEMEIQLnhanrmaaealrnyrntqgil 1656
Cdd:COG4913 666 -AEREIAELEAELERLDASS-----------------------------DDLAALEEQL--------------------- 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1657 KDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDasERVQLLHTQNtSLINTKKKL 1736
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE--ERFAAALGDA-VERELRENL 771
|
650 660
....*....|....*....|.
gi 153791586 1737 ETDISQMQGEMEDILQEARNA 1757
Cdd:COG4913 772 EERIDALRARLNRAEEELERA 792
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1492-1935 |
5.83e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 61.38 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1492 NAYEESLDQL-ETL--KRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALE-EAEASLEHEEGKILRI 1567
Cdd:pfam10174 154 GARDESIKKLlEMLqsKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHrRNQLQPDPAKTKALQT 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1568 QLELNQVK-SEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKME---GDLNEMEIQLnHANRMAA 1643
Cdd:pfam10174 234 VIEMKDTKiSSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDqlkQELSKKESEL-LALQTKL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1644 EALRNYRNtqgilkDTQIHLddalrsqEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLH 1723
Cdd:pfam10174 313 ETLTNQNS------DCKQHI-------EVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1724 TQNTSLINTKKKLETDISQMQGEMEDILQEARNAE-------EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM-EQT 1795
Cdd:pfam10174 380 GEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDkqlaglkERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQR 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1796 VKDLQLRLDEAEQL--ALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDL 1873
Cdd:pfam10174 460 EREDRERLEELESLkkENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQ 539
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791586 1874 VDKLQakvksykrQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSREVHT 1935
Cdd:pfam10174 540 LKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVEN 593
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1683-1941 |
6.10e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1683 RANLLQAE--IEELRATLEQTERSRKIAEQ--------ELLDASERVQLLHTQNTSLintkKKLETDISQMQGEMEDILQ 1752
Cdd:COG1196 185 EENLERLEdiLGELERQLEPLERQAEKAERyrelkeelKELEAELLLLKLRELEAEL----EELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1753 EARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEV 1832
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--------RLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1833 ESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEA 1912
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
250 260
....*....|....*....|....*....
gi 153791586 1913 EERADIAESQVNKLRVKSREVHTKVISEE 1941
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEE 441
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1512-1764 |
9.67e-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: 59.78 E-value: 9.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1512 QQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNqvksEVDRKIAEKDEEIDQ 1591
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1592 LKRNHIRIVESMQSTLDAEIRSrndairlkkkmeGDLNEMEIQLNHANrmAAEALRNYRNTQGILKDTQIHLddalrsqE 1671
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRL------------GRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQA-------E 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1672 DLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDIL 1751
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250
....*....|...
gi 153791586 1752 QEARNAEEKAKKA 1764
Cdd:COG4942 234 AEAAAAAERTPAA 246
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
980-1941 |
9.84e-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: 60.84 E-value: 9.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 980 KVKNLTEEMAGLDETIAKLTKEKKALQEAHQQtlddLQAEEDKVntltkakIKLEQQVDDLegsleQEKKLRMDLERAK- 1058
Cdd:TIGR01612 535 KAKLYKEIEAGLKESYELAKNWKKLIHEIKKE----LEEENEDS-------IHLEKEIKDL-----FDKYLEIDDEIIYi 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1059 RKLEGDLKlaqESIMDIENEkqqlDEKLKKKefeiSNLQSKIEDEQALgIQLQKKIKELQARIEELEEEIEAERASRAKA 1138
Cdd:TIGR01612 599 NKLKLELK---EKIKNISDK----NEYIKKA----IDLKKIIENNNAY-IDELAKISPYQVPEHLKNKDKIYSTIKSELS 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1139 EKQRSDLSRELEEISERLEEA---GGATSAQIE-MNKKREAEFQKMRrDLEEATLQ-HEATAATLRKKHADSVAEL---- 1209
Cdd:TIGR01612 667 KIYEDDIDALYNELSSIVKENaidNTEDKAKLDdLKSKIDKEYDKIQ-NMETATVElHLSNIENKKNELLDIIVEIkkhi 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1210 -GEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINdltaqrgrlqt 1288
Cdd:TIGR01612 746 hGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYD----------- 814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1289 ESGEFSRQLDEKEALVSQLsrgkqaftqqIEELKRQLEEEIKAKNALAHAlqssRHDCdllREQYEEEQESKAELqraLS 1368
Cdd:TIGR01612 815 KSKEYIKTISIKEDEIFKI----------INEMKFMKDDFLNKVDKFINF----ENNC---KEKIDSEHEQFAEL---TN 874
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1369 KANTEVAQWR-TKYETDAIQRTEELEEAKKKLAQR------LQAAEEHVEAVNAKCASLEK--TKQRLQNEVEDLMLDV- 1438
Cdd:TIGR01612 875 KIKAEISDDKlNDYEKKFNDSKSLINEINKSIEEEyqnintLKKVDEYIKICENTKESIEKfhNKQNILKEILNKNIDTi 954
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1439 ERTNaacaALDKKQRN-FDKILAEWKQKCEETHAELEASQKEARSlgTELFKIKNAYEESL---------DQLETLKREN 1508
Cdd:TIGR01612 955 KESN----LIEKSYKDkFDNTLIDKINELDKAFKDASLNDYEAKN--NELIKYFNDLKANLgknkenmlyHQFDEKEKAT 1028
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1509 KNLQQEISDLTEQIAEGGKRIH--------ELEK-IKKQVEQEKCELqaaLEEAEASLEHEEGkiLRIQLELNQVKSEVD 1579
Cdd:TIGR01612 1029 NDIEQKIEDANKNIPNIEIAIHtsiyniidEIEKeIGKNIELLNKEI---LEEAEINITNFNE--IKEKLKHYNFDDFGK 1103
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1580 RKIAEKDEEIDQLKRNhiriVESMQSTLDAEIrsrNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNyRNTQGILKDT 1659
Cdd:TIGR01612 1104 EENIKYADEINKIKDD----IKNLDQKIDHHI---KALEEIKKKSENYIDEIKAQINDLEDVADKAISN-DDPEEIEKKI 1175
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1660 Q---IHLDDALRSQEDLKEQLAMVerranllqAEIEELRATLEQTersrkiaeqelldasERVQLLHTQNTSLI------ 1730
Cdd:TIGR01612 1176 EnivTKIDKKKNIYDEIKKLLNEI--------AEIEKDKTSLEEV---------------KGINLSYGKNLGKLflekid 1232
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1731 NTKKKLETDISQMQGEMEDI--LQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQlrldeAEQ 1808
Cdd:TIGR01612 1233 EEKKKSEHMIKAMEAYIEDLdeIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIR-----EKS 1307
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1809 LALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKherrvkeltyqtEEDRKNILRLQDlVDKLQAKVKSYKRQA 1888
Cdd:TIGR01612 1308 LKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNE------------IANIYNILKLNK-IKKIIDEVKEYTKEI 1374
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1889 EEAEEQSNTNLAKFRKL------QHELEEAEERAD--IAESQVNKLRVKSREVHTKVISEE 1941
Cdd:TIGR01612 1375 EENNKNIKDELDKSEKLikkikdDINLEECKSKIEstLDDKDIDECIKKIKELKNHILSEE 1435
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1256-1476 |
1.18e-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: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1256 RTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNAL 1335
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1336 AHALQssrhdcDLLREQYEEEQESKAELqrALSKANTEVAQWRTKY----------ETDAIQRT-EELEEAKKKLAQRLQ 1404
Cdd:COG4942 103 KEELA------ELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYlkylaparreQAEELRADlAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791586 1405 AAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEAS 1476
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
986-1859 |
1.21e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 986 EEMAGLDETIAKLTKEK---KALQEAHQQTLDDLQAEEDkvnTLTKAKIKLEQQVDDLEGSL----------EQEKKLRM 1052
Cdd:PRK04863 279 NERRVHLEEALELRRELytsRRQLAAEQYRLVEMARELA---ELNEAESDLEQDYQAASDHLnlvqtalrqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1053 DLERAKRKLEGDL---KLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQarieeleeeie 1129
Cdd:PRK04863 356 DLEELEERLEEQNevvEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE----------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1130 aerasRAKAEKQRSDLsrELEEISERLEEAggATSAQIEMNKKREAEfQKMRrDLEEATLQHEATAATLRKkhadsvaeL 1209
Cdd:PRK04863 425 -----RAKQLCGLPDL--TADNAEDWLEEF--QAKEQEATEELLSLE-QKLS-VAQAAHSQFEQAYQLVRK--------I 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1210 GEQID--NLQRVKQKLEKEKSEMKMEIDDLASnvetvskakgnlekmcrtLEDQLSELKSKEEEQQ---RLINDLTAQRG 1284
Cdd:PRK04863 486 AGEVSrsEAWDVARELLRRLREQRHLAEQLQQ------------------LRMRLSELEQRLRQQQraeRLLAEFCKRLG 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1285 RLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEE---EIKAKNALAHALQSSRHDCDLLREQYEEEQESK- 1360
Cdd:PRK04863 548 KNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQlqaRIQRLAARAPAWLAAQDALARLREQSGEEFEDSq 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1361 ---------AELQRALSKANTEVAQwrtkyetdaiqRTEELEEAKKKLAQ-------RLQAAEEHVEAV----------- 1413
Cdd:PRK04863 628 dvteymqqlLERERELTVERDELAA-----------RKQALDEEIERLSQpggsedpRLNALAERFGGVllseiyddvsl 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1414 -----------NAKCA----SLEKTKQRLQNEvEDLMLDVERTNAACAALDKKQrnFDKILAEWKQKCEETHAELEASQ- 1477
Cdd:PRK04863 697 edapyfsalygPARHAivvpDLSDAAEQLAGL-EDCPEDLYLIEGDPDSFDDSV--FSVEELEKAVVVKIADRQWRYSRf 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1478 KEARSLGtelfkiKNAYEESLDQLetlkrenknlQQEISDLTEQIAEGGKRIHELEKIKKQV----------------EQ 1541
Cdd:PRK04863 774 PEVPLFG------RAAREKRIEQL----------RAEREELAERYATLSFDVQKLQRLHQAFsrfigshlavafeadpEA 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1542 EKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVD--RKIAekdEEIDQLKRNHI--RIVEsmqstLDAEIRSRNDA 1617
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSalNRLL---PRLNLLADETLadRVEE-----IREQLDEAEEA 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1618 IRLKKKMEGDLNEMEIQLN--HANRMAAEALR-NYRNTQGILKDTQIHLDdalrsqeDLKEqlaMVERRA--------NL 1686
Cdd:PRK04863 910 KRFVQQHGNALAQLEPIVSvlQSDPEQFEQLKqDYQQAQQTQRDAKQQAF-------ALTE---VVQRRAhfsyedaaEM 979
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1687 LQAE---IEELRATLEQTERSRKIAEQELLDASERvqllHTQN----TSLINTKKKLETDISQMQGEMEDI-LQEARNAE 1758
Cdd:PRK04863 980 LAKNsdlNEKLRQRLEQAEQERTRAREQLRQAQAQ----LAQYnqvlASLKSSYDAKRQMLQELKQELQDLgVPADSGAE 1055
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1759 EKakkaitdAAMMAEELKKEQDTSahleRMKKN-MEQTVKDLQLRLDEAEqlalkggkKQIQKLEARVRELEGEVESEQK 1837
Cdd:PRK04863 1056 ER-------ARARRDELHARLSAN----RSRRNqLEKQLTFCEAEMDNLT--------KKLRKLERDYHEMREQVVNAKA 1116
|
970 980
....*....|....*....|....*.
gi 153791586 1838 RNAEAVKGLRKH--ERRV--KELTYQ 1859
Cdd:PRK04863 1117 GWCAVLRLVKDNgvERRLhrRELAYL 1142
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1134-1712 |
1.27e-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: 60.14 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1134 SRAKAEKQRSDLSRELEEISerLEEAGGATSAQIEMNKKREAEFQKMRRDLEEatLQHEATAAtlrkkhadsvaeLGEQI 1213
Cdd:pfam05557 12 SQLQNEKKQMELEHKRARIE--LEKKASALKRQLDRESDRNQELQKRIRLLEK--REAEAEEA------------LREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1214 DNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLindltaqrgrlqtesgef 1293
Cdd:pfam05557 76 ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL------------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1294 SRQLDEKEALVSQLSRGKQAFTQQIEELKRQlEEEIKaknALAHALQSSRHDCDLLREQyEEEQESKAELQRALSKANTE 1373
Cdd:pfam05557 138 QERLDLLKAKASEAEQLRQNLEKQQSSLAEA-EQRIK---ELEFEIQSQEQDSEIVKNS-KSELARIPELEKELERLREH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1374 VAQWRTKYETDAIQRtEELEEAKKKLaqrlqaaeEHVEAVNAKCASLEKTKQRLQNEvedlmldvertnaacaaldkkqr 1453
Cdd:pfam05557 213 NKHLNENIENKLLLK-EEVEDLKRKL--------EREEKYREEAATLELEKEKLEQE----------------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1454 nfdkiLAEWKQKCEETHAELEASQKEARslgtelfkiknayeesldQLETLKRENKNLQQEISDLTEQiaeggkrIHELE 1533
Cdd:pfam05557 261 -----LQSWVKLAQDTGLNLRSPEDLSR------------------RIEQLQQREIVLKEENSSLTSS-------ARQLE 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1534 KIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQlelnqvksevdRKIAEKDEEIDQLKrnhiRIVESMQSTLDAEIRS 1613
Cdd:pfam05557 311 KARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-----------RRVLLLTKERDGYR----AILESYDKELTMSNYS 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1614 RNDAIRLK------KKMEGDLNEMEIQLNHANRmaaealrnyrnTQGILKDTQIHLD---DALRSQEDLKEQLAMVERRA 1684
Cdd:pfam05557 376 PQLLERIEeaedmtQKMQAHNEEMEAQLSVAEE-----------ELGGYKQQAQTLErelQALRQQESLADPSYSKEEVD 444
|
570 580
....*....|....*....|....*...
gi 153791586 1685 NLLQaEIEELRATLEQTERSRKIAEQEL 1712
Cdd:pfam05557 445 SLRR-KLETLELERQRLREQKNELEMEL 471
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
850-1409 |
1.52e-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: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 850 ETEKEMATMKEEFQKIKD---ELAKSEAKRK---ELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKI-QLE 922
Cdd:COG4913 222 DTFEAADALVEHFDDLERaheALEDAREQIEllePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELeELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 923 AKIKEVTERAEDEEEINAELTAKKRKLEDECSELK-KDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKE 1001
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1002 KKALQEAHQQTLDDLQAEEDKVNT----LTKAKIKLEQQVDDLEG---SLEQeKKLRMD--LERAKRKLEGDLKLAQESI 1072
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAeiaSLER-RKSNIParLLALRDALAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1073 ------MDIENEKQQ-----------------LDEKLKKKefeisnLQSKIEDEQ-ALGIQLQKKIKELQARIEELEEEI 1128
Cdd:COG4913 461 pfvgelIEVRPEEERwrgaiervlggfaltllVPPEHYAA------ALRWVNRLHlRGRLVYERVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1129 EAERASRAKAEKQRSDLSRELEEIS-----ERLEEAGGATSA-----QIEMNKKReaeFQK-MRRDLEE----------- 1186
Cdd:COG4913 535 SLAGKLDFKPHPFRAWLEAELGRRFdyvcvDSPEELRRHPRAitragQVKGNGTR---HEKdDRRRIRSryvlgfdnrak 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1187 -ATLQHEATAATLRKKHADS-VAELGEQIDNLQRVKQKLEKeKSEMKMEIDDLASNVETVSKAKGNLEKM------CRTL 1258
Cdd:COG4913 612 lAALEAELAELEEELAEAEErLEALEAELDALQERREALQR-LAEYSWDEIDVASAEREIAELEAELERLdassddLAAL 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1259 EDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAftQQIEELKRQLEEEIKAK--NALA 1336
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAALGDAveRELR 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1337 HALQSSRHDCDLLREQYEEEQESKaeLQRALSKANTEVAQWRTKYET----DAI---QRTEELEEAKKKLAQRLQAAEEH 1409
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERA--MRAFNREWPAETADLDADLESlpeyLALldrLEEDGLPEYEERFKELLNENSIE 846
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1391-1833 |
1.69e-08 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 59.32 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1391 ELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAE--------- 1461
Cdd:pfam05622 4 EAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEEnfrletard 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1462 -WKQKCEETHA----------ELEASQKEARSLGTELFKIKNA-------------YEESLDQLETLKRENKNLQQEISD 1517
Cdd:pfam05622 84 dYRIKCEELEKevlelqhrneELTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1518 LTEQIAEGGKRIHELEKIKKQVEQEKCELQaaleEAEASLEHEEGKILRIQLELNQ-------VKSEVDRKIAEKD---E 1587
Cdd:pfam05622 164 YMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKleekleaLQKEKERLIIERDtlrE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1588 EIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQgiLKDTQIHLDDAL 1667
Cdd:pfam05622 240 TNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRER--LTELQQLLEDAN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1668 RSQEDLKEQLAMVERRANLLQAEIEELRATLeqtersrkiaeqelldaservQLLHTQNTSLINTKKKLETDISQMQgEM 1747
Cdd:pfam05622 318 RRKNELETQNRLANQRILELQQQVEELQKAL---------------------QEQGSKAEDSSLLKQKLEEHLEKLH-EA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1748 EDILQEARNA-EEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQT---VKDLQLRLDEAEQLALKGGKKQI 1818
Cdd:pfam05622 376 QSELQKKKEQiEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKAksvIKTLDPKQNPASPPEIQALKNQL 455
|
490
....*....|....*
gi 153791586 1819 QKLEARVRELEGEVE 1833
Cdd:pfam05622 456 LEKDKKIEHLERDFE 470
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
920-1248 |
1.92e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 59.14 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 920 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 999
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1000 KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEK 1079
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1080 QQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR------------ 1147
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrtqael 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1148 -----ELEEISERLEEA------GGATSAQ--------IEMNKKR----EAEFQKMRRDLEEATLQHEATAATL------ 1198
Cdd:pfam07888 275 hqarlQAAQLTLQLADAslalreGRARWAQeretlqqsAEADKDRieklSAELQRLEERLQEERMEREKLEVELgrekdc 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 153791586 1199 -RKKHADSVAELGEQIDNL---QRVKQKLEKEKSEMKMEIDDLASNVETVSKAK 1248
Cdd:pfam07888 355 nRVQLSESRRELQELKASLrvaQKEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1464-1684 |
4.01e-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: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1464 QKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEK 1543
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1544 CELQAALEEAEASLeHEEGKILRIQLELNQVKSEvdrKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKK 1623
Cdd:COG4942 100 EAQKEELAELLRAL-YRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1624 MEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRA 1684
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
975-1205 |
4.23e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 975 HATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSL----EQEKKL 1050
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1051 RMDLERAKRKLEGDLKLAQESimdieNEKQQLDEKLKKKEFE-----ISNLQSKIEDEQALGIQLQKKIKELQARIEELE 1125
Cdd:COG4942 96 RAELEAQKEELAELLRALYRL-----GRQPPLALLLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1126 EEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADS 1205
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARL----EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
847-1552 |
4.53e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 58.70 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 847 KSAETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGL---------------------- 904
Cdd:pfam12128 302 KRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLeerlkaltgkhqdvtakynrrr 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 905 ADAEERCDQLIKTKIQLEAKIKEVTER----AED-----EEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKH 975
Cdd:pfam12128 382 SKIKEQNNRDIAGIKDKLAKIREARDRqlavAEDdlqalESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 976 ATENKvKNLTEEMAGLDETIAKLTKEKKALQE-------AHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSL-EQE 1047
Cdd:pfam12128 462 LLLQL-ENFDERIERAREEQEAANAEVERLQSelrqarkRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlHFL 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1048 KKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDE------KLKKKEFEISnlqSKIEDEQALGIQLQKKIKELQARI 1121
Cdd:pfam12128 541 RKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGElnlygvKLDLKRIDVP---EWAASEEELRERLDKAEEALQSAR 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1122 EeleeeieaeraSRAKAEKQRSDLSRELEEISERLEEAGGAtsaqiemnkkreaeFQKMRRDLEEATLQHEATAATLRKK 1201
Cdd:pfam12128 618 E-----------KQAAAEEQLVQANGELEKASREETFARTA--------------LKNARLDLRRLFDEKQSEKDKKNKA 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1202 HADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGN-LEKMCRTLEDQLSELKSKEEEQqrlindLT 1280
Cdd:pfam12128 673 LAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQvVEGALDAQLALLKAAIAARRSG------AK 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1281 AQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRhdcDLLREQYEEEQESK 1360
Cdd:pfam12128 747 AELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRR---PRLATQLSNIERAI 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1361 AELQRALSKANTEVAQWRTKYET--DAIQRTE-ELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQneVEDLMLD 1437
Cdd:pfam12128 824 SELQQQLARLIADTKLRRAKLEMerKASEKQQvRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQ--LEDLKLK 901
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1438 VERtnaACAALDKKQRNFDKILAewKQKCEETHAELEASQKEARSLGTELFKIKNaYEESLDQLETLKreNKNLQQEISD 1517
Cdd:pfam12128 902 RDY---LSESVKKYVEHFKNVIA--DHSGSGLAETWESLREEDHYQNDKGIRLLD-YRKLVPYLEQWF--DVRVPQSIMV 973
|
730 740 750
....*....|....*....|....*....|....*....
