|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 1333.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 340 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 420 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKPEAH 579
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 580 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAGGGKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 115527082 740 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14910 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
100-770 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1313.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEvtsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKES---GKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 340 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd01377 238 DILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 420 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd01377 318 KEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPakGKPEA 578
Cdd:cd01377 398 EQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKP--KKSEA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 579 HFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVgatgAEAEAGGGKKGGKKKGSSFQTVSALFREN 658
Cdd:cd01377 476 HFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFK----DYEESGGGGGKKKKKGGSFRTVSQLHKEQ 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 659 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 738
Cdd:cd01377 552 LNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGF 631
|
650 660 670
....*....|....*....|....*....|..
gi 115527082 739 FiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd01377 632 D-DGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 1313.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEvtSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKK--DSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14913 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 340 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 420 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14913 319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKPEAH 579
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 580 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVgATGAEAEAGGGKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYA-TFATADADSGKKKVAKKKGSSFQTVSALFRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14913 558 NKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 115527082 740 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14913 638 IDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 1266.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 340 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 420 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKPEAH 579
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 580 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAGGGKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14915 561 NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 115527082 740 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14915 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 1258.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEvtSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEE--SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 340 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 420 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKPEAH 579
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 580 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvGATGAEAEAGGGKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF-STYASAEADSGAKKGAKKKGSSFQTVSALFRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14918 558 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 115527082 740 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14918 638 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 1241.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 340 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 420 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKPEAH 579
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 580 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLF--VGATGAEAEAGGGKKGGKKKGSSFQTVSALFRE 657
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFsgAQTAEGASAGGGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 658 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 737
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 115527082 738 QFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 1214.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEvTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQ-QPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 340 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14923 240 DILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 420 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKPEAH 579
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 580 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEA-EAGGGKKGGKKKGSSFQTVSALFREN 658
Cdd:cd14923 480 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAgDSGGSKKGGKKKGSSFQTVSAVFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 659 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 738
Cdd:cd14923 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 115527082 739 FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14923 640 FIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 1160.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVIQYFATIAVTGE--KKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDgpGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 338
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 339 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 419 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 499 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKPE 577
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPdKKRKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 578 AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLF--VGATGAEAEAGGGKKGGKKKGSSFQTVSALF 655
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYenYVGSDSTEDPKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 656 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 735
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 115527082 736 EGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
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 ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 1139.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14917 159 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 340 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 420 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKPEAH 579
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 580 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVgATGAEAEAGGGKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFA-NYAGADAPIEKGKGKAKKGSSFQTVSALHRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14917 558 NKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 115527082 740 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14917 638 IDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 1134.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNAN-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 340 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14916 240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 420 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKPEAH 579
Cdd:cd14916 400 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 580 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAGGGKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14916 480 FSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14916 560 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 639
|
650 660 670
....*....|....*....|....*....|.
gi 115527082 740 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14916 640 IDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
88-770 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1027.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 88 IEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFML 167
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 168 TDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEevtsgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV--------GRLEEQILQSNPILEAFGNAKTVRNNNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 248 GKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQ-GEITVPSI 326
Cdd:pfam00063 153 GKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTIDGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 327 DDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPR 406
Cdd:pfam00063 232 DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 407 VKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:pfam00063 312 IKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 486 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSN 564
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 565 NFQKPKPakgKPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLF---VGATGAEAEAGGGKKGG 641
Cdd:pfam00063 470 HFQKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFpdyETAESAAANESGKSTPK 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 642 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 721
Cdd:pfam00063 547 RTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 115527082 722 FKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:pfam00063 627 FVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 1026.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEevtsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14929 154 MLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 340 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14929 233 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 420 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14929 313 IEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKPEAH 579
Cdd:cd14929 393 EQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 580 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvGATGAEAEAGGGKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14929 473 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF-ENYISTDSAIQFGEKKRKKGASFQTVASLHKENL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14929 552 NKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKF 631
|
650 660 670
....*....|....*....|....*....|.
gi 115527082 740 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14929 632 VSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 996.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEvtsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTGKQSSDG------KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 340
Cdd:cd14934 156 LAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 341 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd14934 236 VLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 421 QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14934 316 EQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 501 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGK-PEAH 579
Cdd:cd14934 396 QEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 580 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgatgaEAEAGGGKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14934 476 FELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLF------KEEEAPAGSKKQKRGSSFMTVSNFYREQL 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqF 739
Cdd:cd14934 550 NKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-F 628
|
650 660 670
....*....|....*....|....*....|.
gi 115527082 740 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14934 629 VDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
81-782 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 988.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 81 NPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISD 160
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 161 NAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAvtgekkkeevTSGKMQGTLEDQIISANPLLEAFGNAKTVR 240
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVS----------GSNTEVGSVEDQILESNPILEAFGNAKTLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 241 NDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQG- 319
Cdd:smart00242 151 NNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 320 EITVPSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQA-EPDGTEVADKAAYLQNLNSADL 398
Cdd:smart00242 230 CLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 399 LKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQ 478
Cdd:smart00242 310 EKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 479 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYe 557
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 558 QHLGKSNNFQKPKPakgKPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgatgaeaeagGG 637
Cdd:smart00242 468 QHHKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLF-----------PS 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 638 KKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRI 717
Cdd:smart00242 534 GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRL 613
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115527082 718 LYADFKQRYKVLNASAIPEGQFiDSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGLLEEMRD 782
Cdd:smart00242 614 PFDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 976.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEvtsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAA----KSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14909 157 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 340 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 420 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14909 317 VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAK-GKPEA 578
Cdd:cd14909 397 EQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 579 HFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAGGGKKGGKKKGSSFQTVSALFREN 658
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQ 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 659 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 738
Cdd:cd14909 557 LNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE 636
|
650 660 670
....*....|....*....|....*....|..
gi 115527082 739 fiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14909 637 --DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
100-770 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 833.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQ-EAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 179 GESGAGKTVNTKRVIQYFATIAvtgekKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALS-----GSGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDY----AFVSQGEITVPSIDDQEELMA 334
Cdd:cd00124 156 GRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYylndYLNSSGCDRIDGVDDAEEFQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 335 TDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREE--QAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNE 412
Cdd:cd00124 236 LLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 413 YVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 490
Cdd:cd00124 316 TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 491 FFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKP 569
Cdd:cd00124 396 FFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 570 KPAKGkpeaHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKsamktlallfvgatgaeaeagggkkggkkkgssfq 649
Cdd:cd00124 475 RKAKL----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS----------------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 650 tvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 729
Cdd:cd00124 516 --GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRIL 593
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 115527082 730 NASAiPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd00124 594 APGA-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
30-1116 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 825.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 30 KPFDAKTSVFVVDPKESFVKATVQsregGKVTAKTEAGATVTVKDDQVFPMNPPKYDKIEDMAMMTHLHEPAVLYNLKER 109
Cdd:COG5022 14 IPDEEKGWIWAEIIKEAFNKGKVT----EEGKKEDGESVSVKKKVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 110 YAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNT 189
Cdd:COG5022 90 YNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 190 KRVIQYFAtiAVTGekkkeevTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETY 269
Cdd:COG5022 170 KRIMQYLA--SVTS-------SSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 270 LLEKSRVTFQLKAERSYHIFYQIMSNKkPDLIEMLLITTNPYDYAFVSQGE-ITVPSIDDQEELMATDSAIEILGFTSDE 348
Cdd:COG5022 241 LLEKSRVVHQNKNERNYHIFYQLLAGD-PEELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 349 RVSIYKLTGAVMHYGNMKFKqKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVG 428
Cdd:COG5022 320 QDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 429 ALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEG 508
Cdd:COG5022 399 SLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 509 IEWTFIDFgMDLAACIELIEK--PMGIFSILEEECMFPKATDTSFKNKLYEQ-HLGKSNNFQKPKPAKGKpeahFSLIHY 585
Cdd:COG5022 479 IEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVKHY 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 586 AGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgatgaeaeaggGKKGGKKKGSSFQTVSALFRENLNKLMTN 665
Cdd:COG5022 554 AGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLF------------DDEENIESKGRFPTLGSRFKESLNSLMST 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 666 LRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI---DS 742
Cdd:COG5022 622 LNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDT 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 743 KKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDEKLAQLITRTQAMCRGFLARVEYQKMVERRESIFCIQYNV 822