gi 153791586 1518 LTEQIAEGGKRIHE----LEKIKKQVEQEKCELQAALEE 1552
Cdd:pfam12128 974 LREQVSILGVDLTEfydvLADFDRRIASFSRELQREVGE 1012
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
853-1719 |
4.59e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.43 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 853 KEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKiQLEAKIKEVTERA 932
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIE-RYQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 933 EDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKV-----EKEKHATE-NKVKNLTEEMAGLDEtIAKLTKEKkaLQ 1006
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYqqaldVQQTRAIQyQQAVQALERAKQLCG-LPDLTADN--AE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1007 EAHQQtlddLQAEEDkvnTLTKAKIKLEQQVDDLEGSLEQ-EKKLR--------MDLERAKRKlegdlklAQESIMDIEN 1077
Cdd:PRK04863 442 DWLEE----FQAKEQ---EATEELLSLEQKLSVAQAAHSQfEQAYQlvrkiageVSRSEAWDV-------ARELLRRLRE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1078 EKQQlDEKLKKKEFEISNLQSKIEDEQalgiQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISER-- 1155
Cdd:PRK04863 508 QRHL-AEQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERrm 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1156 -LEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAT------LRKKHADSVAELGEQIDNLQRVKQKLEKEKS 1228
Cdd:PRK04863 583 aLRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDsqdvteYMQQLLERERELTVERDELAARKQALDEEIE 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1229 EMK----------------------------MEIDDL------------ASNVETVSKAKGNLEKMCRTLED-------- 1260
Cdd:PRK04863 663 RLSqpggsedprlnalaerfggvllseiyddVSLEDApyfsalygparhAIVVPDLSDAAEQLAGLEDCPEDlyliegdp 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1261 -QLSELKSKEEEQQRLINDLTAQR-------------GR---------LQTESGEFSRQLDEKEALVSQLSRGKQAFTQ- 1316
Cdd:PRK04863 743 dSFDDSVFSVEELEKAVVVKIADRqwrysrfpevplfGRaarekrieqLRAEREELAERYATLSFDVQKLQRLHQAFSRf 822
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1317 ---------------QIEELKRQLEEEIKAKNALAHALQSsrhdcdlLREQYEEEQESKAELQRALSKANTEVAQWRTKY 1381
Cdd:PRK04863 823 igshlavafeadpeaELRQLNRRRVELERALADHESQEQQ-------QRSQLEQAKEGLSALNRLLPRLNLLADETLADR 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1382 ETDAIQRTEELEEAKKKLAQR-------------LQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNA----- 1443
Cdd:PRK04863 896 VEEIREQLDEAEEAKRFVQQHgnalaqlepivsvLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHfsyed 975
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1444 ACAALDKKQRNFDKI---LAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLetlkrenKNLQQEISDLTE 1520
Cdd:PRK04863 976 AAEMLAKNSDLNEKLrqrLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQML-------QELKQELQDLGV 1048
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1521 QIAEGgkrihelekIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNqvksEVDRKIAEKDEEIDQLKRNHIRIV 1600
Cdd:PRK04863 1049 PADSG---------AEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMD----NLTKKLRKLERDYHEMREQVVNAK 1115
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1601 ESMQSTLDAeIRSRNDAIRLKKKMEGDLNEMEiqLNHANRMAAEALRnyrntQGILKDTqiHLDDALRSQEDLK--EQL- 1677
Cdd:PRK04863 1116 AGWCAVLRL-VKDNGVERRLHRRELAYLSADE--LRSMSDKALGALR-----LAVADNE--HLRDVLRLSEDPKrpERKv 1185
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1678 -------AMVERRAN------------LLQAEIEELRATLEQTERsrkiaEQELLDASERV 1719
Cdd:PRK04863 1186 qfyiavyQHLRERIRqdiirtddpveaIEQMEIELSRLTEELTSR-----EQKLAISSESV 1241
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
852-1615 |
5.02e-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: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 852 EKEMATMKEEFQKIKDELAKS--EAKRKELEeKMVTLLKE------KNDLQLQVQAEAEGLADAEERCDQLIKT----KI 919
Cdd:TIGR01612 969 DNTLIDKINELDKAFKDASLNdyEAKNNELI-KYFNDLKAnlgknkENMLYHQFDEKEKATNDIEQKIEDANKNipniEI 1047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 920 QLEAKIKEVTERAEDEEEINAELTAKK--RKLEDECSELKKDIDDLEL----TLAKVEKEKHATE-NKVKNlteEMAGLD 992
Cdd:TIGR01612 1048 AIHTSIYNIIDEIEKEIGKNIELLNKEilEEAEINITNFNEIKEKLKHynfdDFGKEENIKYADEiNKIKD---DIKNLD 1124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 993 ETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIkleqQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQEsI 1072
Cdd:TIGR01612 1125 QKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAI----SNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNE-I 1199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1073 MDIENEK----------------------QQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELqARIEELEEEIEA 1130
Cdd:TIGR01612 1200 AEIEKDKtsleevkginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEM-GIEMDIKAEMET 1278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1131 ERASRAKAEKQRSDLSRELEEISERLEEaggatSAQIEMNKKREAEFQKMRRDLEEATLQHEataatlrkKHADSVAELG 1210
Cdd:TIGR01612 1279 FNISHDDDKDHHIISKKHDENISDIREK-----SLKIIEDFSEESDINDIKKELQKNLLDAQ--------KHNSDINLYL 1345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1211 EQIDNLQRVKQ--KLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLED--QLSELKSKEEEQ------QRLINDLT 1280
Cdd:TIGR01612 1346 NEIANIYNILKlnKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDdiNLEECKSKIESTlddkdiDECIKKIK 1425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1281 AQRGRLQTESGE---FSRQLDEKEALVSQLSRgkqafTQQIEELKRQLEEEIKAKNAlahalqSSRHDCDL--LREQYEE 1355
Cdd:TIGR01612 1426 ELKNHILSEESNidtYFKNADENNENVLLLFK-----NIEMADNKSQHILKIKKDNA------TNDHDFNIneLKEHIDK 1494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1356 EQESKAELQRalskantevaqwrtkyETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNaKCASLEKTKQRLQNEVEDLm 1435
Cdd:TIGR01612 1495 SKGCKDEADK----------------NAKAIEKNKELFEQYKKDVTELLNKYSALAIKN-KFAKTKKDSEIIIKEIKDA- 1556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1436 ldverTNAACAALDKKQRNFDKILAEwKQKCEETHAELEASQKEA-------RSLGTELFKIKNAYEESLDQLetlkREN 1508
Cdd:TIGR01612 1557 -----HKKFILEAEKSEQKIKEIKKE-KFRIEDDAAKNDKSNKAAidiqlslENFENKFLKISDIKKKINDCL----KET 1626
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1509 KNLQQEISDLT-----EQIAEGGKRIHELEKIKKQVEQEKcelqAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIA 1583
Cdd:TIGR01612 1627 ESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQK----KNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGII 1702
|
810 820 830
....*....|....*....|....*....|...
gi 153791586 1584 EKDEEIDQLKRNHIR-IVESMQSTLDAEIRSRN 1615
Cdd:TIGR01612 1703 EKIKEIAIANKEEIEsIKELIEPTIENLISSFN 1735
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
867-1322 |
5.45e-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: 58.19 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 867 DELAKSEAKRKELEE---KMVTLLKEKNDLQLQVQAEAEGLADAE-ERCDQLIKTKIQLEAKIKEVteraedeEEINAEL 942
Cdd:pfam05483 362 EELLRTEQQRLEKNEdqlKIITMELQKKSSELEEMTKFKNNKEVElEELKKILAEDEKLLDEKKQF-------EKIAEEL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 943 TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT--------KEKKALQEAHQQTLD 1014
Cdd:pfam05483 435 KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTahcdklllENKELTQEASDMTLE 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1015 dLQAEEDKVNTLTKAKIKLEQQVDDLEgslEQEKKLRMDLERAKRKL--EGD-----LKLAQESIMDIENEKQQLDEKLK 1087
Cdd:pfam05483 515 -LKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFiqKGDevkckLDKSEENARSIEYEVLKKEKQMK 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1088 KKEFEISNLQSKIEDEQalgiqlqKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQI 1167
Cdd:pfam05483 591 ILENKCNNLKKQIENKN-------KNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEI 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1168 EMNKKREaefQKMRRDLEEAtlqheataatlrKKHADSVAELGEQIDnlQRVKQKLekeksemkmeiddlASNVETVSKA 1247
Cdd:pfam05483 664 EDKKISE---EKLLEEVEKA------------KAIADEAVKLQKEID--KRCQHKI--------------AEMVALMEKH 712
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791586 1248 KGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELK 1322
Cdd:pfam05483 713 KHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1394-1604 |
5.65e-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: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1394 EAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAEL 1473
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1474 EASQKEARSLGTELFKIKNA-----------YEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQe 1542
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA- 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791586 1543 kceLQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQ 1604
Cdd:COG4942 179 ---LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1007-1455 |
6.11e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 6.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1007 EAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQesimdIENEKQQLDEKL 1086
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-----LEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1087 KKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEEleeeieaeraSRAKAEKQRSDLSRELEEISERLEEAGGATsaq 1166
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQ----------LSLATEEELQDLAEELEELQQRLAELEEEL--- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1167 iemnKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSK 1246
Cdd:COG4717 216 ----EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1247 AKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLE 1326
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1327 EEIKAKNALAHALQSSRHDCDLLREqYEEEQESKAELQRALSKANTEVAQWRTKYETDAI-QRTEELEEAKKKLAQRLQA 1405
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEELeEELEELEEELEELEEELEE 450
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791586 1406 AEEHVEAVNAKCASLEKT---------KQRLQNEVEDLMLDVERTNAACAALDKKQRNF 1455
Cdd:COG4717 451 LREELAELEAELEQLEEDgelaellqeLEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1134-1336 |
1.38e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1134 SRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAEFQKMRRDLEEATLQHEATAATLRKKHADsVAELGEQI 1213
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAA--------------QAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1214 DNLQrvkQKLEKEKSEMKM----------------------EIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEE 1271
Cdd:COG3883 75 AEAE---AEIEERREELGEraralyrsggsvsyldvllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791586 1272 QQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALA 1336
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
657-681 |
1.46e-07 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 53.12 E-value: 1.46e-07
10 20
....*....|....*....|....*
gi 153791586 657 FRENLNKLMTNLRSTHPHFVRCIIP 681
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
924-1414 |
2.29e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.06 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 924 KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT---K 1000
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSsleD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1001 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDD--------------LEGSLEQEKKLRMDLERAKRKLEGDLK 1066
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDpvyknrnyindyfkYKNDIENKKQILSNIDAEINKYHAIIK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1067 LAQesimDIENEKQQLDEKLKKKE---FEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRS 1143
Cdd:PRK01156 330 KLS----VLQKDYNDYIKKKSRYDdlnNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1144 DLSRELEEISERLEE-AGGATSAQIEMNKKREAEfQKMRRDLEE----------ATLQHEATAATLRKKHADSVAELGEQ 1212
Cdd:PRK01156 406 AIKKELNEINVKLQDiSSKVSSLNQRIRALRENL-DELSRNMEMlngqsvcpvcGTTLGEEKSNHIINHYNEKKSRLEEK 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1213 IDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRT----LEDQLSELKSKEEEQQRLIN--------DLT 1280
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARAdledIKIKINELKDKHDKYEEIKNrykslkleDLD 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1281 AQRGR---------------LQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHD 1345
Cdd:PRK01156 565 SKRTSwlnalavislidietNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKIL 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1346 CDLLREQYEEEQESKAE------------------------LQRALSKANTEVAQWRTKYETDaIQRTEELEEAKKKLAQ 1401
Cdd:PRK01156 645 IEKLRGKIDNYKKQIAEidsiipdlkeitsrindiednlkkSRKALDDAKANRARLESTIEIL-RTRINELSDRINDINE 723
|
570
....*....|...
gi 153791586 1402 RLQAAEEHVEAVN 1414
Cdd:PRK01156 724 TLESMKKIKKAIG 736
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1097-1331 |
2.36e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1097 QSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEaggaTSAQIEMNKKREAE 1176
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA----LEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1177 FQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETvskakgnlekmcr 1256
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE------------- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791586 1257 tLEDQLSELKSKEEEQQRLINDLTAQRGRLQtesgefsRQLDEKEALVSQLSRGKQAFTQQIEELKRQ---LEEEIKA 1331
Cdd:COG4942 162 -LAALRAELEAERAELEALLAELEEERAALE-------ALKAERQKLLARLEKELAELAAELAELQQEaeeLEALIAR 231
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1251-1524 |
2.41e-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: 56.01 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1251 LEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIK 1330
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1331 AKNALAHALQSSRhdcdllreQYEEEQESKAELQRALSKANTevaqwrtKYETDAI-QRTEELEEAKKKLAQRLQAAEEH 1409
Cdd:pfam09726 480 ARASAEKQLAEEK--------KRKKEEEATAARAVALAAASR-------GECTESLkQRKRELESEIKKLTHDIKLKEEQ 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1410 VEAVNAKCASLEKTKQRlQNEVEDLMldvertnAACAALDKKQRNFDKILAewkqkcEETHAELeasqkearslgtELFk 1489
Cdd:pfam09726 545 IRELEIKVQELRKYKES-EKDTEVLM-------SALSAMQDKNQHLENSLS------AETRIKL------------DLF- 597
|
250 260 270
....*....|....*....|....*....|....*
gi 153791586 1490 ikNAYEESLDQLETLKRENKNLQQEISDLTEQIAE 1524
Cdd:pfam09726 598 --SALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAE 630
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
850-1247 |
2.85e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 55.53 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 850 ETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEgladaEERCDQLIKTKIQLEAKIKEVT 929
Cdd:pfam09731 53 EDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEE-----KEATKDAAEAKAQLPKSEQEKE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 930 ERAEDEEEINAELTAKKRKLEdecselkkdiddLELTLAKVEKEKHATEN-KVKNLTEEMAGLDETIAKLTKEKKALQEA 1008
Cdd:pfam09731 128 KALEEVLKEAISKAESATAVA------------KEAKDDAIQAVKAHTDSlKEASDTAEISREKATDSALQKAEALAEKL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1009 HQQTLDDLQAEEDKVN-TLTKAKIKLEQQVDDL---EGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDE 1084
Cdd:pfam09731 196 KEVINLAKQSEEEAAPpLLDAAPETPPKLPEHLdnvEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1085 KLKKkeFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEaerasrakaEKQRSDLSRELEEISERLEEAGGATS 1164
Cdd:pfam09731 276 EDNL--LSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERAL---------EKQKEELDKLAEELSARLEEVRAADE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1165 AQIEmnKKREAEFQKMRRDLEE---ATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNV 1241
Cdd:pfam09731 345 AQLR--LEFEREREEIRESYEEklrTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNELLANL 422
|
....*.
gi 153791586 1242 ETVSKA 1247
Cdd:pfam09731 423 KGLEKA 428
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1438-1915 |
2.91e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1438 VERTNAACAALDKKQRNFDKILAEwKQKCEETHAELEASQKEARSLGTELFKIKNAYEEsLDQLETLKRENKNLQQEISD 1517
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1518 LTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHI 1597
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1598 RIVESMQSTLDAEIRSRNDAIRLkkkmegDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQL 1677
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLL------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1678 AMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLEtdISQMQGEMEDILQEARNA 1757
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1758 EEkakKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkggKKQIQKLEARVRELEGEVESEQK 1837
Cdd:COG4717 383 DE---EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL------EEELEELEEELEELEEELEELRE 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791586 1838 RNAEAVKGLRKHERrvkeltyqteedrknilrlQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEER 1915
Cdd:COG4717 454 ELAELEAELEQLEE-------------------DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1083-1328 |
3.38e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1083 DEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIeeleeeieaerasrAKAEKQRSDLSRELEEISERLEEAgga 1162
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEY--------------NELQAELEALQAEIDKLQAEIAEA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1163 tSAQIEmnkKREAEFQKMRRDLEEATLQHEATAATLrkkHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVE 1242
Cdd:COG3883 78 -EAEIE---ERREELGERARALYRSGGSVSYLDVLL---GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1243 TVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELK 1322
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
....*.
gi 153791586 1323 RQLEEE 1328
Cdd:COG3883 231 AAAAAA 236
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1670-1918 |
3.59e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1670 QEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKI--AEQELLDASERVQLLHTQNTSLintkkklETDISQMQGEm 1747
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSEL-------ESQLAEARAE- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1748 ediLQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMkknmeqtvkdLQLRLDEAEQLALKGGK-KQIQKLEARVR 1826
Cdd:COG3206 235 ---LAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQL----------AELEAELAELSARYTPNhPDVIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1827 ELEGEVESEQKRNAEAVKG-LRKHERRVKELTYQTEEDRKNILRLQdlvdKLQAKVKSYKRQAEEAEEQSNTNLAKFRKL 1905
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAeLEALQAREASLQAQLAQLEARLAELP----ELEAELRRLEREVEVARELYESLLQRLEEA 377
|
250
....*....|...
gi 153791586 1906 QheLEEAEERADI 1918
Cdd:COG3206 378 R--LAEALTVGNV 388
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1565-1915 |
3.87e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.73 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1565 LRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESmQSTLDAEIRSRND-------AIRLKKKME---GDLNEMEIQ 1634
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEA-ESDLEQDYQAASDhlnlvqtALRQQEKIEryqADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1635 LNHANRMAAEAlrnyrntQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQaeieelratleqterSRKIAEQELLD 1714
Cdd:PRK04863 364 LEEQNEVVEEA-------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQ---------------TRAIQYQQAVQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1715 ASERVQLLhTQNTSLinTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERmkKNMEQ 1794
Cdd:PRK04863 422 ALERAKQL-CGLPDL--TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSR--SEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1795 TVKDLQLRLDEAEQLAlkggkKQIQKLEARVRELEGEVESEQkrnaEAVKGLRKHERRVkELTYQTEEDrknilrLQDLV 1874
Cdd:PRK04863 497 VARELLRRLREQRHLA-----EQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRL-GKNLDDEDE------LEQLQ 560
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 153791586 1875 DKLQAKVKSYKRQAEEAEEQSNTnlakfrkLQHELEEAEER 1915
Cdd:PRK04863 561 EELEARLESLSESVSEARERRMA-------LRQQLEQLQAR 594
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
857-1023 |
3.91e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 857 TMKEEFQKIKDeLAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTER-AEDE 935
Cdd:COG1579 1 AMPEDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARiKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 936 EEINAELTAKKRK-LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLD 1014
Cdd:COG1579 80 EQLGNVRNNKEYEaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
....*....
gi 153791586 1015 DLQAEEDKV 1023
Cdd:COG1579 160 ELEAEREEL 168
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1471-1623 |
5.30e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.62 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1471 AELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRI-------------HELEKIKK 1537
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnkeyealqKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1538 QV---EQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNhiriVESMQSTLDAEIRSR 1614
Cdd:COG1579 104 RIsdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE----REELAAKIPPELLAL 179
|
....*....
gi 153791586 1615 NDAIRLKKK 1623
Cdd:COG1579 180 YERIRKRKN 188
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
920-1430 |
5.32e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 920 QLEAKIKEVTErAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEK--HATENKVKNLTEEMAGLDETIAK 997
Cdd:COG4717 72 ELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqlLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 998 LTKEKKALQEAHQQtlddlqaeedkvntltkaKIKLEQQVDDLEGSLEQEkklrmdLERAKRKLEGDLKLAQESIMDIEN 1077
Cdd:COG4717 151 LEERLEELRELEEE------------------LEELEAELAELQEELEEL------LEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1078 EKQQLDEKLKKKEFEISNLQSKIEdeqalgiqlqkkikelqarieeleeeieaerasRAKAEKQRSDLSRELEEISERLE 1157
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELE---------------------------------QLENELEAAALEERLKEARLLLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1158 EAGGATSAQIEMnkkreAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDL 1237
Cdd:COG4717 254 IAAALLALLGLG-----GSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1238 ASNVETVSKAKGNLEKMCRTLEDQLSELksKEEEQQRLINDLTAQRGRLQTESGefsrqLDEKEALVSQLSRGKQAftQQ 1317
Cdd:COG4717 329 GLPPDLSPEELLELLDRIEELQELLREA--EELEEELQLEELEQEIAALLAEAG-----VEDEEELRAALEQAEEY--QE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1318 IEELKRQLEEEIKAKNALAHALqSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAqwRTKYETDAIQRTEELEEAKK 1397
Cdd:COG4717 400 LKEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEELEEELEELREELA--ELEAELEQLEEDGELAELLQ 476
|
490 500 510
....*....|....*....|....*....|....*.
gi 153791586 1398 KLAQRLQAAEEHVEAVNAKCAS---LEKTKQRLQNE 1430
Cdd:COG4717 477 ELEELKAELRELAEEWAALKLAlelLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1536-1774 |
6.67e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1536 KKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVksevDRKIAEKDEEIDQLkrnhirivESMQSTLDAEIRsrn 1615
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRAL--------EQELAALEAELA--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1616 daiRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELR 1695
Cdd:COG4942 87 ---ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791586 1696 ATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEE 1774
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
859-1049 |
9.55e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 859 KEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEI 938
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 939 NAELTAKKRKLEDECS-------------------------ELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDE 993
Cdd:COG4942 106 LAELLRALYRLGRQPPlalllspedfldavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791586 994 TIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKK 1049
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1679-1941 |
9.81e-07 |
|
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: 54.29 E-value: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1679 MVERranLLQAEIEELRATLEQ-------TERsRKIAEQELLDASE---RVQLLHTQntslinTKKKLETdiSQMQGEME 1748
Cdd:TIGR02168 145 KISE---IIEAKPEERRAIFEEaagiskyKER-RKETERKLERTREnldRLEDILNE------LERQLKS--LERQAEKA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1749 DILQEARNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVREL 1828
Cdd:TIGR02168 213 ERYKELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEELRLEVSEL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1829 EGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHE 1908
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
250 260 270
....*....|....*....|....*....|...
gi 153791586 1909 LEEAEERADIAESQVNKLRVKSREVHTKVISEE 1941
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1284-1703 |
1.14e-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: 53.36 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1284 GRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAEL 1363
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1364 ---QRALSKANTEvaqwrtkyetdAIQRTEELEEAKKKLAQRLQAAEehveavnakcASLEKTKQRLQNevedlmldver 1440
Cdd:pfam07888 114 seeKDALLAQRAA-----------HEARIRELEEDIKTLTQRVLERE----------TELERMKERAKK----------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1441 tnaacAALDKKQRNFDKilaewkqkcEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETlkrenknLQQEISDLTE 1520
Cdd:pfam07888 162 -----AGAQRKEEEAER---------KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1521 QIAEGGKRIHELEKIKKqveqekcELQAALEEAEASLEHEEGkilrIQLELNQVKSEVDRKIAEKdeeidqlkrnHIRIV 1600
Cdd:pfam07888 221 KLTTAHRKEAENEALLE-------ELRSLQERLNASERKVEG----LGEELSSMAAQRDRTQAEL----------HQARL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1601 ESMQSTL---DAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQ-------------GILKD-TQIHL 1663
Cdd:pfam07888 280 QAAQLTLqlaDASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQeermereklevelGREKDcNRVQL 359
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 153791586 1664 DDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTER 1703
Cdd:pfam07888 360 SESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1318-1893 |
1.20e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1318 IEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYE--TDAIQRTEELEEA 1395
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1396 KKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLqNEVEDLMLDVERTNAACAALDKKQ-RNFDKILAEWK---QKCEETHA 1471
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYKELEERH-MKIINDPVYKNRNYINDYFKYKNDiENKKQILSNIDaeiNKYHAIIK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1472 ELEASQKEArslgtelfkiknayeeslDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALE 1551
Cdd:PRK01156 330 KLSVLQKDY------------------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1552 EAEASLEHEEGKILRIQLELNQVKSEVDR---KIAEKDEEIDQLKRNHIRIVESMQ-----------STLDAEIRSRnda 1617
Cdd:PRK01156 392 FISEILKIQEIDPDAIKKELNEINVKLQDissKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcGTTLGEEKSN--- 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1618 iRLKKKMEGDLNEMEIQLNHANRMAAEalrnyrntqgilkdtqihLDDALRSQEDLKEQLAMVE-RRANLLQAEIEELRA 1696
Cdd:PRK01156 469 -HIINHYNEKKSRLEEKIREIEIEVKD------------------IDEKIVDLKKRKEYLESEEiNKSINEYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1697 TLEQTersrKIAEQELLDASERVQLLHTQNTSL-INTKKKLETDISQMQGEMEDILQEA-RNAEEKAKKAITDAAMMAEE 1774
Cdd:PRK01156 530 DLEDI----KIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWLNALAVISLIDIETnRSRSNEIKKQLNDLESRLQE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1775 LKKE-QDTSAHLERMKKNMEQTVKDLQLRLDEAEQLalkggKKQIQKLEARVRELE---GEVESEQKRNAEAVKGLRKHE 1850
Cdd:PRK01156 606 IEIGfPDDKSYIDKSIREIENEANNLNNKYNEIQEN-----KILIEKLRGKIDNYKkqiAEIDSIIPDLKEITSRINDIE 680
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 153791586 1851 RRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEE 1893
Cdd:PRK01156 681 DNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
841-1465 |
1.27e-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: 53.97 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 841 KIKPLLKSAETEKEM------------ATMKEEFQKIKDELAKSEAKRKELE--EKMVTLLKEKNDLQLQ----VQAEAE 902
Cdd:pfam15921 462 KVSSLTAQLESTKEMlrkvveeltakkMTLESSERTVSDLTASLQEKERAIEatNAEITKLRSRVDLKLQelqhLKNEGD 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 903 GLADAEERCDQLiktKIQLEAK---IKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATEN 979
Cdd:pfam15921 542 HLRNVQTECEAL---KLQMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 980 KVKNLTEEMAGLDETIAKLT-------KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQE-KKLR 1051
Cdd:pfam15921 619 KIRELEARVSDLELEKVKLVnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTtNKLK 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1052 MDLERAKRKLE---GDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIedeqalgiqlqkkikelqariEELEEEI 1128
Cdd:pfam15921 699 MQLKSAQSELEqtrNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKI---------------------QFLEEAM 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1129 EAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQ----------HEATAATL 1198
Cdd:pfam15921 758 TNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQfaecqdiiqrQEQESVRL 837
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1199 RKKHADSVAEL-GEQIDNLQRVKQKLEKEKSEMKMEiDDLASNVETVS-------KAKGNLEKMCRTLEDQLSELKSKEE 1270
Cdd:pfam15921 838 KLQHTLDVKELqGPGYTSNSSMKPRLLQPASFTRTH-SNVPSSQSTASflshhsrKTNALKEDPTRDLKQLLQELRSVIN 916
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1271 EQQRLINDLTAQRGRlQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQ-SSRHDCDLL 1349
Cdd:pfam15921 917 EEPTVQLSKAEDKGR-APSLGALDDRVRDCIIESSLRSDICHSSSNSLQTEGSKSSETCSREPVLLHAGElEDPSSCFTF 995
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1350 REQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKklaqrLQAAEEHVEAVNAKCASLEKTKQRLQN 1429
Cdd:pfam15921 996 PSTASPSVKNSASRSFHSSPKKSPVHSLLTSSAEGSIGSSSQYRSAKT-----IHSPDSVKDSQSLPIETTGKTCRKLQN 1070
|
650 660 670
....*....|....*....|....*....|....*.