Cdd:COG5022 702 KNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGF 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 823 RAFMNVKHWPWMKLYFKIKPLLKSAETEKEMANMKEEFEKTKEELaKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSL 902
Cdd:COG5022 782 RLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTI-KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKR 860
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 903 ADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINaELTAKKRKLEDECSELKKDID-----DLELTLAKVEKEKHATEN 977
Cdd:COG5022 861 FSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELESEIIELKKSLSsdlieNLEFKTELIARLKKLLNN 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 978 -KVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQekkiRMDLERAK 1056
Cdd:COG5022 940 iDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQ----YGALQEST 1015
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1057 RKLEGDLKLAQESTMDIENDKQQLDEKLKKKefEMSGLQSKIEDEQalgMQLQKKIKELQ 1116
Cdd:COG5022 1016 KQLKELPVEVAELQSASKIISSESTELSILK--PLQKLKGLLLLEN---NQLQARYKALK 1070
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 776.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVIQYFATIAVTGEKK-----KEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASKPKGsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 256 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDDQEELMAT 335
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 336 DSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYV 414
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 415 TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 494 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLgksnnfQKPKPAK 573
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 574 G--KPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGAT---GAEAEAGGGKKGGKKKGSSF 648
Cdd:cd14911 474 TdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgMAQQALTDTQFGARTRKGMF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 649 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 115527082 729 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14911 634 LTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 764.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEevtsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVASSHKGRKD----HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14920 158 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL--EGFNnYRFLSNGYIPIPGQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 340 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 419 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14920 315 TKEQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 497 FVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNFQKPKPAK 573
Cdd:cd14920 394 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 574 GkpEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAGGGKKGGKKKGSS------ 647
Cdd:cd14920 473 D--KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAyktkkg 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 648 -FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 726
Cdd:cd14920 551 mFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 115527082 727 KVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14920 631 EILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 716.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 340
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAG-DKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 341 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 420 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14932 320 QEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 499 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNFQKPKpaKGK 575
Cdd:cd14932 400 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKV-VQEQGNNPKFQKPK--KLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 576 PEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLF------VGATGAEAEAGGGKKGGKKKGSSFQ 649
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWkdvdriVGLDKVAGMGESLHGAFKTRKGMFR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 650 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 729
Cdd:cd14932 557 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 115527082 730 NASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14932 637 TPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 689.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASSHKGKKDTSITGE----LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMATDSAIE 340
Cdd:cd14921 158 IVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN-NYTFLSNGFVPIPAAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 341 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 420 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14921 316 KEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 499 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGK 575
Cdd:cd14921 396 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 576 PEahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAGGGKKGGKKKGSS-------F 648
Cdd:cd14921 475 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSAsktkkgmF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 649 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 115527082 729 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14921 633 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-770 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 680.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 179 GESGAGKTVNTKRVIQYFATiaVTGEKKKEEVTsgkmqgtlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFAT--VGGSSSGETQV--------EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 338
Cdd:cd01380 151 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 339 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 419 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd01380 311 TLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNN-FQKPKPAKGK 575
Cdd:cd01380 391 FKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFSNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 576 peahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKtlallfvgatgaeaeagggkkggkkkgssFQTVSALF 655
Cdd:cd01380 470 ----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR-----------------------------KKTVGSQF 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 656 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAip 735
Cdd:cd01380 517 RDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK-- 594
|
650 660 670
....*....|....*....|....*....|....*
gi 115527082 736 EGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd01380 595 EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-770 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 672.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 340
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL-ENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 341 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 421 QQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKpaKGKP 576
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPK--KLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 577 EAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLF-----VGATGAEAEAGGGKKGGKKKGSSFQTV 651
Cdd:cd15896 478 EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWkdvdrIVGLDKVSGMSEMPGAFKTRKGMFRTV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 652 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 731
Cdd:cd15896 558 GQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 637
|
650 660 670
....*....|....*....|....*....|....*....
gi 115527082 732 SAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
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 ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 665.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEevtsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14919 155 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 340 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 419 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14919 312 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 498 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 574
Cdd:cd14919 392 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 575 KpeAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVG-------ATGAEAEAGGGKKGGKKKGSS 647
Cdd:cd14919 471 K--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGMSETALPGAFKTRKGM 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 648 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14919 549 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 115527082 728 VLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
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 ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 652.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEvtsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPKGRKEP----GVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATDSAIE 340
Cdd:cd14930 158 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 341 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14930 236 VLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 420 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14930 315 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 498 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 574
Cdd:cd14930 394 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLRD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 575 kpEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLF-----VGATGAEAEAGGGKKGGKKKGSSFQ 649
Cdd:cd14930 473 --QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegIVGLEQVSSLGDGPPGGRPRRGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 650 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 729
Cdd:cd14930 551 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 115527082 730 NASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14930 631 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-770 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 629.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRgkKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIAVTGekkkeevtsgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd01383 79 ESGAGKTETAKIAMQYLAALGGGS-------------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSA 338
Cdd:cd01383 146 KICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNcLTIDGVDDAKKFHELKEA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 339 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd01383 225 LDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 419 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDT-KQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd01383 305 TLQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 498 VLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNFqkpkpaKGKP 576
Cdd:cd01383 385 KLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGER 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 577 EAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKtLALLFVGATGAEAEAGGGKKGGKKKGSSFQTVSALFR 656
Cdd:cd01383 457 GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQ-LPQLFASKMLDASRKALPLTKASGSDSQKQSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 657 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 736
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSA 615
|
650 660 670
....*....|....*....|....*....|....
gi 115527082 737 GQFIDSkkASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd01383 616 SQDPLS--TSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
101-770 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 626.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVIQYFATIavtgekkkeevtSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd01381 82 SGAGKTESTKLILQYLAAI------------SGQ-HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSAI 339
Cdd:cd01381 149 IEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD-ASDYYYLTQGNcLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 340 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQRE--EQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 417
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 418 QTVQQVYNAVGALAKAVYDKMFLWMVTRIN----QQLDTKQPRQYfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINsaiyKPRGTDSSRTS-IGVLDIFGFENFEVNSFEQLCINFANENLQQFFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 494 HHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPkpa 572
Cdd:cd01381 387 RHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 573 KGKPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAGGGKkggkkkgssfQTVS 652
Cdd:cd01381 462 KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKS----------PTLS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 653 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnAS 732
Cdd:cd01381 532 SQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVL-VP 610
|
650 660 670
....*....|....*....|....*....|....*...
gi 115527082 733 AIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd01381 611 GIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
101-770 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 623.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVIQYFAtiAVTGeKKKEEVTSGKmqgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd01378 82 SGAGKTEASKRIMQYIA--AVSG-GSESEVERVK------DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 340
Cdd:cd01378 153 PVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 341 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDgTEVADKAAYLQNLNSADLLKALCYPRVKVGNEY---VTKG 417
Cdd:cd01378 233 VIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 418 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQ-YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHhm 496
Cdd:cd01378 312 LNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 497 FVL--EQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNKLyEQHLGKSNNFQKPKPA 572
Cdd:cd01378 390 LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 573 KGKPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAGGGkkggkkkgssfqTVS 652
Cdd:cd01378 468 FELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSKKRPP------------TAG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 653 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 732
Cdd:cd01378 536 TKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPK 615
|
650 660 670
....*....|....*....|....*....|....*...
gi 115527082 733 AIPEGQFIDsKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd01378 616 TWPAWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
101-770 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 605.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVIQYFAtiAVTGEkkkeevtsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14883 82 SGAGKTETTKLILQYLC--AVTNN-----------HSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPDLIEMLLITTNPYDYAFVSQ-GEITVPSIDDQEELMATDSA 338
Cdd:cd14883 149 IKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGaKHSKELKEKLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 339 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 417
Cdd:cd14883 229 MNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 418 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14883 309 LKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 498 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGKP 576
Cdd:cd14883 389 KLEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPDRRRWKT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 577 EahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAGGGKKGGKKKGS----SFQTVS 652
Cdd:cd14883 467 E--FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTSRgtskGKPTVG 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 653 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 732
Cdd:cd14883 545 DTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPR 624
|
650 660 670
....*....|....*....|....*....|....*...