gi 153791586 1430 EVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQK 1465
Cdd:pfam15921 1071 RLESLQTLVEDLQLKNQAMSSMIRNQEKRIQKVKDQ 1106
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1403-1614 |
1.39e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1403 LQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELE---ASQKE 1479
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraRALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1480 ARSLGTELFKIKNA--YEESLDQLETLKRENKNLQQEISDLTEQIAEggkriheLEKIKKQVEQEKCELQAALEEAEASL 1557
Cdd:COG3883 98 SGGSVSYLDVLLGSesFSDFLDRLSALSKIADADADLLEELKADKAE-------LEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791586 1558 EHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSR 1614
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1456-1621 |
1.85e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1456 DKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAE----------- 1524
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1525 ----GG------------------KRIHELEKI----KKQVEQEKcELQAALEEAEASLEHEEGKILRIQLELNQVKSEV 1578
Cdd:COG3883 95 lyrsGGsvsyldvllgsesfsdflDRLSALSKIadadADLLEELK-ADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 153791586 1579 DRKIAEKDEEIDQLKRNhIRIVESMQSTLDAEIRSRNDAIRLK 1621
Cdd:COG3883 174 EAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1195-1556 |
2.56e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.20 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1195 AATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQR 1274
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1275 LINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELK-------RQLEEEIKAKNALAHALQSSRHDCD 1347
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKerakkagAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1348 LLREQYEEEQESKAELQRALSKANTEVAQWRTKYETdAIQRTEELEEAKKKLA---QRLQAAEEHVEAVNAKCASLEKTK 1424
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT-AHRKEAENEALLEELRslqERLNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1425 QRLQNEVEDLMLDVERTNAACAALDKKQRNFDkilAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEE-------- 1496
Cdd:pfam07888 268 DRTQAELHQARLQAAQLTLQLADASLALREGR---ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEermerekl 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791586 1497 ----------SLDQLETLKRENKNL-------QQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEAS 1556
Cdd:pfam07888 345 evelgrekdcNRVQLSESRRELQELkaslrvaQKEKEQLQAEKQELLEYIRQLEQRLETVADAKWSEAALTSTERPD 421
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1005-1561 |
2.87e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.50 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1005 LQEAHQQTLDD-LQAEEDKVNTLTKAKIKLEQQVDdlegSLEQEKKLRMDLERAKRKLegdlklaQESIMDIENEKQQLD 1083
Cdd:PRK10246 213 LTPEQVQSLTAsLQVLTDEEKQLLTAQQQQQQSLN----WLTRLDELQQEASRRQQAL-------QQALAAEEKAQPQLA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1084 E-KLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAErasRAKAEKQRSDLSRELEEISERLEEAGGA 1162
Cdd:PRK10246 282 AlSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARI---RHHAAKQSAELQAQQQSLNTWLAEHDRF 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1163 TSAQIEMNKKReAEFQKMRRDLEEATLQHEATAATLRKKHA----------DSVAELGEQIDNLQRVKQKLEKEKSEMKM 1232
Cdd:PRK10246 359 RQWNNELAGWR-AQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltaDEVAAALAQHAEQRPLRQRLVALHGQIVP 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1233 EIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEE---------EQQRLINDLTAQRGRLQT--------------- 1288
Cdd:PRK10246 438 QQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQqladvkticEQEARIKDLEAQRAQLQAgqpcplcgstshpav 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1289 ------ESGEFSRQLDEKEALVSQLS------RGK-QAFTQQI----EELKRQLEEE---IKAKNALAHALQSSRHDCD- 1347
Cdd:PRK10246 518 eayqalEPGVNQSRLDALEKEVKKLGeegaalRGQlDALTKQLqrdeSEAQSLRQEEqalTQQWQAVCASLNITLQPQDd 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1348 ---LLREQYEEEQE-----SKAELQRALSKANTEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQAAEEHVEAVNAKcAS 1419
Cdd:PRK10246 598 iqpWLDAQEEHERQlrllsQRHELQGQIAAHNQQIIQYQQQIE----QRQQQLLTALAGYALTLPQEDEEASWLATR-QQ 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1420 LEKTKQRLQNEVEDLM---------------LDVERTNAACAALDKKQRNFDKIL---AEW----KQKCEETHAELEASQ 1477
Cdd:PRK10246 673 EAQSWQQRQNELTALQnriqqltplletlpqSDDLPHSEETVALDNWRQVHEQCLslhSQLqtlqQQDVLEAQRLQKAQA 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1478 KEARSLGTELFKIKNAY------EESLDQLETLKRENKN-----------------------------------LQQEIS 1516
Cdd:PRK10246 753 QFDTALQASVFDDQQAFlaalldEETLTQLEQLKQNLENqrqqaqtlvtqtaqalaqhqqhrpdgldltvtveqIQQELA 832
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 153791586 1517 DLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEE-AEASLEHEE 1561
Cdd:PRK10246 833 QLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQQiAQATQQVED 878
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1241-1559 |
3.77e-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: 52.26 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1241 VETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLIN------DLTAQRGRLQTESgefsrqldekEALVSQLSRGKQAF 1314
Cdd:COG3096 274 MRHANERRELSERALELRRELFGARRQLAEEQYRLVEmareleELSARESDLEQDY----------QAASDHLNLVQTAL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1315 TQQ---------IEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRtkyetDA 1385
Cdd:COG3096 344 RQQekieryqedLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQ-----QA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1386 IQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLekTKQRLQNE-------------------VEDLMLDVERTNAACA 1446
Cdd:COG3096 419 VQALEKARALCGLPDLTPENAEDYLAAFRAKEQQA--TEEVLELEqklsvadaarrqfekayelVCKIAGEVERSQAWQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1447 A--LDKKQRNFdKILAEWKQKCEETHAELE---ASQKEARSLGTELFKIKNAYEESLDQLETLKREnknLQQEISDLTEQ 1521
Cdd:COG3096 497 AreLLRRYRSQ-QALAQRLQQLRAQLAELEqrlRQQQNAERLLEEFCQRIGQQLDAAEELEELLAE---LEAQLEELEEQ 572
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 153791586 1522 IAEGGKRIHELEKIKKQVEQEKCELQA---ALEEAEASLEH 1559
Cdd:COG3096 573 AAEAVEQRSELRQQLEQLRARIKELAArapAWLAAQDALER 613
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1495-1693 |
3.91e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.78 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1495 EESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKikkqveqEKCELQAALEEAEASLEHEEGKILRIQLELNQv 1574
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-------EVEELEAELEEKDERIERLERELSEARSEERR- 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1575 KSEVDRKIAEKDEEIDQLKrnhiRIVESMQSTLDaEIRSRNDaiRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQG 1654
Cdd:COG2433 460 EIRKDREISRLDREIERLE----RELEEERERIE-ELKRKLE--RLKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYG 532
|
170 180 190
....*....|....*....|....*....|....*....
gi 153791586 1655 ILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEE 1693
Cdd:COG2433 533 LKEGDVVYLRDASGAGRSTAELLAEAGPRAVIVPGELSE 571
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
858-1105 |
4.16e-06 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 51.78 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 858 MKEEFQKIKDELAKSEAKRKELEEkmvtlLKEKNDLqLQVQAEAEGLADAEERCDQLiktKIQLEAKIKEVTERAEDEEE 937
Cdd:PLN03229 509 LMEKIEKLKDEFNKRLSRAPNYLS-----LKYKLDM-LNEFSRAKALSEKKSKAEKL---KAEINKKFKEVMDRPEIKEK 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 938 INAeltakkRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMaGLDETIAKltkeKKALQEAHQQTLDDLQ 1017
Cdd:PLN03229 580 MEA------LKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSM-GLEVIGVT----KKNKDTAEQTPPPNLQ 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1018 AEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKklrmdLERAKRKLEGDLKLAQEsimdIENEKQQLDEKLKKKeFEISNLQ 1097
Cdd:PLN03229 649 EKIESLNEEINKKIERVIRSSDLKSKIELLK-----LEVAKASKTPDVTEKEK----IEALEQQIKQKIAEA-LNSSELK 718
|
....*...
gi 153791586 1098 SKIEDEQA 1105
Cdd:PLN03229 719 EKFEELEA 726
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1358-1912 |
4.70e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 51.76 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1358 ESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDlMLD 1437
Cdd:pfam12128 119 ETVAELGRFMKNAGIQRTNLLNTREYRSIIQNDRTLLGRERVELRSLARQFALCDSESPLRHIDKIAKAMHSKEGK-FRD 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1438 VERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEArslgTELFKIKNAYEesldQLETLKRENKNLQQEISD 1517
Cdd:pfam12128 198 VKSMIVAILEDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIR----PEFTKLQQEFN----TLESAELRLSHLHFGYKS 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1518 LTEQIAEggkrihelekikkqvEQEKC-ELQAALEEAEASLEHEegkILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNH 1596
Cdd:pfam12128 270 DETLIAS---------------RQEERqETSAELNQLLRTLDDQ---WKEKRDELNGELSAADAAVAKDRSELEALEDQH 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1597 IRI----VESMQSTLDAEIRSRNDAIRLKKKMEGDL-NEMEIQLNHANRMAAEALRNYRNTQGIlkdtqihlDDALRSQE 1671
Cdd:pfam12128 332 GAFldadIETAAADQEQLPSWQSELENLEERLKALTgKHQDVTAKYNRRRSKIKEQNNRDIAGI--------KDKLAKIR 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1672 DLKEQLAMVERraNLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLhtQNTSLINTKKKLETDISQmqgemeDIL 1751
Cdd:pfam12128 404 EARDRQLAVAE--DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLR--LNQATATPELLLQLENFD------ERI 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1752 QEARNAEEKAKKAITDAAMMAEELKKEQD-TSAHLERmkknMEQTVKDLQLRLDEAE-QLALKGG-------------KK 1816
Cdd:pfam12128 474 ERAREEQEAANAEVERLQSELRQARKRRDqASEALRQ----ASRRLEERQSALDELElQLFPQAGtllhflrkeapdwEQ 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1817 QIQKLEARVR----ELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDrknilRLQDLVDKLQAKVKSYKRQAEEAE 1892
Cdd:pfam12128 550 SIGKVISPELlhrtDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEE-----ELRERLDKAEEALQSAREKQAAAE 624
|
570 580
....*....|....*....|
gi 153791586 1893 EQSNTNLAKFRKLQHELEEA 1912
Cdd:pfam12128 625 EQLVQANGELEKASREETFA 644
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
957-1539 |
5.87e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 957 KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLD----------ETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTL 1026
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDyleeklkssnLELENIKKQIADDEKSHSITLKEIERLSIEYNNA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1027 TKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGD------LKLAQESIMDIENEKQQLDE-------KLKKKEFEI 1093
Cdd:PRK01156 231 MDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMEleknnyYKELEERHMKIINDPVYKNRnyindyfKYKNDIENK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1094 SNLQSKIEDEQALGIQLQKKIKELQARIEELEeeieaerasraKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKR 1173
Cdd:PRK01156 311 KQILSNIDAEINKYHAIIKKLSVLQKDYNDYI-----------KKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKI 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1174 EAEfqkmrrdleeatlqheataatlRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEK 1253
Cdd:PRK01156 380 EEY----------------------SKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1254 MCRTLEDQLSELKSK-----------EEEQQRLINDLTAQRGRLQTESGEFSRQ---LDEK----EALVSQLSRGK---- 1311
Cdd:PRK01156 438 NLDELSRNMEMLNGQsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREIEIEvkdIDEKivdlKKRKEYLESEEinks 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1312 QAFTQQIEELKRQLEEEIKAKNALAHAlqssrhdcDLLREQYEEEQES-KAELQRALSKANTEVAQWRTKYETDAIQ-RT 1389
Cdd:PRK01156 518 INEYNKIESARADLEDIKIKINELKDK--------HDKYEEIKNRYKSlKLEDLDSKRTSWLNALAVISLIDIETNRsRS 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1390 EELEEAKKKLAQRLQAAEEHVEAVNakcASLEKTKQRLQNEVEDL---MLDVERTNAACAALDKKQRNFDKILAEwKQKC 1466
Cdd:PRK01156 590 NEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLnnkYNEIQENKILIEKLRGKIDNYKKQIAE-IDSI 665
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791586 1467 EETHAELEAsqkEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQV 1539
Cdd:PRK01156 666 IPDLKEITS---RINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1581-1932 |
6.06e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.44 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1581 KIAEKDEEIDQLKRNHIRIVESM--QSTLDAEIRSRNDAIRLKKKMEGDLNEMEiqlnhaNRMAAEALRNYR--NTQGIL 1656
Cdd:PLN02939 64 KLQSNTDENGQLENTSLRTVMELpqKSTSSDDDHNRASMQRDEAIAAIDNEQQT------NSKDGEQLSDFQleDLVGMI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1657 KDTQ---IHLDDA-LRSQEDLKEQLAmvERRAnlLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINT 1732
Cdd:PLN02939 138 QNAEkniLLLNQArLQALEDLEKILT--EKEA--LQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1733 KKKLETDISQMQGEMEDILQEarNAEEKAkkaitDAAMMAEELKKEQDTS---AHLERMKKNMEQTVKDLQLRLDEAEQL 1809
Cdd:PLN02939 214 GATEGLCVHSLSKELDVLKEE--NMLLKD-----DIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQED 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1810 ALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKH---ERRVKELTYQTEEdrKNILRLQ-DLVDKLQAKVKSYK 1885
Cdd:PLN02939 287 VSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNqdlRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLLE 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 153791586 1886 RQAEEAEEQSNTNLAKFrklQHELEEAEeraDIAESQVNKLRVKSRE 1932
Cdd:PLN02939 365 ERLQASDHEIHSYIQLY---QESIKEFQ---DTLSKLKEESKKRSLE 405
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1459-1940 |
6.08e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1459 LAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQ 1538
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1539 VEQEKCELQAALEEAEASLEHeegkiLRIQLElnQVKSEVDRKIAEKDEEIDQLKRNHIRIV---ESMQSTLDAEIRSRN 1615
Cdd:pfam05483 181 TRQVYMDLNNNIEKMILAFEE-----LRVQAE--NARLEMHFKLKEDHEKIQHLEEEYKKEIndkEKQVSLLLIQITEKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1616 DAIR----LKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEI 1691
Cdd:pfam05483 254 NKMKdltfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1692 EELRATLEQTERSRKIAEQELLDASERVQ-LLHTQNTSLINTKKKLETDISQMQ---GEMEDILQEARNAE---EKAKKA 1764
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFEATTCSLEeLLRTEQQRLEKNEDQLKIITMELQkksSELEEMTKFKNNKEvelEELKKI 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1765 ITDAAMMAEELKKEQDTSahlERMKKNMEQTVKDLQLRLDEAEQLALK--GGKKQIQKLEARVRELEGEVESEQKRNAE- 1841
Cdd:pfam05483 414 LAEDEKLLDEKKQFEKIA---EELKGKEQELIFLLQAREKEIHDLEIQltAIKTSEEHYLKEVEDLKTELEKEKLKNIEl 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1842 --------------------AVKGLRKHERRVKELTYQTEEDRKNILRLQD----LVDKLQAKVKSYKRQAEEAEEQSNT 1897
Cdd:pfam05483 491 tahcdklllenkeltqeasdMTLELKKHQEDIINCKKQEERMLKQIENLEEkemnLRDELESVREEFIQKGDEVKCKLDK 570
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 153791586 1898 NLAKFRKLQHELEEAEERADIAESQVNKLRvKSREVHTKVISE 1940
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLK-KQIENKNKNIEE 612
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
843-1092 |
6.56e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.28 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 843 KPLLKSAETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMvTLLKEKNDLQLQVQAEAEGLADAEER------------ 910
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE-KARQAEMDRQAAIYAEQERMAMERERelerirqeerkr 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 911 -CDQLIKTKIQLE-AKIKEV----TERAEDEEEINAEL-TAKKRKLEDECSELKKDIDDLELTLAKVEKEKhATENKVKN 983
Cdd:pfam17380 361 eLERIRQEEIAMEiSRMRELerlqMERQQKNERVRQELeAARKVKILEEERQRKIQQQKVEMEQIRAEQEE-ARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 984 LTEEMAGLDETIAKLTKEKKALQEAHQQtlddlQAEEDKVNTLTKAKIKLEQQVDD------LEGSLEQEKKLRMDLERA 1057
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQQQVERLRQ-----QEEERKRKKLELEKEKRDRKRAEeqrrkiLEKELEERKQAMIEEERK 514
|
250 260 270
....*....|....*....|....*....|....*
gi 153791586 1058 KRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFE 1092
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEME 549
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
849-1033 |
7.28e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 849 AETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQV-----------QAEAEGLADAEERCDQLIKT 917
Cdd:COG4942 58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrlgRQPPLALLLSPEDFLDAVRR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 918 KIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAK 997
Cdd:COG4942 138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
170 180 190
....*....|....*....|....*....|....*...
gi 153791586 998 LTKEKKALQEAHQQTLDDLQAEEDKVNT--LTKAKIKL 1033
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPAagFAALKGKL 255
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1683-1941 |
7.43e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1683 RANLLQAE--IEELRATLEQTERSRKIAE--QELLDASERVQ--LLHTQNTSLINTKKKLETDISQMQGEMEDILQEARN 1756
Cdd:TIGR02168 185 RENLDRLEdiLNELERQLKSLERQAEKAEryKELKAELRELElaLLVLRLEELREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1757 AEEKAkkaitdaammaEELKKEqdtsahlermKKNMEQTVKDLQLRLDEAEQLaLKGGKKQIQKLEARVRELEGEVESEQ 1836
Cdd:TIGR02168 265 LEEKL-----------EELRLE----------VSELEEEIEELQKELYALANE-ISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1837 KRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHE-------- 1908
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiaslnnei 402
|
250 260 270
....*....|....*....|....*....|....*....
gi 153791586 1909 ------LEEAEERADIAESQVNKLRVKSREVHTKVISEE 1941
Cdd:TIGR02168 403 erlearLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1044-1554 |
7.78e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1044 LEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQalgiqLQKKIKELQARIEE 1123
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-----LEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1124 LEeeieaerasraKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkreaefqkmRRDLEEATLQHEATAATLRKKHA 1203
Cdd:COG4717 151 LE-----------ERLEELRELEEELEELEAELAEL---------------------QEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1204 DSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKgNLEKMCRTLEdQLSELKSKEEEQQRLINDLTAQR 1283
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLL-IAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1284 GRLQTESGEFSrqldekeALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAEL 1363
Cdd:COG4717 277 GVLFLVLGLLA-------LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1364 QRALSKANTEVAQWrtkyetdaiqRTEELEEAKKKLAQRLQAAEEhvEAVNAKCASLEKtKQRLQNEVEDLMLDVERtna 1443
Cdd:COG4717 350 QELLREAEELEEEL----------QLEELEQEIAALLAEAGVEDE--EELRAALEQAEE-YQELKEELEELEEQLEE--- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1444 acAALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYE--ESLDQLETLKRENKNLQQEISDLTEQ 1521
Cdd:COG4717 414 --LLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEE 491
|
490 500 510
....*....|....*....|....*....|...
gi 153791586 1522 IAEGGKRIHELEKIKKQVEQEKceLQAALEEAE 1554
Cdd:COG4717 492 WAALKLALELLEEAREEYREER--LPPVLERAS 522
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
866-1092 |
8.72e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.06 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 866 KDELAKSEAKRKELEEkMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKI-------QLEAKIKEVTERAEDEEEI 938
Cdd:PLN02939 142 KNILLLNQARLQALED-LEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIhveileeQLEKLRNELLIRGATEGLC 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 939 NAELTAKKRKLEDECSELKKDIDDLELTLAKVEKekhaTENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQtLDDLQA 1018
Cdd:PLN02939 221 VHSLSKELDVLKEENMLLKDDIQFLKAELIEVAE----TEERVFKLEKERSLLDASLRELESKFIVAQEDVSK-LSPLQY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1019 EE--DKVNTLT-----------KAKIKLEQ------QVDDLEGSLEQE-----------------KKLRMDLERAKRKLE 1062
Cdd:PLN02939 296 DCwwEKVENLQdlldratnqveKAALVLDQnqdlrdKVDKLEASLKEAnvskfssykvellqqklKLLEERLQASDHEIH 375
|
250 260 270
....*....|....*....|....*....|
gi 153791586 1063 GDLKLAQESIMDIENEKQQLDEKLKKKEFE 1092
Cdd:PLN02939 376 SYIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
986-1760 |
9.06e-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: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 986 EEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEED---KVNTLTKAKIKLEQQVDDLEgsleqekklrmDLERAKRKLE 1062
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlnLVQTALRQQEKIERYQEDLE-----------ELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1063 GDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQarieeleeeieaerasRAKAEKQR 1142
Cdd:COG3096 368 EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALE----------------KARALCGL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1143 SDLSreLEEISERLEEAGGATSAQIEmnKKREAEfQKMRrDLEEATLQHEATAATLRK-------KHADSVA-ELGEQID 1214
Cdd:COG3096 432 PDLT--PENAEDYLAAFRAKEQQATE--EVLELE-QKLS-VADAARRQFEKAYELVCKiageverSQAWQTArELLRRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1215 NLQRVKQKLEkeksEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLindlTAQRGRLQTESGEFS 1294
Cdd:COG3096 506 SQQALAQRLQ----QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAEL----EAQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1295 RQLdekealvSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHalqssrhdcdlLREQYEEEQESKAELQRALSK-ANTE 1373
Cdd:COG3096 578 EQR-------SELRQQLEQLRARIKELAARAPAWLAAQDALER-----------LREQSGEALADSQEVTAAMQQlLERE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1374 VAQWRTKYEtdAIQRTEELEEAKKKLAQ-------RLQAAEEHVEAV------------NAKCAS--------------L 1420
Cdd:COG3096 640 REATVERDE--LAARKQALESQIERLSQpggaedpRLLALAERLGGVllseiyddvtleDAPYFSalygparhaivvpdL 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1421 EKTKQRLQNeVEDLMLDV------------------ERTNAACAALDKKQRNFDKI-------LAEWKQKCEETHAELEA 1475
Cdd:COG3096 718 SAVKEQLAG-LEDCPEDLyliegdpdsfddsvfdaeELEDAVVVKLSDRQWRYSRFpevplfgRAAREKRLEELRAERDE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1476 SQKEARSLGTELFKIKNAYEeSLDQLETLKRE---NKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEE 1552
Cdd:COG3096 797 LAEQYAKASFDVQKLQRLHQ-AFSQFVGGHLAvafAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQL 875
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1553 -----AEASLEHEEGKILRIQlelnQVKSEVDrkIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSrNDAIRLkkkmegD 1627
Cdd:COG3096 876 lnkllPQANLLADETLADRLE----ELREELD--AAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQ-FEQLQA------D 942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1628 LNEMEIQLNHAnRMAAEALR---------NYRNTQGILKDTQiHLDDALRSQ--------EDLKEQLAMVERRANLLQAE 1690
Cdd:COG3096 943 YLQAKEQQRRL-KQQIFALSevvqrrphfSYEDAVGLLGENS-DLNEKLRARleqaeearREAREQLRQAQAQYSQYNQV 1020
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1691 IEELRATLEQTERSRKIAEQELLD------------ASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAE 1758
Cdd:COG3096 1021 LASLKSSRDAKQQTLQELEQELEElgvqadaeaeerARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAE 1100
|
..
gi 153791586 1759 EK 1760
Cdd:COG3096 1101 RD 1102
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1078-1569 |
1.09e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1078 EKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIeaeraSRAKAEKQRSDLSRELEEISERLE 1157
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1158 EAggatsaqiemnKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDL 1237
Cdd:COG4717 150 EL-----------EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1238 ASNVETVSKAKGNLEKmcrtlEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEAL----------VSQL 1307
Cdd:COG4717 219 QEELEELEEELEQLEN-----ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1308 SRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTkyetdaiq 1387
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL-------- 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1388 rtEELEEAKKKLAQRLQAAEEhvEAVNAKCASLEKtkqrlqnevedlmldvertnaacaaldkkqrnfdkiLAEWKQKCE 1467
Cdd:COG4717 366 --EELEQEIAALLAEAGVEDE--EELRAALEQAEE------------------------------------YQELKEELE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1468 ETHAELEASQKEARSLGTELfkiknayeesldQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKC--E 1545
Cdd:COG4717 406 ELEEQLEELLGELEELLEAL------------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaE 473
|
490 500
....*....|....*....|....
gi 153791586 1546 LQAALEEAEASLEHEEGKILRIQL 1569
Cdd:COG4717 474 LLQELEELKAELRELAEEWAALKL 497
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1007-1168 |
1.19e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1007 EAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRM-------DLERAKRKLEGDLKLAQEsimDIENEK 1079
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEaakteleDLEKEIKRLELEIEEVEA---RIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1080 QQLDEKLKKKEFEisNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEA 1159
Cdd:COG1579 80 EQLGNVRNNKEYE--ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
....*....
gi 153791586 1160 GGATSAQIE 1168
Cdd:COG1579 158 LEELEAERE 166
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1257-1415 |
1.63e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1257 TLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAK--NA 1334
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1335 LAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVN 1414
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
.
gi 153791586 1415 A 1415
Cdd:COG1579 174 P 174
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1108-1430 |
1.94e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1108 IQLQKKIKELQARIEELEEEIEaerasRAKAEKQrsDLSRELEEiSERLEEAGGATSAQIEMNKKREAEFQK--MRRDLE 1185
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQE-----RLRQEKE--EKAREVER-RRKLEEAEKARQAEMDRQAAIYAEQERmaMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1186 EATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIddlasnvETVSKAKGNLEKMCRTLEDQLSEL 1265
Cdd:pfam17380 350 LERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQEL-------EAARKVKILEEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1266 ----KSKEEEQQRLINDLTAQRGRlqtesgEFSRQLDEKEALVSQLSRgkqaFTQQIEELKRQLEEEIKAKNALAHALQS 1341
Cdd:pfam17380 423 eqirAEQEEARQREVRRLEEERAR------EMERVRLEEQERQQQVER----LRQQEEERKRKKLELEKEKRDRKRAEEQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1342 SR----HDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKC 1417
Cdd:pfam17380 493 RRkileKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAME 572
|
330
....*....|...
gi 153791586 1418 ASLEKTKQRLQNE 1430
Cdd:pfam17380 573 REREMMRQIVESE 585
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1733-1932 |
2.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1733 KKKLETDISQMQGEMEDiLQEARNAEEKAKKAI---TDAAMMAEELKKEQDTSAHLERMKK-----NMEQTVKDLQLRLD 1804
Cdd:COG4913 220 EPDTFEAADALVEHFDD-LERAHEALEDAREQIellEPIRELAERYAAARERLAELEYLRAalrlwFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1805 EAEQlALKGGKKQIQKLEARVRELEGEVES-EQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKS 1883
Cdd:COG4913 299 ELRA-ELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 153791586 1884 YKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNK-LRVKSRE 1932
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRReLRELEAE 427
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1457-1893 |
2.24e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1457 KILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKR--ENKNLQQEISDLTEQIAEGGKRIHELEK 1534
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1535 IKKQVEqekcELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDaEIRSR 1614
Cdd:COG4717 154 RLEELR----ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE-ELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1615 NDAIRLKKKMEGDLNEMEIQLNHANRMAA---------EALRNYRNTQGILKDTQ----IHLDDALRSQEDLKEQLAMVE 1681
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLLLLIAAAllallglggSLLSLILTIAGVLFLVLgllaLLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1682 RRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQ-------------GEME 1748
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaallaeagvedeEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1749 DILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmKKNMEQTVKDLQLRLDEAEQlALKGGKKQIQKLEARVREL 1828
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALD--EEELEEELEELEEELEELEE-ELEELREELAELEAELEQL 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791586 1829 EGEVESEQKRnaeavkglRKHERRVKELTYQTEEDRKNILrLQDLVDKLQAKVKSYKRQA--EEAEE 1893
Cdd:COG4717 466 EEDGELAELL--------QELEELKAELRELAEEWAALKL-ALELLEEAREEYREERLPPvlERASE 523
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1487-1933 |
2.30e-05 |
|
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: 49.47 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1487 LFKIKNAYEEsLDQLETLKRE--NKNLQQEISDLtEQIAEGGKRIHELEKIKKQ----VEQEKCELQAALEEAEASLEhe 1560
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1561 EGKILRIQLELNQVKS---EVDRKIAEKDEEIDQLK------RNHIRIVESMQSTLDAEIRSRNDAI-RLKKKMEGDLNE 1630
Cdd:pfam06160 78 KYRFKKAKKALDEIEElldDIEEDIKQILEELDELLeseeknREEVEELKDKYRELRKTLLANRFSYgPAIDELEKQLAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1631 MEIQLNHANRMAAEAlrNYRNTQGILKDTQIHLDDAlrsQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQ 1710
Cdd:pfam06160 158 IEEEFSQFEELTESG--DYLEAREVLEKLEEETDAL---EELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALEH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1711 elLDASERVQLLHTQNTSLINTKKKLETDisQMQGEMEDI------LQEARNAEEKAKKaitdaammaeELKKEQDT-SA 1783
Cdd:pfam06160 233 --LNVDKEIQQLEEQLEENLALLENLELD--EAEEALEEIeeridqLYDLLEKEVDAKK----------YVEKNLPEiED 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1784 HLERMKKNMEQTVKDLQL-----RLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRN-------AEAVKGLRKHER 1851
Cdd:pfam06160 299 YLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYselqeelEEILEQLEEIEE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1852 RVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAE----------------EAEEQSNTNLAKFRKLQHELEEAEER 1915
Cdd:pfam06160 379 EQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEksnlpglpesyldyffDVSDEIEDLADELNEVPLNMDEVNRL 458
|
490
....*....|....*...
gi 153791586 1916 ADIAESQVNKLRVKSREV 1933
Cdd:pfam06160 459 LDEAQDDVDTLYEKTEEL 476
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1663-1941 |
2.40e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1663 LDDALRSQEDLKEQLAMVER-----RANLLQAEIEELRATLEQTERSRKIAEQELLDASERVqllhtqntslintkkkle 1737
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEADEVL------------------ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1738 TDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQLRLDEAEQLALkggkkQ 1817
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER---LEELEEERDDLLAEAGLDDADAEAVEA-----R 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1818 IQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNT 1897
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 153791586 1898 NLAKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 1941
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1457-1941 |
2.47e-05 |
|
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: 49.66 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1457 KILAEWKQKCEETHAELEASQKEARSLGtelfKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIK 1536
Cdd:TIGR00606 210 KYLKQYKEKACEIRDQITSKEAQLESSR----EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1537 KQVEQEKCELQAALEEAEASLEHEEG--------KILRIQLE----------LNQVKSEVDRKIAEKDEEIDQ-----LK 1593
Cdd:TIGR00606 286 SELELKMEKVFQGTDEQLNDLYHNHQrtvrekerELVDCQREleklnkerrlLNQEKTELLVEQGRLQLQADRhqehiRA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1594 RNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDL 1673
Cdd:TIGR00606 366 RDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELK 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1674 KEQLAMVERRANLLQAEIEELRAT----LEQTERSRKiAEQELLDASE---------RVQLLHTQNTSLINTKKKLETDI 1740
Cdd:TIGR00606 446 KEILEKKQEELKFVIKELQQLEGSsdriLELDQELRK-AERELSKAEKnsltetlkkEVKSLQNEKADLDRKLRKLDQEM 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1741 SQMQGEMEDILQEARNAEEKAKK-------------AITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAE 1807
Cdd:TIGR00606 525 EQLNHHTTTRTQMEMLTKDKMDKdeqirkiksrhsdELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1808 QLA------LKGGKKQIQKLEARVRE-------------LEGEVESEQKRNAEAVKGLRKHERRVKELTYQT-------E 1861
Cdd:TIGR00606 605 QNKnhinneLESKEEQLSSYEDKLFDvcgsqdeesdlerLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcQ 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1862 EDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 1941
Cdd:TIGR00606 685 RVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
940-1166 |
2.61e-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: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 940 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAE 1019
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1020 EDKVNTLTkakIKLE--------QQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlaqesimDIENEKQQLDEKLKKKEF 1091
Cdd:COG3883 99 GGSVSYLD---VLLGsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKA-------ELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791586 1092 EISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQ 1166
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1688-1915 |
2.69e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 49.35 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1688 QAEIEELRATLEQTERSRKiaEQELLDASERVQLLHTQNTSlintKKKLETDISQMQgEMEDILQEARNAEEKAKKAITD 1767
Cdd:pfam05557 1 RAELIESKARLSQLQNEKK--QMELEHKRARIELEKKASAL----KRQLDRESDRNQ-ELQKRIRLLEKREAEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1768 AAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRL-DEAEQLalkggKKQIQKLEARVRELEGEVESEQKRNAEAVKGL 1846
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSEL-----RRQIQRAELELQSTNSELEELQERLDLLKAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791586 1847 RKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVksykrQAEEAEEQSNTNLAKFRKLQHELEEAEER 1915
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQE-----QDSEIVKNSKSELARIPELEKELERLREH 212
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1017-1247 |
2.72e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1017 QAEEDKVNTLTKAKIKLEQQVDDLEGSLEQ-EKKlrmdLERAKRK-----LEGDLKLAQESIMDIENEKQQLDEKLKKKE 1090
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAA----LEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1091 FEISNLQSKIED---------EQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEagg 1161
Cdd:COG3206 240 ARLAALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA--- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1162 ATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRkkhadsvaELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNV 1241
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAELR--------RLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
....*.
gi 153791586 1242 ETVSKA 1247
Cdd:COG3206 389 RVIDPA 394
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1739-1932 |
2.85e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1739 DISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlALKGGKKQI 1818
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1819 QKLEARVRELEGEVESEQKRNAEAV----KGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQ 1894
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 153791586 1895 SNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSRE 1932
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
931-1077 |
3.13e-05 |
|
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: 48.13 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 931 RAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETI-AKLTKEKKALQEAH 1009
Cdd:cd22656 101 DDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALkDLLTDEGGAIARKE 180
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791586 1010 qqtLDDLQAEEDKVNT----LTKAKI-KLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIEN 1077
Cdd:cd22656 181 ---IKDLQKELEKLNEeyaaKLKAKIdELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEK 250
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1467-1753 |
3.14e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.99 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1467 EETHAELEASQKEARS-LGTELFKIKNAYEESL----DQLETLKRENKNLQQEISDLTEqiaeggkrihELEKIKKQVEQ 1541
Cdd:pfam00038 24 EQQNKLLETKISELRQkKGAEPSRLYSLYEKEIedlrRQLDTLTVERARLQLELDNLRL----------AAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1542 EkcelQAALEEAEASLeheegKILRIQL-ELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRN-DAIR 1619
Cdd:pfam00038 94 E----LNLRTSAENDL-----VGLRKDLdEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEmDAAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1620 lKKKMEGDLNEMEIQL-NHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQedlKEQLAMVERRANLLQAEIEELRATL 1698
Cdd:pfam00038 165 -KLDLTSALAEIRAQYeEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSA---KEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 153791586 1699 EQTERSrkIAEQElldasERVQLLHTQNTSLINtkkKLETDISQMQGEMEDILQE 1753
Cdd:pfam00038 241 ASLERQ--LAETE-----ERYELQLADYQELIS---ELEAELQETRQEMARQLRE 285
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1202-1408 |
3.41e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1202 HADS-VAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLT 1280
Cdd:COG3883 13 FADPqIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1281 A---QRGRLQT------ESGEFSRQLDeKEALVSQLSRGKQAFTQQIEELKRQLEEeikAKNALAHALQSsrhdcdlLRE 1351
Cdd:COG3883 93 RalyRSGGSVSyldvllGSESFSDFLD-RLSALSKIADADADLLEELKADKAELEA---KKAELEAKLAE-------LEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791586 1352 QYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEE 1408
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1547-1933 |
3.46e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.68 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1547 QAALEEAEASLEHEEGKILRIQLELNQ-VKSEvdrkiAEKDEEIDQLKRNHirivESMQSTLDAEIRSRNDAIrlkKKME 1625
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQElLESE-----EKNREEVEQLKDLY----RELRKSLLANRFSFGPAL---DELE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1626 GDLNEMEIQLNHANRMAAEAlrNYRNTQGILKDTQIHLDDAlrsQEDLKEQLAMVERRANLLQAEIEELRATLEQ-TERS 1704
Cdd:PRK04778 172 KQLENLEEEFSQFVELTESG--DYVEAREILDQLEEELAAL---EQIMEEIPELLKELQTELPDQLQELKAGYRElVEEG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1705 RKIAEQELLdasERVQLLHTQNTSLINTKKKLE--------TDISQMQGEMEDILQ---EARNAEEKAKKAITDAAMMAE 1773
Cdd:PRK04778 247 YHLDHLDIE---KEIQDLKEQIDENLALLEELDldeaeeknEEIQERIDQLYDILErevKARKYVEKNSDTLPDFLEHAK 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1774 ELKKEqdTSAHLERMKKNMEqtvkdlqlrLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRV 1853
Cdd:PRK04778 324 EQNKE--LKEEIDRVKQSYT---------LNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1854 KELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAE---EQSN------TNLAKFRKLQHELEEAEER--------- 1915
Cdd:PRK04778 393 EEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKrylEKSNlpglpeDYLEMFFEVSDEIEALAEEleekpinme 472
|
410 420
....*....|....*....|...
gi 153791586 1916 -----ADIAESQVNKLRVKSREV 1933
Cdd:PRK04778 473 avnrlLEEATEDVETLEEETEEL 495
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
967-1409 |
3.54e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.53 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 967 LAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEahqqTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQ 1046
Cdd:pfam05622 2 LSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQE----RLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1047 EKKLRMDLERAKRKLE---GDLKLAQESIMDIENEKQQL----------DEKLKKKEFEISNLQSKIEDeqaLGiQLQKK 1113
Cdd:pfam05622 78 LETARDDYRIKCEELEkevLELQHRNEELTSLAEEAQALkdemdilresSDKVKKLEATVETYKKKLED---LG-DLRRQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1114 IKELQARIEELEEEieaerasrakaekqrsdlSRELEEISERleeaGGATSAQIEMNKKREAEFQKMrrdLEEATLQHEA 1193
Cdd:pfam05622 154 VKLLEERNAEYMQR------------------TLQLEEELKK----ANALRGQLETYKRQVQELHGK---LSEESKKADK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1194 TAATLRKKHadsvaelgEQIDNLQRVKQKLEKEKSEMKMEIDDL---ASNVETVSKAKGNLEKMCRTLEDQLSELKSKE- 1269
Cdd:pfam05622 209 LEFEYKKLE--------EKLEALQKEKERLIIERDTLRETNEELrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPAEi 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1270 -EEQQRLIND----LTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAhalqSSRH 1344
Cdd:pfam05622 281 rEKLIRLQHEnkmlRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQG----SKAE 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791586 1345 DCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEH 1409
Cdd:pfam05622 357 DSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEDMKAMEER 421
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
860-1090 |
4.33e-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: 48.62 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 860 EEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEErCDQLIKTKIQLEAKIKEVTERAEDeeeIN 939
Cdd:pfam18971 610 DEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDE-IFALINKEANRDARAIAYTQNLKG---IK 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 940 AELTAKKRKLEDECSELKKDIDDLE----LTLAKVEKEKHATENKVKNLteemaGLD-ETIAKLTKEKKALQEAHQQTLD 1014
Cdd:pfam18971 686 RELSDKLEKISKDLKDFSKSFDEFKngknKDFSKAEETLKALKGSVKDL-----GINpEWISKVENLNAALNEFKNGKNK 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1015 DL----QAEEDKVNTLTKAKI--KLEQQVDDLEGSLEQEKKLrmdlerakrkleGDLKLAQESIMDIEN-EKQQLDEKLK 1087
Cdd:pfam18971 761 DFskvtQAKSDLENSVKDVIInqKVTDKVDNLNQAVSVAKAM------------GDFSRVEQVLADLKNfSKEQLAQQAQ 828
|
...
gi 153791586 1088 KKE 1090
Cdd:pfam18971 829 KNE 831
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1044-1868 |
4.68e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1044 LEQEKKLRMDLERAKRKLegdlKLAQESIMDIENEKQQLDEKLKKKEFEisnLQSKiEDEQAL---GIQLQKKIKELQAR 1120
Cdd:COG3096 284 SERALELRRELFGARRQL----AEEQYRLVEMARELEELSARESDLEQD---YQAA-SDHLNLvqtALRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1121 IEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGG--ATSAQ-IEMNKKREAEFQKMRRDLEEATLQHEA---T 1194
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSqlADYQQaLDVQQTRAIQYQQAVQALEKARALCGLpdlT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1195 AATLRKKHADSVAELGEQIDNLQRVKQKLE-----KEKSEMKME-IDDLASNVETVSKAKGNLEKMCR------------ 1256
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELEQKLSvadaaRRQFEKAYElVCKIAGEVERSQAWQTARELLRRyrsqqalaqrlq 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1257 TLEDQLSELKSKEEEQQRLIN-----------------DLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIE 1319
Cdd:COG3096 516 QLRAQLAELEQRLRQQQNAERlleefcqrigqqldaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1320 ELKRQLEEEIKAKNALAHalqssrhdcdlLREQYEEEQESKAELQRALSK-ANTEVAQWRTKYEtdAIQRTEELEEAKKK 1398
Cdd:COG3096 596 ELAARAPAWLAAQDALER-----------LREQSGEALADSQEVTAAMQQlLEREREATVERDE--LAARKQALESQIER 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1399 LAQ-------RLQAAEEHVEAV------------NAKCAS--------------LEKTKQRLQNeVEDLMLDV------- 1438
Cdd:COG3096 663 LSQpggaedpRLLALAERLGGVllseiyddvtleDAPYFSalygparhaivvpdLSAVKEQLAG-LEDCPEDLyliegdp 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1439 -----------ERTNAACAALDKKQRNFDKI-------LAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYeESLDQ 1500
Cdd:COG3096 742 dsfddsvfdaeELEDAVVVKLSDRQWRYSRFpevplfgRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLH-QAFSQ 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1501 LETLKRE---NKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEE-----AEASLEHEEGKILRIQleln 1572
Cdd:COG3096 821 FVGGHLAvafAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLlnkllPQANLLADETLADRLE---- 896
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1573 QVKSEVDrkIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSrNDAIRLkkkmegDLNEMEIQLNHAnRMAAEALrnyrnT 1652
Cdd:COG3096 897 ELREELD--AAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQ-FEQLQA------DYLQAKEQQRRL-KQQIFAL-----S 961
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1653 QGILKDTQIHLDDAlrsQEDLKEQLAMVERranllqaeieeLRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINT 1732
Cdd:COG3096 962 EVVQRRPHFSYEDA---VGLLGENSDLNEK-----------LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSS 1027
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1733 KKKLETDISQMQGEMEDI-LQEARNAEEKAKkaitdaammaeELKKEQDTSAHLERMKKNmeQTVKDLQLRLDEAEQLAl 1811
Cdd:COG3096 1028 RDAKQQTLQELEQELEELgVQADAEAEERAR-----------IRRDELHEELSQNRSRRS--QLEKQLTRCEAEMDSLQ- 1093
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791586 1812 kggkKQIQKLEARVRELEGEVESeQKRNAEAVKGLRKH---ERRV--KELTYQTEEDRKNIL 1868
Cdd:COG3096 1094 ----KRLRKAERDYKQEREQVVQ-AKAGWCAVLRLARDndvERRLhrRELAYLSADELRSMS 1150
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1455-1916 |
4.82e-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: 48.43 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1455 FDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEisdlTEQIAEGGKRIHELEK 1534
Cdd:TIGR00618 178 YTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ----TQQSHAYLTQKREAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1535 IKKQVEQEKCELQAALEEAEASL-EHEEG--------KILRIQLELNQVkSEVDRKIAEKDEEIDQLKRNHIRIVESMQS 1605
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRAQEaVLEETqerinrarKAAPLAAHIKAV-TQIEQQAQRIHTELQSKMRSRAKLLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1606 TLDAEiRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQI--HLDDALRSQEDLKEQLamverR 1683
Cdd:TIGR00618 333 HVKQQ-SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQktTLTQKLQSLCKELDIL-----Q 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1684 ANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLE-TDISQMQGEMEDILQEARNAEEKAK 1762
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHlQESAQSLKEREQQLQTKEQIHLQET 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1763 KAITDAAMMAEELKKEQdtsahLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNA-- 1840
Cdd:TIGR00618 487 RKKAVVLARLLELQEEP-----CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRAsl 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1841 -----EAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEER 1915
Cdd:TIGR00618 562 keqmqEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQEL 641
|
.