gi 115527082 733 AIPEGQFIDsKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14883 625 ARSADHKET-CGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
100-770 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 579.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 179 GESGAGKTVNTKRVIQYFATIAvtgekkKEEVTSGKmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG------GRAVTEGR---SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDS 337
Cdd:cd01384 152 GRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKD-PKQFHYLNQSKcFELDGVDDAEEYRATRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 338 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKqkqreEQAEPDGTEVADKAA--YLQNlnSADLL--------KALCYPRV 407
Cdd:cd01384 231 AMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEKSefHLKA--AAELLmcdekaleDALCKRVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 408 KVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd01384 304 VTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 488 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKSNNF 566
Cdd:cd01384 384 LQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 567 QKPKpakgKPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgatgaeaeaGGGKKGGKKKGS 646
Cdd:cd01384 462 SKPK----LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF----------PPLPREGTSSSS 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 647 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 726
Cdd:cd01384 528 KFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRF 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 115527082 727 KVLnASAIPEGQFiDSKKASEKLLGSIDIDhtQYKFGHTKVFFK 770
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 ... |
101-770 |
3.64e-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: 539.75 E-value: 3.64e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAY-QFM---LTDRENQSI 175
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtQLIqsgVLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 176 LITGESGAGKTVNTKRVIQYFATI----AVTGEKKKEEVTSGKMQ--GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARItsgfAQGASGEGEAASEAIEQtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQGEITVPSIDDQ 329
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 330 EELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT-EVADKAAYLQNLNSADLLKALCYPRVK 408
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 409 VGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 489 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-----KPmGIFSILEEECMFPKA-TDTSFKNKLYEQHLGK 562
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgkvngKP-GIFITLDDCWRFKGEeANKKFVSQLHASFGRK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 563 SNNFQKPKPAKGKP---------EAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSamktlallfvgatgaeae 633
Cdd:cd14890 479 SGSGGTRRGSSQHPhfvhpkfdaDKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS------------------ 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 634 agggkkggkkkGSSFQTVS--ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRK 711
Cdd:cd14890 541 -----------RRSIREVSvgAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQ 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 712 GFPSRILYADFKQRYKVLNASAipegqfiDSKKASEKLLGSI-DIDHTQYKFGHTKVFFK 770
Cdd:cd14890 610 GFALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKMlGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
103-770 |
2.99e-171 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 536.45 E-value: 2.99e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 182 GAGKTVNTKRVIQYFATIAvtgekkkeevtsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01382 84 GAGKTESTKYILRYLTESW------------GSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLittnpydyafvsqgeiTVPSIDDQEELMATDSAIEI 341
Cdd:cd01382 152 VGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 342 LGFTSDERVSIYKLTGAVMHYGNMKFkqkqrEEQAEPD--GTEVADK-------AAYLQNLNSADLLKALCYpRVKVGNE 412
Cdd:cd01382 216 IGLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSggGCNVKPKseqsleyAAELLGLDQDELRVSLTT-RVMQTTR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 413 YVTKGQ------TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQpRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 486
Cdd:cd01382 290 GGAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 487 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLgksNN 565
Cdd:cd01382 369 KLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK---NH 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 566 FQKPKPAKGKPEAH--------FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAGGG 637
Cdd:cd01382 445 FRLSIPRKSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSKQK 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 638 KKGGkkkgsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRI 717
Cdd:cd01382 525 AGKL-----SFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRT 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 115527082 718 LYADFKQRYKVLNASAIPEgqfIDSK---KASEKLLGSIDIDhtqYKFGHTKVFFK 770
Cdd:cd01382 600 SFHDLYNMYKKYLPPKLAR---LDPRlfcKALFKALGLNEND---FKFGLTKVFFR 649
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
100-770 |
1.04e-165 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 522.33 E-value: 1.04e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRgKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 179 GESGAGKTVNTKRVIQYFATIAVTGEKKKEEVtsgkmqgtlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF--- 255
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSLV---------EAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFskl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 256 ------GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMS-----------------------NKKPDLIEMLLI 306
Cdd:cd14888 151 kskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 307 TT-NPYDYAFVSqGEITVPSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTE 382
Cdd:cd14888 231 EPhLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 383 VADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIG 461
Cdd:cd14888 310 DLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 462 VLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPMGIFSILEEE 540
Cdd:cd14888 390 VLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 541 CMFPKATDTSFKNKLYEQHLGkSNNFqkpKPAKGKPEAhFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTL 620
Cdd:cd14888 469 CFVPGGKDQGLCNKLCQKHKG-HKRF---DVVKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFI 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 621 ALLFvgatgaeAEAGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCN 700