gi 153791586 1916 A 1916
Cdd:TIGR00618 642 A 642
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
923-1914 |
5.64e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 48.67 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 923 AKIKEVTERAEDEEEINAELTAK-KRKLEDECSELKKDID----DLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAK 997
Cdd:PTZ00440 410 SLSEHTLKAAEDVLKENSQKIADyALYSNLEIIEIKKKYDekinELKKSINQLKTLISIMKSFYDLIISEKDSMDSKEKK 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 998 LTKEKKALQ-------------EAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDlERAKRKLEGD 1064
Cdd:PTZ00440 490 ESSDSNYQEkvdellqiinsikEKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKD-EKLKRSMKND 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1065 LKlaqeSIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKElQARIEELEEEIEAERASRAKAEKQRSD 1144
Cdd:PTZ00440 569 IK----NKIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFIN-EKNDLQEKVKYILNKFYKGDLQELLDE 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1145 LSRELEEISERLEEAGGATSAQIEMNKKRE--AEFQKMRRDLEEATLQheataatLRKKHADSVAELGEQI--DNLQRVK 1220
Cdd:PTZ00440 644 LSHFLDDHKYLYHEAKSKEDLQTLLNTSKNeyEKLEFMKSDNIDNIIK-------NLKKELQNLLSLKENIikKQLNNIE 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1221 QKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEqqrliNDLTAQRGR-LQTESGEFSRQLDE 1299
Cdd:PTZ00440 717 QDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYE-----NDKDLPDGKnTYEEFLQYKDTILN 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1300 KEALVSQLsrgkqafTQQIEELKRQLEEEIKAKNALAHALQ--SSRHDCDL--LREQYEEEQE--SKAELQRALSKANTE 1373
Cdd:PTZ00440 792 KENKISND-------INILKENKKNNQDLLNSYNILIQKLEahTEKNDEELkqLLQKFPTEDEnlNLKELEKEFNENNQI 864
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1374 VaqwrtkyetDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACaalDKKQR 1453
Cdd:PTZ00440 865 V---------DNIIKDIENMNKNINIIKTLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINTDNIIQ---KNEKL 932
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1454 NFDKILAEWKQKCEEthaelEASQKEARSLGTELFKIKNAYEES-----------LDQLETLKRENKNLQQEISDLTEQI 1522
Cdd:PTZ00440 933 NLLNNLNKEKEKIEK-----QLSDTKINNLKMQIEKTLEYYDKSkeningndgthLEKLDKEKDEWEHFKSEIDKLNVNY 1007
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1523 AEGGKRIHELekIKKQVEqekcelqaaleeaeaslEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRI-VE 1601
Cdd:PTZ00440 1008 NILNKKIDDL--IKKQHD-----------------DIIELIDKLIKEKGKEIEEKVDQYISLLEKMKTKLSSFHFNIdIK 1068
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1602 SMQSTLdaeirSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVE 1681
Cdd:PTZ00440 1069 KYKNPK-----IKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKTL 1143
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1682 RRANllqaEIEELRATLEQTERSRKIAEQELLDasERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARN-AEEK 1760
Cdd:PTZ00440 1144 KELE----NMNLEDITLNEVNEIEIEYERILID--HIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERNDhLTTF 1217
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1761 AKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQlRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNA 1840
Cdd:PTZ00440 1218 EYNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELK-EIKLQVFSYLQQVIKENNKMENALHEIKNMYEFLISIDS 1296
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791586 1841 EAV-KGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEE--QSNTNLAKFRKLQHELEEAEE 1914
Cdd:PTZ00440 1297 EKIlKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAKEHKNKIYGSLEdkQIDDEIKKIEQIKEEISNKRK 1373
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1319-1828 |
5.83e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.41 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1319 EELKRQLEEEIKAKNALAHAlqssrhdcdllREQYEEEQESKAELQRALskantevaqwrtkyetdaiqrtEELEEAKKK 1398
Cdd:COG3096 278 NERRELSERALELRRELFGA-----------RRQLAEEQYRLVEMAREL----------------------EELSARESD 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1399 LAQRLQAAEEHVEAVNAKCASLEKTkQRLQNEVEDLMLDVERTNAACAALDKKQrnfdkilaewkqkcEETHAELEASQK 1478
Cdd:COG3096 325 LEQDYQAASDHLNLVQTALRQQEKI-ERYQEDLEELTERLEEQEEVVEEAAEQL--------------AEAEARLEAAEE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1479 EARSLGTELFKiknaYEESLDQLETlkrenKNLQQeisdlteqiaeggkrihelekikKQVEQEKCELQAALEEAEASLE 1558
Cdd:COG3096 390 EVDSLKSQLAD----YQQALDVQQT-----RAIQY-----------------------QQAVQALEKARALCGLPDLTPE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1559 HEEGKILRIQLELNQVKSEVdrkiaekdeeidqlkrnhiRIVESMQSTLDAEIRSRNDAIRLKKKMEGdlnemEIQLNHA 1638
Cdd:COG3096 438 NAEDYLAAFRAKEQQATEEV-------------------LELEQKLSVADAARRQFEKAYELVCKIAG-----EVERSQA 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1639 NRMAAEALRNYRNTQGILKDTQ---IHLDDA---LRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQEL 1712
Cdd:COG3096 494 WQTARELLRRYRSQQALAQRLQqlrAQLAELeqrLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1713 LDASERvqllhtqntsLINTKKKLEtDISQMQGEMEDILQEARNAEEKAKKAitdAAMMAEELKKEQDTSAHlermkknM 1792
Cdd:COG3096 574 AEAVEQ----------RSELRQQLE-QLRARIKELAARAPAWLAAQDALERL---REQSGEALADSQEVTAA-------M 632
|
490 500 510
....*....|....*....|....*....|....*.
gi 153791586 1793 EQTVKDLQLRLDEAEQLAlkggkKQIQKLEARVREL 1828
Cdd:COG3096 633 QQLLEREREATVERDELA-----ARKQALESQIERL 663
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1233-1376 |
6.08e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.27 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1233 EIDDLASNVETVSKAKGNLEKMCRTLEDQLS----ELKSKEEEQQRL---INDLTAQRGRLQTESGEFSRQLDEKEALVS 1305
Cdd:PRK09039 54 ALDRLNSQIAELADLLSLERQGNQDLQDSVAnlraSLSAAEAERSRLqalLAELAGAGAAAEGRAGELAQELDSEKQVSA 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1306 QLSRGKQAFTQQIEELKRQLeeeikakNALAHALQSSRhdcdllreqyEEEQESKAELQRALSKANTEVAQ 1376
Cdd:PRK09039 134 RALAQVELLNQQIAALRRQL-------AALEAALDASE----------KRDRESQAKIADLGRRLNVALAQ 187
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1350-1711 |
6.15e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 47.83 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1350 REQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQA-AEEHVEAVNAKCASLEKTKQRLQ 1428
Cdd:pfam09731 77 GESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEvLKEAISKAESATAVAKEAKDDAI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1429 NEVEDLMLDVERTNAACAALDKKQRNFDKILAE-WKQKCEETHAELEASQKE-ARSLGTELFKIKNAYEESLDQLETLKR 1506
Cdd:pfam09731 157 QAVKAHTDSLKEASDTAEISREKATDSALQKAEaLAEKLKEVINLAKQSEEEaAPPLLDAAPETPPKLPEHLDNVEEKVE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1507 ENKNLQQEISDLTEQIAEG-GKRIHELEKIKKQVEQEKCELQAAL-EEAEASLEHEEGKILRIQLELNQVKSEVDRK--- 1581
Cdd:pfam09731 237 KAQSLAKLVDQYKELVASErIVFQQELVSIFPDIIPVLKEDNLLSnDDLNSLIAHAHREIDQLSKKLAELKKREEKHier 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1582 -IAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIR--LKKKMEgdlNEMEIQLNHANRMAAEALRNYRNTQGILKD 1658
Cdd:pfam09731 317 aLEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREReeIRESYE---EKLRTELERQAEAHEEHLKDVLVEQEIELQ 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791586 1659 tqihlddaLRSQEDLKEQlamVERRANLLQAEIEELRATLEQTER---SRKIAEQE 1711
Cdd:pfam09731 394 --------REFLQDIKEK---VEEERAGRLLKLNELLANLKGLEKatsSHSEVEDE 438
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1642-1842 |
6.90e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1642 AAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERV-- 1719
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELge 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1720 QLLHTQNTSLINTK-------KKLETDISQMQGeMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNM 1792
Cdd:COG3883 91 RARALYRSGGSVSYldvllgsESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 153791586 1793 EQTVKDLQLRLDEAEQLaLKGGKKQIQKLEARVRELEGEVESEQKRNAEA 1842
Cdd:COG3883 167 EAAKAELEAQQAEQEAL-LAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1680-1924 |
9.32e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1680 VERRANLLQAEIEELRAtleqtersrkiAEQELLDASERVQLLhtqntslintkkkleTDISQMQGEMEDILQEARNAEE 1759
Cdd:COG4913 223 TFEAADALVEHFDDLER-----------AHEALEDAREQIELL---------------EPIRELAERYAAARERLAELEY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1760 -KAKKAITDAAMMAEELKKEQDtsaHLERMKKNMEQTVKDLQLRLDEAEQlALKGGKKQIQKLE-ARVRELEGEVESEQK 1837
Cdd:COG4913 277 lRAALRLWFAQRRLELLEAELE---ELRAELARLEAELERLEARLDALRE-ELDELEAQIRGNGgDRLEQLEREIERLER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1838 RNAEAVKGLRKHERRVKELTYQTEEDRKnilRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAE-ERA 1916
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEaEIA 429
|
....*...
gi 153791586 1917 DIAESQVN 1924
Cdd:COG4913 430 SLERRKSN 437
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1671-1916 |
9.39e-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: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1671 EDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQllhTQNTSLINTKKKLETDISQMQGEMEDI 1750
Cdd:pfam07888 16 EEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYK---RDREQWERQRRELESRVAELKEELRQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1751 LQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEqLALKGGKKQIQKLEARVRELEG 1830
Cdd:pfam07888 93 REKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE-TELERMKERAKKAGAQRKEEEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1831 EVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQsntnLAKFRKLQHELE 1910
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL----LEELRSLQERLN 247
|
....*.
gi 153791586 1911 EAEERA 1916
Cdd:pfam07888 248 ASERKV 253
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1354-1483 |
9.64e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1354 EEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqaaeehVEAVNAKCASLEKTKQRLQNEVED 1433
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK-------EENLDRKLELLEKREEELEKKEKE 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 153791586 1434 lmldvertnaacaaLDKKQRNFDKILAEWKQKCEETHAELEA----SQKEARSL 1483
Cdd:PRK12704 119 --------------LEQKQQELEKKEEELEELIEEQLQELERisglTAEEAKEI 158
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
849-981 |
9.90e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 849 AETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTL---LKEKNDLQLQVQAEAEgLADAEERCDQLIKTKIQLEAKI 925
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearIKKYEEQLGNVRNNKE-YEALQKEIESLKRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 926 KEVTERAEDEE----EINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV 981
Cdd:COG1579 113 LELMERIEELEeelaELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
882-1117 |
1.06e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.23 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 882 KMVTLLKEKNDL--QLQVqaeaEGLADAEERCDQLIKTKIQLEAKIKEVTERAED--EEEINAELTAKKRKLEDECSELK 957
Cdd:PRK05771 10 LIVTLKSYKDEVleALHE----LGVVHIEDLKEELSNERLRKLRSLLTKLSEALDklRSYLPKLNPLREEKKKVSVKSLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 958 KDIDDLELTLAKVEKEkhatenkVKNLTEEMAGLDETIAKLTKEKKALQ--EAHQQTLDDLQAEED---KVNTLTKAKIK 1032
Cdd:PRK05771 86 ELIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvFVGTVPEDKLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1033 LEQQVDDLEGSLE-QEKKLRM-----DLERAKRKLEGDLKLAQESIMDIENEKqQLDEKLKKKEFEISNLQSKIEDeqal 1106
Cdd:PRK05771 159 ELKLESDVENVEYiSTDKGYVyvvvvVLKELSDEVEEELKKLGFERLELEEEG-TPSELIREIKEELEEIEKERES---- 233
|
250
....*....|.
gi 153791586 1107 giqLQKKIKEL 1117
Cdd:PRK05771 234 ---LLEELKEL 241
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1390-1925 |
1.27e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 46.95 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1390 EELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKqrlqNEVEDLMLDVERtnaacAALDKKQRNFDKILAEWKQKCEET 1469
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTK----RLIEELKLNLER-----AQTEEAQAKQDSELAKLRVEEMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1470 HAELEASQkearSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKR----IHELEKIKKQVEQEKCE 1545
Cdd:pfam05701 113 GIADEASV----AAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRaeeaVSASKEIEKTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1546 LQAALEEAE----ASLEHEEGKIlRIQLELNQVKSEVDRKIAEKDEEIDQLkRNHIRIVESMQSTLDAeirsrndAIRLK 1621
Cdd:pfam05701 189 LIATKESLEsahaAHLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-------ASALL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1622 KKMEGDLNE-MEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELR---AT 1697
Cdd:pfam05701 260 LDLKAELAAyMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAASLRSELEKEKaelAS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1698 LEQTERSRKIAEQELLDASERVQllhtqntSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAitdaAMMA-EELK 1776
Cdd:pfam05701 340 LRQREGMASIAVSSLEAELNRTK-------SEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSL----AQAArEELR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1777 KEQD-----------TSAHLERMKKNMEQTvkdlqlrlDEAEQLALkggkkqiqkleARVRELEgevESEQKRNAEAVKG 1845
Cdd:pfam05701 409 KAKEeaeqakaaastVESRLEAVLKEIEAA--------KASEKLAL-----------AAIKALQ---ESESSAESTNQED 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1846 lrkherRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNK 1925
Cdd:pfam05701 467 ------SPRGVTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIALEKAEK 540
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1572-1769 |
1.39e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.14 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1572 NQVKSEVDRKI--AEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAI---------RLKKKMEGdLNEMEIQLNHAnr 1640
Cdd:NF012221 1563 DKERAEADRQRleQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAIleesravtkELTTLAQG-LDALDSQATYA-- 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1641 maAEALRNYRN--TQGILKDTQIHLDDA-LRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASE 1717
Cdd:NF012221 1640 --GESGDQWRNpfAGGLLDRVQEQLDDAkKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKA 1717
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791586 1718 RVQLLHTQNTSLINTKKKLETDIS------QMQGEmedilQEARNAEEKAKKAITDAA 1769
Cdd:NF012221 1718 DAEKRKDDALAKQNEAQQAESDANaaandaQSRGE-----QDASAAENKANQAQADAK 1770
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1292-1719 |
1.54e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1292 EFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEeIKAKNALAHALQSSRHD--CDLLREQYEEEQESKAELQR---A 1366
Cdd:COG3096 840 ALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQL-LNKLLPQANLLADETLAdrLEELREELDAAQEAQAFIQQhgkA 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1367 LSKANTEVaqwrtkyetDAIQRTEELEEAkkkLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDlmlDVERTNAACA 1446
Cdd:COG3096 919 LAQLEPLV---------AVLQSDPEQFEQ---LQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYE---DAVGLLGENS 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1447 ALDKKQRnfdKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGG 1526
Cdd:COG3096 984 DLNEKLR---ARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIR 1060
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1527 KRihELEKIKKQVEQEKCELQAALEEAEASLEHEEGKIlriqlelnqvkSEVDRKIAEKDEEIDQLKRNHIRIVEsmqst 1606
Cdd:COG3096 1061 RD--ELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRL-----------RKAERDYKQEREQVVQAKAGWCAVLR----- 1122
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1607 ldaeiRSRNDAirlkkkMEGDLNEMEIQLNHANR---MAAEALRNYRNTQGILKdtqiHLDDALRSQEDLKEQLAMV--- 1680
Cdd:COG3096 1123 -----LARDND------VERRLHRRELAYLSADElrsMSDKALGALRLAVADNE----HLRDALRLSEDPRRPERKVqfy 1187
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791586 1681 --------ER-----------RANLLQAEIEELRATLEQTERsrkiaEQELLDASERV 1719
Cdd:COG3096 1188 iavyqhlrERirqdiirtddpVEAIEQMEIELARLTEELTSR-----EQKLAISSESV 1240
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1496-1745 |
1.68e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1496 ESLDQLETLKRENKNLQQEISDLTEQIAEGGKrihELEKIKKQVEQEKCE---------LQAALEEAEASLEheegkilR 1566
Cdd:PRK11281 70 ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQA---ELEALKDDNDEETREtlstlslrqLESRLAQTLDQLQ-------N 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1567 IQLELNQVKSEVdrkIAEKdeeiDQLKRNHIRIVESMQSTLdaEIRSRNDAIRLKKKmegDLNEMEIQLNHANRMAAEAL 1646
Cdd:PRK11281 140 AQNDLAEYNSQL---VSLQ----TQPERAQAALYANSQRLQ--QIRNLLKGGKVGGK---ALRPSQRVLLQAEQALLNAQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1647 RNYR------NTQgilkdtqihLDDALRSQEDLK-EQLAMVERRANLLQAEIEELR-----ATLEQTERSRKIAE----- 1709
Cdd:PRK11281 208 NDLQrkslegNTQ---------LQDLLQKQRDYLtARIQRLEHQLQLLQEAINSKRltlseKTVQEAQSQDEAARiqanp 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791586 1710 -------------QELLDASERVQLLHTQN-------TSLINTKKKLETDISQMQG 1745
Cdd:PRK11281 279 lvaqeleinlqlsQRLLKATEKLNTLTQQNlrvknwlDRLTQSERNIKEQISVLKG 334
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1318-1584 |
2.00e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 46.54 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1318 IEELKRQLEEEIKAKNaLAHALQSSRHDCDLLREQYEEEQESKAELqraLSKANTEVAQWRTKYETDAIQRTEELEEAKK 1397
Cdd:NF033838 71 LSEIQKSLDKRKHTQN-VALNKKLSDIKTEYLYELNVLKEKSEAEL---TSKTKKELDAAFEQFKKDTLEPGKKVAEATK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1398 KLAQRLQAAEEHVEA---------------------VNAKCASLEKTKQRLQNEvedlmLDVERTNAACAALDKKQRN-- 1454
Cdd:NF033838 147 KVEEAEKKAKDQKEEdrrnyptntyktleleiaesdVEVKKAELELVKEEAKEP-----RDEEKIKQAKAKVESKKAEat 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1455 -FDKILAEWKQKCEETHAELEASQKEA---RSLGTELFKIKN-AYEESLDQLETLKRENKNLQQEISDLTEQ-------- 1521
Cdd:NF033838 222 rLEKIKTDREKAEEEAKRRADAKLKEAvekNVATSEQDKPKRrAKRGVLGEPATPDKKENDAKSSDSSVGEEtlpspslk 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1522 ----IAEGGKRIHELEK-IKKQVEQEK----------CELQAA-----LEEAEASLEHEEGKILRIQLELNQVKSEVDRK 1581
Cdd:NF033838 302 pekkVAEAEKKVEEAKKkAKDQKEEDRrnyptntyktLELEIAesdvkVKEAELELVKEEAKEPRNEEKIKQAKAKVESK 381
|
...
gi 153791586 1582 IAE 1584
Cdd:NF033838 382 KAE 384
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
839-1201 |
2.13e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 839 FFKIKPLLKSAE-----TEKEMATMKEEFQKIKdelaKSEAKRKELEEKMVTLLKEkndLQLQVQAEAEGLADAEErcdq 913
Cdd:PRK04778 100 FRKAKHEINEIEslldlIEEDIEQILEELQELL----ESEEKNREEVEQLKDLYRE---LRKSLLANRFSFGPALD---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 914 liktkiQLEAKIKEVTERAEDEEEINAE---LTAKK--RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN----L 984
Cdd:PRK04778 169 ------ELEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 985 TEEMAGLDETiaKLTKEKKALQEAHQQTLDDLQAEE-DKVNTLTKakiKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEG 1063
Cdd:PRK04778 243 VEEGYHLDHL--DIEKEIQDLKEQIDENLALLEELDlDEAEEKNE---EIQERIDQLYDILEREVKARKYVEKNSDTLPD 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1064 DLKLAQESIMDIENEKQQLDEKlkkkeFEISnlqskiEDEQALGIQLQKKIKELQARIEELEEEIeaerasrAKAEKQRS 1143
Cdd:PRK04778 318 FLEHAKEQNKELKEEIDRVKQS-----YTLN------ESELESVRQLEKQLESLEKQYDEITERI-------AEQEIAYS 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791586 1144 DLSRELEEISERLEEAggatsaqiemnKKREAEFQKMRRDLEEATLQHEATAATLRKK 1201
Cdd:PRK04778 380 ELQEELEEILKQLEEI-----------EKEQEKLSEMLQGLRKDELEAREKLERYRNK 426
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1258-1453 |
2.63e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1258 LEDQLSELKSKEEEQQRLINDLTAQRG--RLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNAL 1335
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1336 AHALQSSRhdcdlLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNA 1415
Cdd:COG3206 260 LQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA 334
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 153791586 1416 KCASLEKTKQRL---QNEVEDLMLDVERTNAACAALDKKQR 1453
Cdd:COG3206 335 QLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLE 375
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1671-1937 |
2.64e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1671 EDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKiaeqELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDI 1750
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1751 LQEARNAEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQtvkdlqlrldeaeqlalkgGKKQIQKLEARVRELEG 1830
Cdd:PRK03918 272 KKEIEELEEKVKEL--------KELKEKAEEYIKLSEFYEEYLD-------------------ELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1831 EVEseqkrnaEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQaKVKSYKRQAEEAEEQSNTNlaKFRKLQHELE 1910
Cdd:PRK03918 325 GIE-------ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGL--TPEKLEKELE 394
|
250 260
....*....|....*....|....*..
gi 153791586 1911 EAEERADIAESQVNKLRVKSREVHTKV 1937
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEI 421
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
895-1019 |
2.78e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 895 LQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEI---NAELTAKKRKLEDECSELKKDIDDLELTLAKVE 971
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELrerRNELQKLEKRLLQKEENLDRKLELLEKREEELE 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791586 972 KEKHATENKVKNLTEEMAGLD----------ETIAKLTKEkkalqEAHQQTLDDLQAE 1019
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEelieeqlqelERISGLTAE-----EAKEILLEKVEEE 166
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
867-1116 |
2.99e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 867 DELAKSeaKRKELEEKMVTLLKEKNDLQLQVQAE-----------AEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDE 935
Cdd:PHA02562 169 DKLNKD--KIRELNQQIQTLDMKIDHIQQQIKTYnknieeqrkknGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 936 EEINAELTAKKRKLEDECSELKKDIDdlelTLAKVEK--EKHATenkVKNLTEEMAGLDETIAKLTKEKKALqeahQQTL 1013
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIE----QFQKVIKmyEKGGV---CPTCTQQISEGPDRITKIKDKLKEL----QHSL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1014 DDLQaeedkvntltKAKIKLEQQVDDLegsLEQEKKLRmDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEI 1093
Cdd:PHA02562 316 EKLD----------TAIDELEEIMDEF---NEQSKKLL-ELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEEL 381
|
250 260
....*....|....*....|...
gi 153791586 1094 SNLQskiEDEQALGIQLQKKIKE 1116
Cdd:PHA02562 382 AKLQ---DELDKIVKTKSELVKE 401
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
841-1062 |
3.09e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 841 KIKPLLKSAETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQ 920
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 921 LEAKIKEVTERAEDEEEInAELTAKKRKLEDECSELKKDIDDleltLAKVEKEKhatENKVKNLTEEMAGLDETIAKLTK 1000
Cdd:PRK02224 577 LNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREA----LAELNDER---RERLAEKRERKRELEAEFDEARI 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791586 1001 EKkaLQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLE 1062
Cdd:PRK02224 649 EE--AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVE 708
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1455-1627 |
3.11e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1455 FDKILAEWKQKCEETHAE--LEASQKEARSLGTElfKIKNAYEESLDQLETLKRENKnlqqeisdlteqiaeggKRIHEL 1532
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKriLEEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELR-----------------ERRNEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1533 EKIKKQVEQEKCEL---QAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKD---EEIDQLKRNHIR--IVESMQ 1604
Cdd:PRK12704 85 QKLEKRLLQKEENLdrkLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLqelERISGLTAEEAKeiLLEKVE 164
|
170 180
....*....|....*....|...
gi 153791586 1605 STLDAEIRSRNDAIRLKKKMEGD 1627
Cdd:PRK12704 165 EEARHEAAVLIKEIEEEAKEEAD 187
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
859-1082 |
3.42e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.91 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 859 KEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEG--------LADAEERCDQLIKTKIQLEAKIKEVTE 930
Cdd:pfam00038 3 KEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRlyslyekeIEDLRRQLDTLTVERARLQLELDNLRL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 931 RAEDEEEINAELTAKKRKLEDECSELKKDIDdlELTLAKVEkekhaTENKVKNLTEEMAGL----DETIAKLT------- 999
Cdd:pfam00038 83 AAEDFRQKYEDELNLRTSAENDLVGLRKDLD--EATLARVD-----LEAKIESLKEELAFLkknhEEEVRELQaqvsdtq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1000 -----------------------------KEKKALQEAHQQTLDDLQAEEDKVN-TLTKAKIKLEQ---QVDDLEGSLEQ 1046
Cdd:pfam00038 156 vnvemdaarkldltsalaeiraqyeeiaaKNREEAEEWYQSKLEELQQAAARNGdALRSAKEEITElrrTIQSLEIELQS 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 153791586 1047 EKKLRMDLERAKRKLE----GDLKLAQESIMDIENEKQQL 1082
Cdd:pfam00038 236 LKKQKASLERQLAETEeryeLQLADYQELISELEAELQET 275
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
849-1036 |
3.71e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 849 AETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKE-----KNDLQLQVQAEAEGLADAEERCDQLikTKIqlea 923
Cdd:COG3883 54 NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAlyrsgGSVSYLDVLLGSESFSDFLDRLSAL--SKI---- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 924 kikevterAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKK 1003
Cdd:COG3883 128 --------ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
170 180 190
....*....|....*....|....*....|...
gi 153791586 1004 ALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQ 1036
Cdd:COG3883 200 ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1080-1242 |
3.90e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1080 QQLDEKLKKKEFEISNLQSKIEDeqalgiqLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEA 1159
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1160 GG-----ATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEI 1234
Cdd:COG1579 86 RNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*...
gi 153791586 1235 DDLASNVE 1242
Cdd:COG1579 166 EELAAKIP 173
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1259-1453 |
4.22e-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: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1259 EDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHA 1338
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1339 LQSSRHDCDLLrEQYEEEQE-----SKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAV 1413
Cdd:COG3883 95 LYRSGGSVSYL-DVLLGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 153791586 1414 NAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQR 1453
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
849-974 |
4.23e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.39 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 849 AETEKEMATMKEEFQKIKDELAKSEAKRKELEekmvtLLKEKNDLQLQVQAEAEGLADAEERCdqliktkIQLEAKIKEV 928
Cdd:PTZ00491 672 AELLEQEARGRLERQKMHDKAKAEEQRTKLLE-----LQAESAAVESSGQSRAEALAEAEARL-------IEAEAEVEQA 739
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 153791586 929 TERAEDEE-EINAELTAKKRKLEDECsELKKDIDDLELT----LAKVEKEK 974
Cdd:PTZ00491 740 ELRAKALRiEAEAELEKLRKRQELEL-EYEQAQNELEIAkakeLADIEATK 789
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1357-1540 |
4.37e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1357 QESKAELQRALSKANTEVAQWRTKYE-TDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLM 1435
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGlVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1436 ldverTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLD-QLETLKRENKNLQQE 1514
Cdd:COG3206 261 -----QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEaELEALQAREASLQAQ 335
|
170 180
....*....|....*....|....*.
gi 153791586 1515 ISDLTEQIAEGGKRIHELEKIKKQVE 1540
Cdd:COG3206 336 LAQLEARLAELPELEAELRRLEREVE 361
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1313-1765 |
4.39e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1313 AFTQQIEELKRQLEEEIKAKNALAHAlqssrhdcdllREQYEEEQESKAELQRALskantevaqwrtkyetdaiqrtEEL 1392
Cdd:PRK04863 273 DYMRHANERRVHLEEALELRRELYTS-----------RRQLAAEQYRLVEMAREL----------------------AEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1393 EEAKKKLAQRLQAAEEHVEAVNAKCASLEKTkQRLQNEVEDLMLDVERTNAACAALDKKQrnfdkilaewkqkcEETHAE 1472
Cdd:PRK04863 320 NEAESDLEQDYQAASDHLNLVQTALRQQEKI-ERYQADLEELEERLEEQNEVVEEADEQQ--------------EENEAR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1473 LEASQKEARSLGTELFKiknaYEESLDQLETLKRENKNLQQ---------EISDLTEQIAEGgkRIHELEKIKKQVEQEK 1543
Cdd:PRK04863 385 AEAAEEEVDELKSQLAD----YQQALDVQQTRAIQYQQAVQalerakqlcGLPDLTADNAED--WLEEFQAKEQEATEEL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1544 CELQAALEEAEASLE-HEEGKILriqleLNQVKSEVDRKIAEkdeeidqlkrnhirivESMQSTLDAEIRSRNDAIRLKK 1622
Cdd:PRK04863 459 LSLEQKLSVAQAAHSqFEQAYQL-----VRKIAGEVSRSEAW----------------DVARELLRRLREQRHLAEQLQQ 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1623 kMEGDLNEMEIQLNH---ANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRAtle 1699
Cdd:PRK04863 518 -LRMRLSELEQRLRQqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA--- 593
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791586 1700 QTERSRKIAeQELLDASERVQLLHTQNTSLINTKKKLETDISQMQgEMEDILQEARNAEEKAKKAI 1765
Cdd:PRK04863 594 RIQRLAARA-PAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLL-ERERELTVERDELAARKQAL 657
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1785-1910 |
4.90e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1785 LERMKK-NMEQTVKDLQLRLDEAEQL------ALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVkglrkheRRVKELT 1857
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEAErsrlqaLLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 153791586 1858 YQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAkfRKLQhELE 1910
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALA--QRVQ-ELN 193
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
849-1156 |
4.91e-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: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 849 AETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV 928
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 929 TERAE-------DEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAkltkE 1001
Cdd:pfam07888 156 KERAKkagaqrkEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEA----E 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1002 KKALQEAHQQTLDDLQAEEDKVNTLTKakikleqqvdDLEGSLEQEKKLRMDLERAKRKL-EGDLKLAQESIMDIENEKQ 1080
Cdd:pfam07888 232 NEALLEELRSLQERLNASERKVEGLGE----------ELSSMAAQRDRTQAELHQARLQAaQLTLQLADASLALREGRAR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1081 QLDEKlkkkefeiSNLQSKIEDE----QALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERL 1156
Cdd:pfam07888 302 WAQER--------ETLQQSAEADkdriEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASL 373
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1089-1326 |
5.14e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1089 KEFEISNLQSKIEDEQALGIQLQKKIKELQARIeeleeeieaerasrAKAEKQRSDLSRELEEISerLEEAGGATSAQIe 1168
Cdd:COG3206 159 EAYLEQNLELRREEARKALEFLEEQLPELRKEL--------------EEAEAALEEFRQKNGLVD--LSEEAKLLLQQL- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1169 mnkkreAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNlqRVKQKLEKEKSEMKMEIDDLAsnvetvSKAK 1248
Cdd:COG3206 222 ------SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELS------ARYT 287
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791586 1249 GNLEKMcRTLEDQLSELKSK-EEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRgKQaftQQIEELKRQLE 1326
Cdd:COG3206 288 PNHPDV-IALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE-LE---AELRRLEREVE 361
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1733-1920 |
5.19e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1733 KKKLETDISQMQGEMEDILQEARN-AEEKAKKAITDAAMMAEELKKEQDtsahlermkknmeqtvKDLQLRldeaeqlal 1811
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKeAEAIKKEALLEAKEEIHKLRNEFE----------------KELRER--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1812 kggKKQIQKLEARVRELEGEVESEQKRnaeavkgLRKHERRVkeltyqtEEDRKNILRLQDLVDKLQAKVKS-YKRQAEE 1890
Cdd:PRK12704 81 ---RNELQKLEKRLLQKEENLDRKLEL-------LEKREEEL-------EKKEKELEQKQQELEKKEEELEElIEEQLQE 143
|
170 180 190
....*....|....*....|....*....|
gi 153791586 1891 AEEQSNTNLAKFRKLQHELEEAEERADIAE 1920
Cdd:PRK12704 144 LERISGLTAEEAKEILLEKVEEEARHEAAV 173
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1472-1927 |
5.36e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.12 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1472 ELEASQKEARSLGTELFKIKNAYEESLDQLEtlkRENKNLQQEISDLTEQIAEggkrihELEKIKKQVEQEKCELQAALE 1551
Cdd:pfam05557 62 KREAEAEEALREQAELNRLKKKYLEALNKKL---NEKESQLADAREVISCLKN------ELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1552 EAEASLEHEEGKILRIQlELNQVKSEVDRKIAEKDEEIDQLKrnhirivesmqsTLDAEIRSRNDAIRLKKKMEGDL--- 1628
Cdd:pfam05557 133 ELEELQERLDLLKAKAS-EAEQLRQNLEKQQSSLAEAEQRIK------------ELEFEIQSQEQDSEIVKNSKSELari 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1629 NEMEIQLNHAnRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIA 1708
Cdd:pfam05557 200 PELEKELERL-REHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1709 EqellDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKakkaITDAAMMAEELK------------ 1776
Cdd:pfam05557 279 E----DLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK----IEDLNKKLKRHKalvrrlqrrvll 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1777 --KEQD-TSAHLERMKK--NMEQTVKDLQLRLDEAEQLALKGgKKQIQKLEARVRELEGEVESEQKRNA--EAVKGLRKH 1849
Cdd:pfam05557 351 ltKERDgYRAILESYDKelTMSNYSPQLLERIEEAEDMTQKM-QAHNEEMEAQLSVAEEELGGYKQQAQtlERELQALRQ 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1850 ERRVKELTYQTEED---RKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKL 1926
Cdd:pfam05557 430 QESLADPSYSKEEVdslRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKL 509
|
.
gi 153791586 1927 R 1927
Cdd:pfam05557 510 Q 510
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1265-1890 |
5.44e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.18 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1265 LKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKE-------------ALVSQLSRGKQ---AFTQQIEELKRQLE-- 1326
Cdd:PRK10246 320 LQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDrfrqwnnelagwrAQFSQQTSDREqlrQWQQQLTHAEQKLNal 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1327 ---------EEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQwrtkyetdaiqRTEELEEAKk 1397
Cdd:PRK10246 400 paitltltaDEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQ-----------RNAALNEMR- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1398 klaQRLQAAEEHVEAVNAKC------ASLEKTKQRLQNevedlmldvertnaacaaldkkqrnfdkilaewKQKC----E 1467
Cdd:PRK10246 468 ---QRYKEKTQQLADVKTICeqeariKDLEAQRAQLQA---------------------------------GQPCplcgS 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1468 ETHAELEASQkearslgtelfkiknAYEESLDQletlkRENKNLQQEISDLTEqiaEGGKRIHELEKIKKQVEQEKCELQ 1547
Cdd:PRK10246 512 TSHPAVEAYQ---------------ALEPGVNQ-----SRLDALEKEVKKLGE---EGAALRGQLDALTKQLQRDESEAQ 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1548 AALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEE--IDQLKRNHirivesmqsTLDAEIrsrNDAIRLKKKME 1625
Cdd:PRK10246 569 SLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHErqLRLLSQRH---------ELQGQI---AAHNQQIIQYQ 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1626 GDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQihlDDALRSQEDLKEQLAmverranlLQAEIEELRATLEQTERSR 1705
Cdd:PRK10246 637 QQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQ---QEAQSWQQRQNELTA--------LQNRIQQLTPLLETLPQSD 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1706 KIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQE---ARNAEEKAKKAITDAAMMAEElkkeqdTS 1782
Cdd:PRK10246 706 DLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQfdtALQASVFDDQQAFLAALLDEE------TL 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1783 AHLERMKKNMEQtvkdlqlRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAV--KGLRKHERRVKELTYQT 1860
Cdd:PRK10246 780 TQLEQLKQNLEN-------QRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQlaQQLRENTTRQGEIRQQL 852
|
650 660 670
....*....|....*....|....*....|
gi 153791586 1861 EEDRKNILRLQDLVdklqAKVKSYKRQAEE 1890
Cdd:PRK10246 853 KQDADNRQQQQALM----QQIAQATQQVED 878
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1759-1931 |
5.52e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1759 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLalkggkKQIQKLEARVRELEGEVESEQKR 1838
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1839 naeaVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQA-EEAEEQSNTNLAKFRKLQHELEEAEERAD 1917
Cdd:COG4717 148 ----LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....
gi 153791586 1918 IAESQVNKLRVKSR 1931
Cdd:COG4717 224 ELEEELEQLENELE 237
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1656-1898 |
5.57e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1656 LKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLhtqntslintKKK 1735
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER----------REE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1736 LETDISQMQ-----GEMEDILQEARNAEEkakkAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLA 1810
Cdd:COG3883 88 LGERARALYrsggsVSYLDVLLGSESFSD----FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1811 lkggkkqiQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEE 1890
Cdd:COG3883 164 --------AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
....*...
gi 153791586 1891 AEEQSNTN 1898
Cdd:COG3883 236 AAAAAAAA 243
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1473-1702 |
6.41e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1473 LEASQKEARS----LGTELFKIKNAYEESLDQLETLKRENK--NLQQEISDLTEQIAEggkriheLEKIKKQVEQEKCEL 1546
Cdd:COG3206 166 LELRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE-------LESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1547 QAALEEAEASLEHEEGKI--LRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVEsmqstLDAEIRSrndairLKKKM 1624
Cdd:COG3206 239 EARLAALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA-----LRAQIAA------LRAQL 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791586 1625 EGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRsqedlkeQLAMVERRANLLQAEIEELRATLEQTE 1702
Cdd:COG3206 308 QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEA-------ELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1226-1584 |
6.55e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1226 EKSEMKMEIDDLASNVETVskakgnlekmcRTLEDQLSELKSKeeeqqrlINDLTAQRGRlqtesgefsrqldekealvs 1305
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKV-----------RFLEQQNKLLETK-------ISELRQKKGA-------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1306 QLSRGKQAFTQQIEELKRQLEeeikaknalahalqssrhdcDLLREqyeeeqesKAELQRALSKANTEVAQWRTKYETDA 1385
Cdd:pfam00038 44 EPSRLYSLYEKEIEDLRRQLD--------------------TLTVE--------RARLQLELDNLRLAAEDFRQKYEDEL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1386 IQRTeELEEAKKKLAQRLQAA-------EEHVEAVNAKCASLEKTKQR----LQNEVEDLMLDVERTNAACAALdkkqrn 1454
Cdd:pfam00038 96 NLRT-SAENDLVGLRKDLDEAtlarvdlEAKIESLKEELAFLKKNHEEevreLQAQVSDTQVNVEMDAARKLDL------ 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1455 fDKILAEWKQKCEEtHAELeaSQKEARslgtELFKIKnaYEESLDQLETLKRENKNLQQEISDLTEQIAEggkRIHELEK 1534
Cdd:pfam00038 169 -TSALAEIRAQYEE-IAAK--NREEAE----EWYQSK--LEELQQAAARNGDALRSAKEEITELRRTIQS---LEIELQS 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 153791586 1535 IKKQveqeKCELQAALEEAEASLEHE----EGKILRIQLELNQVKSEVDRKIAE 1584
Cdd:pfam00038 236 LKKQ----KASLERQLAETEERYELQladyQELISELEAELQETRQEMARQLRE 285
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
954-1280 |
6.62e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 954 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKL 1033
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1034 EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKK 1113
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1114 IKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEA 1193
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1194 TAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQ 1273
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
....*..
gi 153791586 1274 RLINDLT 1280
Cdd:COG4372 347 LVGLLDN 353
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1491-1941 |
6.65e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.51 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1491 KNAYEESLDQLETLKRENKNLQQEISDLTEQIAEggkRIHELEKIKKQVEQEKcelqaaLEEAEASLEHEEGKILRIQLE 1570
Cdd:COG5278 85 RAEIDELLAELRSLTADNPEQQARLDELEALIDQ---WLAELEQVIALRRAGG------LEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1571 LNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYR 1650
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1651 NTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLI 1730
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1731 NTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLA 1810
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1811 LKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEE 1890
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1891 AEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 1941
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1628-1927 |
6.92e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1628 LNEMEIQLnHANRMAAEALRNYRNTQGILK-------------------DTQIHLDDALRSQEDL---KEQLAMVERRAN 1685
Cdd:PRK04863 232 FQDMEAAL-RENRMTLEAIRVTQSDRDLFKhlitestnyvaadymrhanERRVHLEEALELRRELytsRRQLAAEQYRLV 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1686 LLQAEIEELratleqtERSRKIAEQELLDASERVQLLhtqNTSLINTKKkletdISQMQGEMEDI---LQEARNAEEKAK 1762
Cdd:PRK04863 311 EMARELAEL-------NEAESDLEQDYQAASDHLNLV---QTALRQQEK-----IERYQADLEELeerLEEQNEVVEEAD 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1763 KAITDAAMMAEELKKEQDtsahleRMKKNM--------EQTVKDLQLR-----LDEAEQ------LALKGGKKQIQKLEA 1823
Cdd:PRK04863 376 EQQEENEARAEAAEEEVD------ELKSQLadyqqaldVQQTRAIQYQqavqaLERAKQlcglpdLTADNAEDWLEEFQA 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1824 RVRELEGEV-ESEQK-RNAEAVKglRKHE------RRV-------------KELTYQTEEDRKNILRLQDLVDKLQA--- 1879
Cdd:PRK04863 450 KEQEATEELlSLEQKlSVAQAAH--SQFEqayqlvRKIagevsrseawdvaRELLRRLREQRHLAEQLQQLRMRLSEleq 527
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1880 ---KVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLR 1927
Cdd:PRK04863 528 rlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1241-1328 |
7.48e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 42.23 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1241 VETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQ--- 1317
Cdd:pfam08614 66 LAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQlnm 145
|
90
....*....|.
gi 153791586 1318 IEELKRQLEEE 1328
Cdd:pfam08614 146 AEEKLRKLEKE 156
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
859-1465 |
7.88e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.66 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 859 KEEFQKIKDELAKSEAKRKELEEKMVTLLKE----KNDLQLQVQAEAEGLADAEERCDQLIKTK--IQLEAKIKEVTERA 932
Cdd:TIGR01612 1103 KEENIKYADEINKIKDDIKNLDQKIDHHIKAleeiKKKSENYIDEIKAQINDLEDVADKAISNDdpEEIEKKIENIVTKI 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 933 EDEEEINAELtakkRKLEDECSELKKDIDDLE---------------LTLAKVEKEKHATENKVKNLTEEMAGLDEtiak 997
Cdd:TIGR01612 1183 DKKKNIYDEI----KKLLNEIAEIEKDKTSLEevkginlsygknlgkLFLEKIDEEKKKSEHMIKAMEAYIEDLDE---- 1254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 998 lTKEKKALQEAHQQTLDDLQAEEDKVNtLTKAKIK---LEQQVDDLEGSLEQEKKLRM--------DLERAKRKLEGDLK 1066
Cdd:TIGR01612 1255 -IKEKSPEIENEMGIEMDIKAEMETFN-ISHDDDKdhhIISKKHDENISDIREKSLKIiedfseesDINDIKKELQKNLL 1332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1067 LAQESIMDI-------------------------------------ENEKQQLD--EKLKKKEFEISNLQ---SKIE--- 1101
Cdd:TIGR01612 1333 DAQKHNSDInlylneianiynilklnkikkiidevkeytkeieennKNIKDELDksEKLIKKIKDDINLEeckSKIEstl 1412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1102 DEQALGiQLQKKIKELQARIEELEEEIEAERAS--------------------------RAKAEKQRSDLSRELEEISER 1155
Cdd:TIGR01612 1413 DDKDID-ECIKKIKELKNHILSEESNIDTYFKNadennenvlllfkniemadnksqhilKIKKDNATNDHDFNINELKEH 1491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1156 LEEAGG------ATSAQIEMNKKReaeFQKMRRDLEEatLQHEATAATLRKKHADSVAELGEQIDNLQRVKQK--LEKEK 1227
Cdd:TIGR01612 1492 IDKSKGckdeadKNAKAIEKNKEL---FEQYKKDVTE--LLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKfiLEAEK 1566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1228 SEMKME--------IDDLASNVETVSKAKGNLEKMCRTLEDQL---SELKSKeeeqqrlINDLTAQRGRLQTESGEFSrq 1296
Cdd:TIGR01612 1567 SEQKIKeikkekfrIEDDAAKNDKSNKAAIDIQLSLENFENKFlkiSDIKKK-------INDCLKETESIEKKISSFS-- 1637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1297 LDEKEALVSQLSRGK---QAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYE---------------EEQE 1358
Cdd:TIGR01612 1638 IDSQDTELKENGDNLnslQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEigiiekikeiaiankEEIE 1717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1359 S-----KAELQRALSKANTEvaqwrtkyETDAIQRTEELEEAKKKLAqrlQAAEEHVEAVNAKCASLE------------ 1421
Cdd:TIGR01612 1718 SikeliEPTIENLISSFNTN--------DLEGIDPNEKLEEYNTEIG---DIYEEFIELYNIIAGCLEtvskepitydei 1786
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 153791586 1422 -KTKQRLQNEvedLMLDVERTNAACAALDK-KQRNFDKILAEWKQK 1465
Cdd:TIGR01612 1787 kNTRINAQNE---FLKIIEIEKKSKSYLDDiEAKEFDRIINHFKKK 1829
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1264-1850 |
8.18e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.68 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1264 ELKSKEEEQQRLINDLTAQRGRLQTESGEFSRqldEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSsr 1343
Cdd:COG5022 811 EYRSYLACIIKLQKTIKREKKLRETEEVEFSL---KAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQ-- 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1344 hdcdllreQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAvnakcaSLEKT 1423
Cdd:COG5022 886 --------ELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGP------SIEYV 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1424 KQRLQNEVedlmldvertNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLgTELFKIKNAYEESLDQLET 1503
Cdd:COG5022 952 KLPELNKL----------HEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL-AELSKQYGALQESTKQLKE 1020
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1504 LKRENKNLQQEISDLTEQIAEGgKRIHELEKIKKQVEQEKCELQAALEEAeaSLEHEEGKILRIQLELNQVKSEVDRKIA 1583
Cdd:COG5022 1021 LPVEVAELQSASKIISSESTEL-SILKPLQKLKGLLLLENNQLQARYKAL--KLRRENSLLDDKQLYQLESTENLLKTIN 1097
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1584 EKDEEIdqLKRNHIRIVESMQSTLDAEIRSRndairLKKKMEGDLN------EMEIQLNHANRMAAEALRNYRNTQGILk 1657
Cdd:COG5022 1098 VKDLEV--TNRNLVKPANVLQFIVAQMIKLN-----LLQEISKFLSqlvntlEPVFQKLSVLQLELDGLFWEANLEALP- 1169
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1658 dtqiHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRA---TLEQTERSRKIAEQELLDASERVQLLHTQNTSL----- 1729
Cdd:COG5022 1170 ----SPPPFAALSEKRLYQSALYDEKSKLSSSEVNDLKNeliALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLkgfnn 1245
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1730 -----INTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITD-----------------AAMMAEELKKEQDTSAHLER 1787
Cdd:COG5022 1246 lnkkfDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSllqyinvglfnalrtkaSSLRWKSATEVNYNSEELDD 1325
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1788 MKKNME------------QTVKDLQLRLDEAEQLALKGGKK------QIQKLEARVRELEGEVESEQKRNAEAVKGLRKH 1849
Cdd:COG5022 1326 WCREFEisdvdeeleeliQAVKVLQLLKDDLNKLDELLDACyslnpaEIQNLKSRYDPADKENNLPKEILKKIEALLIKQ 1405
|
.
gi 153791586 1850 E 1850
Cdd:COG5022 1406 E 1406
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1198-1413 |
8.28e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1198 LRKKHADSvAELGEQIDNLQRVKQKLEKEKSE-MKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLI 1276
Cdd:PRK05771 45 LRKLRSLL-TKLSEALDKLRSYLPKLNPLREEkKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1277 NDLTaqrgRLQTESGEFSRQLDEK--EALVSQLSRGKQAFTQQIEElKRQLEEEIKAKN-----ALAHALQSSRHDCDLL 1349
Cdd:PRK05771 124 ERLE----PWGNFDLDLSLLLGFKyvSVFVGTVPEDKLEELKLESD-VENVEYISTDKGyvyvvVVVLKELSDEVEEELK 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791586 1350 REQYEEEQ-ESKAELQRALSKANTEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQAAEEHVEAV 1413
Cdd:PRK05771 199 KLGFERLElEEEGTPSELIREIKEELEEIEKERE----SLLEELKELAKKYLEELLALYEYLEIE 259
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
908-1049 |
8.30e-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: 43.85 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 908 EERCDQLIKTKIQLEAKIKEVTEraeDEEEINAELTakkrkledECSELKKDIDDLELTL-AKVEKEKHATENKVKNLTE 986
Cdd:smart00787 136 EWRMKLLEGLKEGLDENLEGLKE---DYKLLMKELE--------LLNSIKPKLRDRKDALeEELRQLKQLEDELEDCDPT 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791586 987 EMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKK 1049
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1668-1932 |
8.63e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1668 RSQEDLKEQLAMVERRANL------LQAEIEELRATLEQTERSRKIAEQELldasERVQLLHTQNTSLINTKKKLETDIS 1741
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLeeaekaRQAEMDRQAAIYAEQERMAMEREREL----ERIRQEERKRELERIRQEEIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1742 QMQgEMEDILQEARNAEEKAKKAItDAAMMAEELKKEqdtsahleRMKKNMEQTVKDLQLRLDEAEqlalkGGKKQIQKL 1821
Cdd:pfam17380 376 RMR-ELERLQMERQQKNERVRQEL-EAARKVKILEEE--------RQRKIQQQKVEMEQIRAEQEE-----ARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1822 EA-RVRELEGEVESEQKRNAEaVKGLRKHE--RRVKELTYQ--------TEEDRKNILRlQDLVDKLQAKVKSYK----- 1885
Cdd:pfam17380 441 EEeRAREMERVRLEEQERQQQ-VERLRQQEeeRKRKKLELEkekrdrkrAEEQRRKILE-KELEERKQAMIEEERkrkll 518
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791586 1886 ------RQAEEAEEQSNTNLAKFRKLQHELEE---AEERADIAESQVNKLRVKSRE 1932
Cdd:pfam17380 519 ekemeeRQKAIYEEERRREAEEERRKQQEMEErrrIQEQMRKATEERSRLEAMERE 574
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1662-1835 |
9.57e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1662 HLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKkkletDIS 1741
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1742 QMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNMEQTVKDLQLRLDEAEqlalkggkKQIQKL 1821
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELE---AELAELEAELEEKKAELDEELAELE--------AELEEL 161
|
170
....*....|....
gi 153791586 1822 EARVRELEGEVESE 1835
Cdd:COG1579 162 EAEREELAAKIPPE 175
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
867-1071 |
1.03e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 867 DELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKK 946
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 947 RKLEDECSELK-----KDIDDLeltLAKVEKEKHATENKvknlTEEMAGLDETIAKLTKEKKALQEAhQQTLDDLQAE-E 1020
Cdd:COG3883 96 YRSGGSVSYLDvllgsESFSDF---LDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAK-LAELEALKAElE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1021 DKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQES 1071
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1673-1941 |
1.07e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1673 LKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKklETDISQMQGEMEDILQ 1752
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQ--ERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1753 EARNAEEKAkkaitdaaMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQiQKLEARVRELEgEV 1832
Cdd:pfam17380 356 EERKRELER--------IRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQ-RKIQQQKVEME-QI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1833 ESEQKrNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEa 1912
Cdd:pfam17380 426 RAEQE-EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE- 503
|
250 260
....*....|....*....|....*....
gi 153791586 1913 EERADIAESQVNKLRVKSREVHTKVISEE 1941
Cdd:pfam17380 504 RKQAMIEEERKRKLLEKEMEERQKAIYEE 532
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
966-1196 |
1.10e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 966 TLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDdlegslE 1045
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE------E 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1046 QEKKLRMDLERAKRKLEGDLKLAQ--------------ESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQAlgiQLQ 1111
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLA---ELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1112 KKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQH 1191
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
....*
gi 153791586 1192 EATAA 1196
Cdd:COG3883 241 AAAAS 245
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
935-1327 |
1.17e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 935 EEEINAEL-TAKKRKL-EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQT 1012
Cdd:PRK11281 38 EADVQAQLdALNKQKLlEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1013 LDDLQAEEdkvntltkakikLEQQVDDLEGSLEQEKK-----------LRMDLERAKRKLEGDLKLAQEsimdIENekqQ 1081
Cdd:PRK11281 118 LSTLSLRQ------------LESRLAQTLDQLQNAQNdlaeynsqlvsLQTQPERAQAALYANSQRLQQ----IRN---L 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1082 LDEKLKKKEFEISNLQSKIEDEQA-LGIQLQKKIKELQARIEELEEeieaerasrakAEKQRSdlsrELEEISERLEEAg 1160
Cdd:PRK11281 179 LKGGKVGGKALRPSQRVLLQAEQAlLNAQNDLQRKSLEGNTQLQDL-----------LQKQRD----YLTARIQRLEHQ- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1161 gATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQI------------DNLqRVKQKLEkeks 1228
Cdd:PRK11281 243 -LQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLlkateklntltqQNL-RVKNWLD---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1229 emkmeiddlasnvetvskakgNLEKMCRTLEDQLSELK-----SKEEEQQR-------LINDLTAQRGRLQTESGEFSRQ 1296
Cdd:PRK11281 317 ---------------------RLTQSERNIKEQISVLKgslllSRILYQQQqalpsadLIEGLADRIADLRLEQFEINQQ 375
|
410 420 430
....*....|....*....|....*....|....*
gi 153791586 1297 LDE---KEALVSQLSRG-KQAFTqqiEELKRQLEE 1327
Cdd:PRK11281 376 RDAlfqPDAYIDKLEAGhKSEVT---DEVRDALLQ 407
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1352-1556 |
1.17e-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: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1352 QYEEEQESKAELQRALSKANTEVAQWRTKYEtdaiqrteELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEV 1431
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE--------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1432 EDLMLDVERTNAA-------------------CAALDKKQRNFDKILAEWKQkceeTHAELEASQKEARSLGTELFKIKN 1492
Cdd:COG3883 89 GERARALYRSGGSvsyldvllgsesfsdfldrLSALSKIADADADLLEELKA----DKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791586 1493 AYEESLDQLETLKRENknlQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEAS 1556
Cdd:COG3883 165 ELEAAKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1486-1879 |
1.22e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1486 ELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEqEKCELQAALEEAEASLEheegkil 1565
Cdd:PRK04863 301 QLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA-DLEELEERLEEQNEVVE------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1566 riqlELNQVKSEVDRKIAEKDEEIDQLKRNhiriVESMQSTLDAEIR---SRNDAIRLKKKMEGDLNEMEIQLNHANRMA 1642
Cdd:PRK04863 373 ----EADEQQEENEARAEAAEEEVDELKSQ----LADYQQALDVQQTraiQYQQAVQALERAKQLCGLPDLTADNAEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1643 AEalrnYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDasERVQLL 1722
Cdd:PRK04863 445 EE----FQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLA--EQLQQL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1723 HTQntslintkkkletdisqmQGEMEDILQEARNAEEKAKKAitdaammAEELKKEQDTSAHLERMKKNMEQTVKDLQLR 1802
Cdd:PRK04863 519 RMR------------------LSELEQRLRQQQRAERLLAEF-------CKRLGKNLDDEDELEQLQEELEARLESLSES 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1803 LDEAEQLALkGGKKQIQKLEARVRELE----------------GEVESEQKRNAEAVKGLRK-HERRVKELTYQTEEDRK 1865
Cdd:PRK04863 574 VSEARERRM-ALRQQLEQLQARIQRLAarapawlaaqdalarlREQSGEEFEDSQDVTEYMQqLLERERELTVERDELAA 652
|
410
....*....|....
gi 153791586 1866 NILRLQDLVDKLQA 1879
Cdd:PRK04863 653 RKQALDEEIERLSQ 666
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1317-1557 |
1.30e-03 |
|
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: 42.78 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1317 QIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQEskaELQRALSKANTEVAQwrtkyETDAIQRTEELEEAK 1396
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQK---KATQTLAKAQQVNAE-----SERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1397 KKLAQRLQAAEEHVEAVNAKCASL-EKTKQRLQNEVEDLMLDVERTNaacaaLDKKQRNFDKILAEWKQKCEETHAELEA 1475
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALpSSDLSRMLAEAQRMLGEIRSRD-----FGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1476 SQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTeqiAEGGKRIHELEKIKKQVEQEKCELQAALEEAEA 1555
Cdd:pfam06008 167 PQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLN---LANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
..
gi 153791586 1556 SL 1557
Cdd:pfam06008 244 SL 245
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1346-1554 |
1.45e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1346 CDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQ 1425
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1426 RLQNEVEDLM----LDV--------ERTNAACAALDKkqRNFDKILAEWKQKCEE--------------THAELEASQ-K 1478
Cdd:PRK05771 118 ELEQEIERLEpwgnFDLdlslllgfKYVSVFVGTVPE--DKLEELKLESDVENVEyistdkgyvyvvvvVLKELSDEVeE 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791586 1479 EARSLGTELFKIKnaYEESLDQ-LETLKRENKNLQQEISDLTEQIAEGGKRIHELEK-IKKQVEQEKCELQAALEEAE 1554
Cdd:PRK05771 196 ELKKLGFERLELE--EEGTPSElIREIKEELEEIEKERESLLEELKELAKKYLEELLaLYEYLEIELERAEALSKFLK 271
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1612-1929 |
1.60e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.77 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1612 RSRNDAI-RLKKKMEGDL------NEMEIQLNHANRMAAEAlrnYRNTQGILKdTQIHLDDALRSQEDLKEQLAMVERra 1684
Cdd:PLN03188 915 QTREDKIiRLESLMDGVLskedflEEELASLMHEHKLLKEK---YENHPEVLR-TKIELKRVQDELEHYRNFYDMGER-- 988
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1685 NLLQAEIEELRATLEQTERSrkiaeqELLDASERVQLLHTQNTSLINTKKKLETdISQMQGEM--EDILQEARNAEEKAK 1762
Cdd:PLN03188 989 EVLLEEIQDLRSQLQYYIDS------SLPSARKRNSLLKLTYSCEPSQAPPLNT-IPESTDESpeKKLEQERLRWTEAES 1061
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1763 KAITdaamMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQK----------LEARVRELEGEV 1832
Cdd:PLN03188 1062 KWIS----LAEELRTELDASRALAEKQKHELDTEKRCAEELKEAMQMAMEGHARMLEQyadleekhiqLLARHRRIQEGI 1137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1833 ESEQKRNAEA-VKGLR--------------KHERRvKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRqAEEAEEQSNT 1897
Cdd:PLN03188 1138 DDVKKAAARAgVRGAEskfinalaaeisalKVERE-KERRYLRDENKSLQAQLRDTAEAVQAAGELLVR-LKEAEEALTV 1215
|
330 340 350
....*....|....*....|....*....|..
gi 153791586 1898 nlakfrkLQHELEEAEERADIAESQVNKLRVK 1929
Cdd:PLN03188 1216 -------AQKRAMDAEQEAAEAYKQIDKLKRK 1240
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
849-1179 |
1.79e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 849 AETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV 928
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 929 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKalqea 1008
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA----- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1009 hQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKK 1088
Cdd:COG4372 182 -EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1089 KEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIE 1168
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
330
....*....|.
gi 153791586 1169 MNKKREAEFQK 1179
Cdd:COG4372 341 DLLQLLLVGLL 351
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1176-1838 |
1.85e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1176 EFQKMRRDLEEATLQHEATAATLRKKHaDSVAELGEQIDNlQRVKQKLEKEKSEMKMEIDDLASNVetvskakGNLEKMc 1255
Cdd:pfam10174 131 ELFLLRKTLEEMELRIETQKQTLGARD-ESIKKLLEMLQS-KGLPKKSGEEDWERTRRIAEAEMQL-------GHLEVL- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1256 rtLEDQLSELKSKEEEQQRlindltaqRGRLQTESGE---FSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAK 1332
Cdd:pfam10174 201 --LDQKEKENIHLREELHR--------RNQLQPDPAKtkaLQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1333 NALAHALQSSRHDCDLLREQYEEeqeskaeLQRALSKANTEVAQWRTKYETDAIQRTEeleeakkklaqrlqaAEEHVEA 1412
Cdd:pfam10174 271 EEEIKQMEVYKSHSKFMKNKIDQ-------LKQELSKKESELLALQTKLETLTNQNSD---------------CKQHIEV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1413 VNAKCASLEKTKQRLQNEVEDLMLDVERTNAAcaaLDKKQRnfdkilaewkqkceethaELEASQKEARSLGTELFKIKn 1492
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEVDALRLRLEEKESF---LNKKTK------------------QLQDLTEEKSTLAGEIRDLK- 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1493 ayeeslDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIqleln 1572
Cdd:pfam10174 387 ------DMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERL----- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1573 qvKSEVDRKIAEKDEEIDQLKRNhIRIVESMQSTLDAEIRSRNDAIRlkkkmegDLNEmeiqlnHANRMAAEALRNYRNT 1652
Cdd:pfam10174 456 --KEQREREDRERLEELESLKKE-NKDLKEKVSALQPELTEKESSLI-------DLKE------HASSLASSGLKKDSKL 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1653 QGILKDTQIHLDDALRSQEDLK--EQLAMVERranlLQAEIEELRATLEQtERSRKIAEQelldaservqllhtqntsli 1730
Cdd:pfam10174 520 KSLEIAVEQKKEECSKLENQLKkaHNAEEAVR----TNPEINDRIRLLEQ-EVARYKEES-------------------- 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1731 ntkkkletdiSQMQGEME---DILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ--TVKDLQLRLDE 1805
Cdd:pfam10174 575 ----------GKAQAEVErllGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKkkGAQLLEEARRR 644
|
650 660 670
....*....|....*....|....*....|...
gi 153791586 1806 AEQLALKGGKKQIQKLEARVRELEGEVESEQKR 1838
Cdd:pfam10174 645 EDNLADNSQQLQLEELMGALEKTRQELDATKAR 677
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
970-1281 |
1.85e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 970 VEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKK 1049
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1050 LRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQarIEELEEEIE 1129
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ--EELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1130 AERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAEL 1209
Cdd:COG4372 173 LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791586 1210 GEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTA 1281
Cdd:COG4372 253 EEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1553-1783 |
1.93e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1553 AEASLEHEEGKILRIQLELNQVKSEVDrkiaEKDEEIDQLKRNHIRIVESMQsTLDAEIrsrndairlkKKMEGDLNEME 1632
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELE-ALQAEI----------DKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1633 IQLNHANRMAAEALRNYRNTQGILKDTqihldDALRSQEDLKEQLamveRRANLLQAEIEELRATLEQTERSRKIAEQEL 1712
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYL-----DVLLGSESFSDFL----DRLSALSKIADADADLLEELKADKAELEAKK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1713 LDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSA 1783
Cdd:COG3883 150 AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
877-1229 |
1.94e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 877 KELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSEL 956
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 957 KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQ 1036
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1037 VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKE 1116
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1117 LQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1196
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350
....*....|....*....|....*....|...
gi 153791586 1197 TLRKKHADSVAELGEQIDNLQRVKQKLEKEKSE 1229
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
838-1395 |
2.03e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 838 LFFKIKPLLKSAETEKEMATMKEEFQKIKDELAKSEakRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAE---ERCDQL 914
Cdd:COG5185 45 LFFPLGISRDSLRVTLRSVINVLDGLNYQNDVKKSE--SSVKARKFLKEKKLDTKILQEYVNSLIKLPNYEwsaDILISL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 915 IKTKIQLEAKIKevteRAEDEEEINAELTAKKRKLEDECSELKKDIddleltlakveKEKHATENKVKNLTEEMAGLDET 994
Cdd:COG5185 123 LYLYKSEIVALK----DELIKVEKLDEIADIEASYGEVETGIIKDI-----------FGKLTQELNQNLKKLEIFGLTLG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 995 I-AKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIK---------------------LEQQVDDLEGSLEQEKKLRM 1052
Cdd:COG5185 188 LlKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKeiinieealkgfqdpeseledLAQTSDKLEKLVEQNTDLRL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1053 DLERAKRKLEGDLK-LAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQ--------LQKKIKELQARIEE 1123
Cdd:COG5185 268 EKLGENAESSKRLNeNANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQeleeskreTETGIQNLTAEIEQ 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1124 LEEEIEA------ERASRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkreaefqkmRRDLEEATLQHEATAAT 1197
Cdd:COG5185 348 GQESLTEnleaikEEIENIVGEVELSKSSEELDSFKDTIEST---------------------KESLDEIPQNQRGYAQE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1198 LRKKHADSVAELGEQIDNLQRvkqklekeksemkmEIDDLASNVETVSKAKGNLEKmcrtlEDQLSELKSKEEEQQRLIN 1277
Cdd:COG5185 407 ILATLEDTLKAADRQIEELQR--------------QIEQATSSNEEVSKLLNELIS-----ELNKVMREADEESQSRLEE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1278 DLTAQRGRLQTESGEFSRQLdekEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQ 1357
Cdd:COG5185 468 AYDEINRSVRSKKEDLNEEL---TQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENL 544
|
570 580 590
....*....|....*....|....*....|....*....
gi 153791586 1358 ESKAELQRALSKANTE-VAQWRTKYETDAIQRTEELEEA 1395
Cdd:COG5185 545 IPASELIQASNAKTDGqAANLRTAVIDELTQYLSTIESQ 583
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1682-1920 |
2.04e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1682 RRANLLQAEIEELratLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDIlqearnaEEKA 1761
Cdd:COG1842 5 RLSDIIRANINAL---LDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW-------EEKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1762 KKAitdaammaeeLKKEQDTSAH--LERmKKNMEQTVKDLQLRLDEAEQLALKGgKKQIQKLEARVRELEGEVES--EQK 1837
Cdd:COG1842 75 RLA----------LEKGREDLAReaLER-KAELEAQAEALEAQLAQLEEQVEKL-KEALRQLESKLEELKAKKDTlkARA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1838 RNAEAVKGLRKHERRVkeltyQTEEDRKNILRLQDLVDKLQAKVKSYkrqAEEAEEQSntnlakfrkLQHELEEAEERAD 1917
Cdd:COG1842 143 KAAKAQEKVNEALSGI-----DSDDATSALERMEEKIEEMEARAEAA---AELAAGDS---------LDDELAELEADSE 205
|
...
gi 153791586 1918 IAE 1920
Cdd:COG1842 206 VED 208
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1424-1780 |
2.20e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1424 KQRLQNEVEDLMLDVERTNAACAALDKKQRNFDK---ILAEWKQKCEETHAELEASQKEARslgtelfkiknayeesldq 1500
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEER------------------- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1501 letlKRENKNLQQEisdlteQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEgkilriqlelnqvksEVDR 1580
Cdd:pfam17380 359 ----KRELERIRQE------EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEE---------------ERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1581 KIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKkkmegdlnEMEIQlnhanrMAAEALRNYRNTQgilKDTQ 1660
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE--------EQERQ------QQVERLRQQEEER---KRKK 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1661 IHLDDALRSQEDLKEQlamverRANLLQAEIEELRATLEQTERSRKIAEQELLDaservqllhTQNTSLINTKKKLETDI 1740
Cdd:pfam17380 477 LELEKEKRDRKRAEEQ------RRKILEKELEERKQAMIEEERKRKLLEKEMEE---------RQKAIYEEERRREAEEE 541
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 153791586 1741 SQMQGEMEdilqEARNAEEKAKKAITDAAMMaEELKKEQD 1780
Cdd:pfam17380 542 RRKQQEME----ERRRIQEQMRKATEERSRL-EAMERERE 576
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1456-1769 |
2.35e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1456 DKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKI 1535
Cdd:PLN02939 113 NEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1536 KKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEvdrKIAEKDeEIDQLKRNHIRIVESMQSTLDAEirsrn 1615
Cdd:PLN02939 193 KIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEE---NMLLKD-DIQFLKAELIEVAETEERVFKLE----- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1616 daiRLKKKMEGDLNEMEIQLNHANrmaAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELR 1695
Cdd:PLN02939 264 ---KERSLLDASLRELESKFIVAQ---EDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1696 ATLEQTERSR------KIAEQELLDASERVQLLHTQntslINTKKKLETDISQmqgEMEDILQEARnaEEKAKKAITDAA 1769
Cdd:PLN02939 338 ASLKEANVSKfssykvELLQQKLKLLEERLQASDHE----IHSYIQLYQESIK---EFQDTLSKLK--EESKKRSLEHPA 408
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1211-1309 |
2.41e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1211 EQIDNLQRVKQKLEKEKSEMKMEIDDlasnvetVSKAK-GNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTE 1289
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDE-------ASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQR 483
|
90 100
....*....|....*....|...
gi 153791586 1290 SG---EFSRQLDEKEALVSQLSR 1309
Cdd:COG0542 484 YGkipELEKELAELEEELAELAP 506
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1440-1584 |
2.52e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1440 RTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEarslgtELFKIKNAYE-ESLDQLETLKRENKNLQQEISDL 1518
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKE------EIHKLRNEFEkELRERRNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791586 1519 TEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRI---------QLELNQVKSEVDRKIAE 1584
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaeeakEILLEKVEEEARHEAAV 173
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1110-1861 |
2.55e-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: 42.89 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1110 LQKKIKELQARIEE-LEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKM-------- 1180
Cdd:pfam10174 1 LQAQLRDLQRENELlRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQHLqltiqalq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1181 -----RRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKG----NL 1251
Cdd:pfam10174 81 delraQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGardeSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1252 EKMCRTLEDQLSELKSKEEEQQRlindlTAQRGRLQTESGEFSRQLDEKE----ALVSQLSRGKQAftQQIEELKRQLEE 1327
Cdd:pfam10174 161 KKLLEMLQSKGLPKKSGEEDWER-----TRRIAEAEMQLGHLEVLLDQKEkeniHLREELHRRNQL--QPDPAKTKALQT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1328 EIKAKNA-----------LAHALQSSRHDCDLLREQYEEE--------QESK------AELQRALSKANTEVAQWRTKYE 1382
Cdd:pfam10174 234 VIEMKDTkisslernirdLEDEVQMLKTNGLLHTEDREEEikqmevykSHSKfmknkiDQLKQELSKKESELLALQTKLE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1383 TDAIQRTEeleeakkklaqrlqaAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNaacAALDKKQRnfdkilaew 1462
Cdd:pfam10174 314 TLTNQNSD---------------CKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKE---SFLNKKTK--------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1463 kqkceethaELEASQKEARSLGTELFKIKnayeeslDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQE 1542
Cdd:pfam10174 367 ---------QLQDLTEEKSTLAGEIRDLK-------DMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTD 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1543 KCELQAALEEAEASLEHEEGKILRIqlelnqvKSEVDRKIAEKDEEIDQLKRN-----------HIRIVESMQSTLDAEI 1611
Cdd:pfam10174 431 SSNTDTALTTLEEALSEKERIIERL-------KEQREREDRERLEELESLKKEnkdlkekvsalQPELTEKESSLIDLKE 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1612 RSRNDAIRLKKKmEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEdLKEQLAMVERRANLLQAEI 1691
Cdd:pfam10174 504 HASSLASSGLKK-DSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRL-LEQEVARYKEESGKAQAEV 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1692 EELRATLEQTE-----RSRKIAEQElldaSERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAIT 1766
Cdd:pfam10174 582 ERLLGILREVEnekndKDKKIAELE----SLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQL 657
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1767 DAAMMA-EELKKEQD-TSAHLERMKKNMEQTVKDL-QLRLDEAEQLALKGGKKQiQKLEARVRELEGEV------ESEQK 1837
Cdd:pfam10174 658 EELMGAlEKTRQELDaTKARLSSTQQSLAEKDGHLtNLRAERRKQLEEILEMKQ-EALLAAISEKDANIallelsSSKKK 736
|
810 820
....*....|....*....|....*
gi 153791586 1838 RNAEAVKGL-RKHERRVKELTYQTE 1861
Cdd:pfam10174 737 KTQEEVMALkREKDRLVHQLKQQTQ 761
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
844-1008 |
2.55e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 844 PLLKSAETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEA 923
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 924 KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLE---LT----LAKVEKEKHATENKVKNLTEEMAGLDETIA 996
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvnLLaieeYEELEERYDFLSEQREDLEEARETLEEAIE 819
|
170
....*....|...
gi 153791586 997 KLTKEKK-ALQEA 1008
Cdd:COG1196 820 EIDRETReRFLET 832
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
987-1158 |
2.63e-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: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 987 EMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAK--RKLEGD 1064
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1065 LKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQAlgiQLQKKIKELQARieeleeeieaerasRAKAEKQRSD 1144
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEE--------------LAELEAELEE 160
|
170
....*....|....
gi 153791586 1145 LSRELEEISERLEE 1158
Cdd:COG1579 161 LEAEREELAAKIPP 174
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
904-1182 |
2.77e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 904 LADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN 983
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 984 LTEEMAGLDETIAKLTKEKKALQEAHQQtLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRmDLERAKRKLEG 1063
Cdd:COG1340 90 LREELDELRKELAELNKAGGSIDKLRKE-IERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKAL-EKNEKLKELRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1064 DLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRS 1143
Cdd:COG1340 168 ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
250 260 270
....*....|....*....|....*....|....*....
gi 153791586 1144 DLSRELEEISERLEEAggatsaqiEMNKKREAEFQKMRR 1182
Cdd:COG1340 248 KLRKKQRALKREKEKE--------ELEEKAEEIFEKLKK 278
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1815-1923 |
2.81e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1815 KKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKEL---TYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEA 1891
Cdd:COG2433 412 EEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArseERREIRKDREISRLDREIERLERELEEERERIEEL 491
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 153791586 1892 EEQSNTnLAKFRKLQH----------------ELEEAEERADIAESQV 1923
Cdd:COG2433 492 KRKLER-LKELWKLEHsgelvpvkvvekftkeAIRRLEEEYGLKEGDV 538
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1212-1343 |
3.10e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1212 QIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEE-QQRL--------------- 1275
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyEEQLgnvrnnkeyealqke 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791586 1276 INDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSR 1343
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1260-1638 |
3.33e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1260 DQLSELKSKEEEQQRLINDLT-AQRGRLQTEsgefsRQLDEKEALVSQLSrgkQAfTQQIEELKRQLEEeIKAKNALAHA 1338
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEqTLALLDKID-----RQKEETEQLKQQLA---QA-PAKLRQAQAELEA-LKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1339 LQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYE------TDAIQRTEELEEAKK--KLAQRLQAAEEHV 1410
Cdd:PRK11281 116 ETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraqaalYANSQRLQQIRNLLKggKVGGKALRPSQRV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1411 EaVNAKCASLE-KTKQR---LQNEVEDLMLDVER---TNAACAALDKKQRNFDKILAEWK-QKCEETHAELEASQKEARS 1482
Cdd:PRK11281 196 L-LQAEQALLNaQNDLQrksLEGNTQLQDLLQKQrdyLTARIQRLEHQLQLLQEAINSKRlTLSEKTVQEAQSQDEAARI 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1483 LGTELFKIKNAYE--------ESLDQLETLKREN---KN----LQQEISDLTEQIA--EGG---KRIhelekikkqVEQE 1542
Cdd:PRK11281 275 QANPLVAQELEINlqlsqrllKATEKLNTLTQQNlrvKNwldrLTQSERNIKEQISvlKGSlllSRI---------LYQQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1543 KCELQAALEEAEASleheeGKI--LRI-QLELNQVKSevdrKIAEKDEEIDQLKRNHirivesmQSTLDAEIR-SRNDAI 1618
Cdd:PRK11281 346 QQALPSADLIEGLA-----DRIadLRLeQFEINQQRD----ALFQPDAYIDKLEAGH-------KSEVTDEVRdALLQLL 409
|
410 420
....*....|....*....|.
gi 153791586 1619 RLKKKMEGDLN-EMEIQLNHA 1638
Cdd:PRK11281 410 DERRELLDQLNkQLNNQLNLA 430
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
1149-1367 |
3.52e-03 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 42.26 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1149 LEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLrkKHADSVAE-LGEQIDNLQRVKQKLEKEK 1227
Cdd:PRK15374 101 LSQLESRLAVWQAMIESQKEMGIQVSKEFQTALGEAQEATDLYEASIKKT--DTAKSVYDaAEKKLTQAQNKLQSLDPAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1228 SEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQqrlINDLTAQRGRLQTESGEFSRQLDEKEalVSQL 1307
Cdd:PRK15374 179 PGYAQAEAAVEQAGKEATEAKEALDKATDATVKAGTDAKAKAEKA---DNILTKFQGTANAASQNQVSQGEQDN--LSNV 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1308 SRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRH-DCDLLREQYEEEQESKAELQRAL 1367
Cdd:PRK15374 254 ARLTMLMAMFIEIVGKNTEESLQNDLALFNALQEGRQaEMEKKSAEFQEETRKAEETNRIM 314
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1778-1941 |
3.99e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1778 EQDTSAHLERMKKNMEQtvkdlqlrLDEAEQLALKGgKKQIQKLEaRVRELEGEVEsEQKRNAEAVKGLR------KHER 1851
Cdd:COG4913 220 EPDTFEAADALVEHFDD--------LERAHEALEDA-REQIELLE-PIRELAERYA-AARERLAELEYLRaalrlwFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1852 RVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTN-LAKFRKLQHELEEAEERADIAESQVNKLRVKS 1930
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALL 368
|
170
....*....|.
gi 153791586 1931 REVHTKVISEE 1941
Cdd:COG4913 369 AALGLPLPASA 379
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
976-1301 |
4.13e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 976 ATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQ-------------------TLDDLQAE----EDKVNTLTKAKIK 1032
Cdd:COG3096 782 AREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAfsqfvgghlavafapdpeaELAALRQRrselERELAQHRAQEQQ 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1033 LEQQVDDLEGSLEQEKKLR--------MDLERAKRKLEGDLKLAQESimdiENEKQQLDEKLKKKEFEISNLQSKIEDEQ 1104
Cdd:COG3096 862 LRQQLDQLKEQLQLLNKLLpqanlladETLADRLEELREELDAAQEA----QAFIQQHGKALAQLEPLVAVLQSDPEQFE 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1105 ALGIQLQkkikelqarieeleeeieaerasRAKAEKQRSDLSRE-LEEISERL-----EEAGGATSAQIEMNKKREAEFQ 1178
Cdd:COG3096 938 QLQADYL-----------------------QAKEQQRRLKQQIFaLSEVVQRRphfsyEDAVGLLGENSDLNEKLRARLE 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1179 KMRRDLEEATLQHEAtaatLRKKHADSVAELGE---QIDNLQRVKQKLEKEKSEMKMEIDDlasnvETVSKAKGNLekmc 1255
Cdd:COG3096 995 QAEEARREAREQLRQ----AQAQYSQYNQVLASlksSRDAKQQTLQELEQELEELGVQADA-----EAEERARIRR---- 1061
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 153791586 1256 RTLEDQLSELKSKeeeqqrlINDLTAQRGRLQTESGEFSRQLDEKE 1301
Cdd:COG3096 1062 DELHEELSQNRSR-------RSQLEKQLTRCEAEMDSLQKRLRKAE 1100
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1447-1835 |
4.95e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1447 ALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGG 1526
Cdd:pfam07888 49 AQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1527 KRIHELEKIKKQVEQEKCELQAALE-------EAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKdeeidQLKRNHIRI 1599
Cdd:pfam07888 129 ARIRELEEDIKTLTQRVLERETELErmkerakKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF-----QELRNSLAQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1600 VESMQSTLDAEIrsrndairlkkkmegdlNEMEIQLNHANRMAAE---ALRNYRNTQGILKDTQihlddalRSQEDLKEQ 1676
Cdd:pfam07888 204 RDTQVLQLQDTI-----------------TTLTQKLTTAHRKEAEneaLLEELRSLQERLNASE-------RKVEGLGEE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1677 LA-MVERR----ANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLhtQNTSLinTKKKLETDISQMQgEMEDIL 1751
Cdd:pfam07888 260 LSsMAAQRdrtqAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQ--QSAEA--DKDRIEKLSAELQ-RLEERL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1752 QEARNAEEKAKKaitdaammaeELKKEQDTS-AHLERMKKNMEQTVKDLQLRLDEAEQLALkggkkQIQKLEARVRELEG 1830
Cdd:pfam07888 335 QEERMEREKLEV----------ELGREKDCNrVQLSESRRELQELKASLRVAQKEKEQLQA-----EKQELLEYIRQLEQ 399
|
....*
gi 153791586 1831 EVESE 1835
Cdd:pfam07888 400 RLETV 404
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1075-1435 |
5.72e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1075 IENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISE 1154
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1155 RLEeaggATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQID---NLQRVKQKLEKEKSEMK 1231
Cdd:pfam07888 116 EKD----ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAerkQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1232 MEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGK 1311
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1312 QAFTQ---QIEELKRQLEEeikAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYEtdaiqr 1388
Cdd:pfam07888 272 AELHQarlQAAQLTLQLAD---ASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMERE------ 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 153791586 1389 TEELEEAKKKLAQRLQAAEEHVEAVNAKCA--SLEKTKQRLQNEVEDLM 1435
Cdd:pfam07888 343 KLEVELGREKDCNRVQLSESRRELQELKASlrVAQKEKEQLQAEKQELL 391
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1315-1589 |
6.00e-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: 41.55 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1315 TQQIEELKRQLEEEIKAknalahalqssrhdcdlLREQYEEEQESKAELQRALSKANTEVAQWRTKYETD--AIQRTEEL 1392
Cdd:pfam05667 323 VETEEELQQQREEELEE-----------------LQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELkeQNEELEKQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1393 EEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVED----LMLDVERTNAACAA-LDKKQRNFDKIlAEWKQKCE 1467
Cdd:pfam05667 386 YKVKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKhrvpLIEEYRALKEAKSNkEDESQRKLEEI-KELREKIK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1468 ETHAelEASQKEarslgtELFKiknayeESLDQLETLKREnKNLQQEIsdlteqiaeggKRIHElekIKKQVEQEKCELQ 1547
Cdd:pfam05667 465 EVAE--EAKQKE------ELYK------QLVAEYERLPKD-VSRSAYT-----------RRILE---IVKNIKKQKEEIT 515
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 153791586 1548 AALEEAEAsleheegkilrIQLELNQVKSEVDRKIAEKDEEI 1589
Cdd:pfam05667 516 KILSDTKS-----------LQKEINSLTGKLDRTFTVTDELV 546
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1680-1919 |
6.57e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.67 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1680 VERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLhtqntslintKKKLETDISQMQgEMEDILQEARNAEE 1759
Cdd:pfam00038 45 PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDF----------RQKYEDELNLRT-SAENDLVGLRKDLD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1760 KAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQTVKDLQLRLDEAEQL-------------ALKGGKKQIQKLEARVR 1826
Cdd:pfam00038 114 EATLARVDLEAKIESLKEE------LAFLKKNHEEEVRELQAQVSDTQVNvemdaarkldltsALAEIRAQYEEIAAKNR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1827 -ELE-------GEVESEQKRNAEAVKGLRKherrvkELTyqteEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTN 1898
Cdd:pfam00038 188 eEAEewyqsklEELQQAAARNGDALRSAKE------EIT----ELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQ 257
|
250 260
....*....|....*....|...
gi 153791586 1899 LAKFRKLQHELEEA--EERADIA 1919
Cdd:pfam00038 258 LADYQELISELEAElqETRQEMA 280
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1604-1926 |
6.85e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1604 QSTLDAEIRSRND-------AIRLKKKME---GDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDaLRSQ-ED 1672
Cdd:COG3096 322 ESDLEQDYQAASDhlnlvqtALRQQEKIEryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDS-LKSQlAD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1673 LKEQLAMVERRA----NLLQAeIEELRATLEQTERSRKIAEQELLDASERVQLLHTqntSLINTKKKLetDISQM-QGEM 1747
Cdd:COG3096 401 YQQALDVQQTRAiqyqQAVQA-LEKARALCGLPDLTPENAEDYLAAFRAKEQQATE---EVLELEQKL--SVADAaRRQF 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1748 EDILQ---------EARNAEEKAKKAITDA------AMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLR----LDEAEQ 1808
Cdd:COG3096 475 EKAYElvckiagevERSQAWQTARELLRRYrsqqalAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRigqqLDAAEE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1809 LALkggkkQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKnilrLQDLVDKLQAKVKSYKRQA 1888
Cdd:COG3096 555 LEE-----LLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLA----AQDALERLREQSGEALADS 625
|
330 340 350
....*....|....*....|....*....|....*...
gi 153791586 1889 EEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKL 1926
Cdd:COG3096 626 QEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
931-1118 |
7.21e-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: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 931 RAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKV---EKEKHATENKVKNLTEEMAGLDETIAKLTK--EKKAL 1005
Cdd:pfam13166 270 KAALEAHFDDEFTEFQNRLQKLIEKVESAISSLLAQLPAVsdlASLLSAFELDVEDIESEAEVLNSQLDGLRRalEAKRK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1006 QEAHQQTLDDLQAEEDKVNTLTKAKIKL----EQQVDDLEgsleqEKKlrmdlERAKRKLEGDLklaqesIMDIENEKQQ 1081
Cdd:pfam13166 350 DPFKSIELDSVDAKIESINDLVASINELiakhNEITDNFE-----EEK-----NKAKKKLRLHL------VEEFKSEIDE 413
|
170 180 190
....*....|....*....|....*....|....*..
gi 153791586 1082 LDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQ 1118
Cdd:pfam13166 414 YKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELE 450
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1427-1776 |
7.21e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1427 LQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKR 1506
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1507 ENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQvksevdRKIAEKD 1586
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA------LSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1587 EEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLnhanRMAAEALRNYRNTQGILKDTQIHLDDA 1666
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL----GLALSALLDALELEEDKEELLEEVILK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1667 LRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGE 1746
Cdd:COG4372 259 EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAE 338
|
330 340 350
....*....|....*....|....*....|
gi 153791586 1747 MEDILQEARNAEEKAKKAITDAAMMAEELK 1776
Cdd:COG4372 339 LADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
959-1061 |
7.25e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 959 DIDDLELTLAKVEKEKHATENkvknltEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVD 1038
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100
....*....|....*....|...
gi 153791586 1039 DLEGSLEQEKKLRMDLERAKRKL 1061
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLL 508
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
868-1004 |
7.26e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 40.90 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 868 ELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAeercdQLIKTKI-QLEAKIKEVTERAEdeeEINAELTAKK 946
Cdd:pfam10186 27 DLARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKL-----RLLKSEVaISNERLNEIKDKLD---QLRREIAEKK 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791586 947 RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKA 1004
Cdd:pfam10186 99 KKIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRS 156
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1296-1526 |
7.45e-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: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1296 QLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANteVA 1375
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA--RA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1376 QWRTKYE-------------TDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTN 1442
Cdd:COG3883 95 LYRSGGSvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1443 AACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQI 1522
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
....
gi 153791586 1523 AEGG 1526
Cdd:COG3883 255 AGAA 258
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
846-972 |
7.52e-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: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 846 LKSAETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVqaeaegladaeERCDQLIKtkiQLEAKI 925
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAEL-----------EEKDERIE---RLEREL 450
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 153791586 926 KEVTERAEDEEEINAELTAKKRK---LEDECSELKKDIDDLELTLAKVEK 972
Cdd:COG2433 451 SEARSEERREIRKDREISRLDREierLERELEEERERIEELKRKLERLKE 500
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1261-1371 |
7.59e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1261 QLSELKSKEEEqqrLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKA--KNALAHA 1338
Cdd:PRK00409 510 LIGEDKEKLNE---LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQaiKEAKKEA 586
|
90 100 110
....*....|....*....|....*....|....
gi 153791586 1339 LQSSRHDCDLLREQYEEEQESKA-ELQRALSKAN 1371
Cdd:PRK00409 587 DEIIKELRQLQKGGYASVKAHELiEARKRLNKAN 620
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
845-1157 |
8.28e-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: 41.31 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 845 LLKSAETEKEMATMKEEFQKIKDELAKSEAKRKeleekmvtllkekndlqlQVQAEAEGLADaeercdqliktkiqleak 924
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARR------------------QAQQERDELAD------------------ 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 925 ikEVTERAEDeeeiNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKA 1004
Cdd:pfam01576 869 --EIASGASG----KSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQ 942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1005 LQEAHQQTLDDLQAEEDKVNTLTKAKIK-LEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlaqESIMDIENEKQQLD 1083
Cdd:pfam01576 943 LERQNKELKAKLQEMEGTVKSKFKSSIAaLEAKIAQLEEQLEQESRERQAANKLVRRTEKKLK---EVLLQVEDERRHAD 1019
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791586 1084 EklKKKEFEISNLQSKiedeqalgiQLQKKIKELQarieeleeeieaERASRAKAekQRSDLSRELEEISERLE 1157
Cdd:pfam01576 1020 Q--YKDQAEKGNSRMK---------QLKRQLEEAE------------EEASRANA--ARRKLQRELDDATESNE 1068
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1666-1861 |
8.73e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1666 ALRSQEDLKEQLAMVERRAN------LLQAEIEELRATLEQTERSRKI----------AEQELLDASERVQLLHTQNTSL 1729
Cdd:PRK11281 34 DLPTEADVQAQLDALNKQKLleaedkLVQQDLEQTLALLDKIDRQKEEteqlkqqlaqAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1730 INTK------KKLETDISQMQGEMEDiLQEA-----------RNAEEKAKKAITDAAMMAEE----LKKEQDTSAHL--- 1785
Cdd:PRK11281 114 TRETlstlslRQLESRLAQTLDQLQN-AQNDlaeynsqlvslQTQPERAQAALYANSQRLQQirnlLKGGKVGGKALrps 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1786 ERMKKNMEQTVKDLQLRLdeaEQLALKG-------GKKQIQKLEARVRELEGEVESEQkrnaEAV--KGLRKHERRVKEL 1856
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDL---QRKSLEGntqlqdlLQKQRDYLTARIQRLEHQLQLLQ----EAInsKRLTLSEKTVQEA 265
|
....*
gi 153791586 1857 TYQTE 1861
Cdd:PRK11281 266 QSQDE 270
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1235-1405 |
9.13e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.17 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1235 DDLASNVETVSKAKGNLEKMCRTLEDQLSelKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDE-----KEALVSQLSR 1309
Cdd:pfam01442 4 DSLDELSTYAEELQEQLGPVAQELVDRLE--KETEALRERLQKDLEEVRAKLEPYLEELQAKLGQnveelRQRLEPYTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1310 GKQAFTQQIEELKRQLEEEI-KAKNALAHALQSsrhdcdlLREQYEE-EQESKAELQRALSKANTEVAQWRTKYETDAIQ 1387
Cdd:pfam01442 82 LRKRLNADAEELQEKLAPYGeELRERLEQNVDA-------LRARLAPyAEELRQKLAERLEELKESLAPYAEEVQAQLSQ 154
|
170
....*....|....*...
gi 153791586 1388 RTEELEEAKKKLAQRLQA 1405
Cdd:pfam01442 155 RLQELREKLEPQAEDLRE 172
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1688-1894 |
9.32e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1688 QAEIEELRATLEQTERSRKIAEQELLDASERVQllhtqntSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITD 1767
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELE-------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1768 AAMMAEELKKEQDTSAHLERMK--KNMEQTVKDLQL--RLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAv 1843
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLgsESFSDFLDRLSAlsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153791586 1844 kglrkhERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQ 1894
Cdd:COG3883 167 ------EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1174-1434 |
9.90e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.29 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1174 EAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEK 1253
Cdd:pfam00038 24 EQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAEN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1254 MCRTLEDQLSEL---KSKEEEQ-QRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLeEEI 1329
Cdd:pfam00038 104 DLVGLRKDLDEAtlaRVDLEAKiESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQY-EEI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1330 KAKNalahalqssrhdcdllREQYEEEQESK-AELQRALSKantevaqwrtkyETDAIQRT-EELEEAKKklaqRLQAAE 1407
Cdd:pfam00038 183 AAKN----------------REEAEEWYQSKlEELQQAAAR------------NGDALRSAkEEITELRR----TIQSLE 230
|
250 260 270
....*....|....*....|....*....|.
gi 153791586 1408 EHVEAVNAKCASLEK----TKQRLQNEVEDL 1434
Cdd:pfam00038 231 IELQSLKKQKASLERqlaeTEERYELQLADY 261
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1384-1678 |
9.99e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 9.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1384 DAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNevedlmldvertnaACAALDKKQRNFDKILAEWK 1463
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQ--------------APAKLRQAQAELEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1464 QKCEETHAELEASQKEARSlgtelfkiknayEESLDQLETLKRE----NKNL--QQEISDLTE-QIAEGGKRIHELEKIK 1536
Cdd:PRK11281 112 EETRETLSTLSLRQLESRL------------AQTLDQLQNAQNDlaeyNSQLvsLQTQPERAQaALYANSQRLQQIRNLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791586 1537 KQVEQEKCEL---QAALEEAEASLeheegkiLRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRS 1613
Cdd:PRK11281 180 KGGKVGGKALrpsQRVLLQAEQAL-------LNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINS 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791586 1614 RNdAIRLKKKMEGDLNEMEIQLNHANRM-AAEALRNYRNTQGILKDTQI-------------HLDDALRSQEDLKEQLA 1678
Cdd:PRK11281 253 KR-LTLSEKTVQEAQSQDEAARIQANPLvAQELEINLQLSQRLLKATEKlntltqqnlrvknWLDRLTQSERNIKEQIS 330
|
|
| |