Cdd:cd14888 544 SNLF-------SAYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYG 616
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 701 GVLEGIRICRKGFPSRILYADFKQRYKVLnasAIPEGQfidskkasekllgsidIDHTQYKFGHTKVFFK 770
Cdd:cd14888 617 GVLQAVQVSRAGYPVRLSHAEFYNDYRIL---LNGEGK----------------KQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
100-770 |
2.77e-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: 520.10 E-value: 2.77e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIAVTgekkkeevTSGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS--------TNG-----VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSnkKPDLIEMLLITTNPyDYAFVSQGE-ITVPSIDDQEELMATDSA 338
Cdd:cd14872 148 RICGASTENYLLEKSRVVYQIKGERNFHIFYQLLA--SPDPASRGGWGSSA-AYGYLSLSGcIEVEGVDDVADFEEVVLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 339 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEP----DGTEVADKAAYLQnLNSADLLKALCYPRVKVgneyv 414
Cdd:cd14872 225 MEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGstvaNRDVLKEVATLLG-VDAATLEEALTSRLMEI----- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 415 tKGQ-------TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 486
Cdd:cd14872 299 -KGCdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 487 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSnn 565
Cdd:cd14872 378 KLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS-- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 566 FQKPKPAKGKPEaHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgatgaeaeagggKKGGKKKG 645
Cdd:cd14872 455 TFVYAEVRTSRT-EFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF-------------PPSEGDQK 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 646 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 725
Cdd:cd14872 521 TSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKR 600
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 115527082 726 YKVLNaSAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14872 601 YRFLV-KTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
850-1927 |
1.19e-162 |
|
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: 528.21 E-value: 1.19e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 850 EKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTER 929
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 930 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQ 1009
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1010 TLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEF 1089
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1090 EMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNK 1169
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1170 KREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNL 1249
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1250 EKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKA 1329
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1330 KSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDAEEHVE 1409
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1410 AVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKC-----EETHAELEASQKESRSLSte 1484
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISaryaeERDRAEAEAREKETRALS-- 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1485 lfkIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKILR 1564
Cdd:pfam01576 641 ---LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLR 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1565 IQLELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEAL 1644
Cdd:pfam01576 718 LEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1645 RNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQN 1724
Cdd:pfam01576 798 KQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGK 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1725 TSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEA 1804
Cdd:pfam01576 878 SALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1805 EQLALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKR 1884
Cdd:pfam01576 958 EGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKR 1037
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|...
gi 115527082 1885 QAEEAEEQSNVNLSKFRRIQHELEEAEERADIAESQVNKLRVK 1927
Cdd:pfam01576 1038 QLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
100-770 |
6.50e-162 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 511.63 E-value: 6.50e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 179 GESGAGKTVNTKRVIQYFATIAvtgekkkeevtSGKMQGTLEdQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA-----------GGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLiEMLLITTNPYDYAFvSQGEITVPSIDDQEELMATDSA 338
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEE-RLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 339 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE--PDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd14903 227 LSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 417 GQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14903 307 PLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgkp 576
Cdd:cd14903 387 FKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR--- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 577 eAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAGGGKKGGKKKGS----SFQTVS 652
Cdd:cd14903 463 -TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRggalTTTTVG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 653 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnas 732
Cdd:cd14903 542 TQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF--- 618
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 115527082 733 aIPEGQFIDSKKAS--EKLLGSIDIDH-TQYKFGHTKVFFK 770
Cdd:cd14903 619 -LPEGRNTDVPVAErcEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
103-770 |
1.03e-160 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 509.61 E-value: 1.03e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESG 182
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 183 AGKTVNTKRVIQYFATIavtgekkkeevtSGKMQGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01385 84 SGKTESTNFLLHHLTAL------------SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSAIE 340
Cdd:cd01385 152 RGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDcYTLEGEDEKYEFERLKQAME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 341 ILGFTSDERVSIYKLTGAVMHYGNMKFKQK--QREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd01385 231 MVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 419 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQL----DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 494
Cdd:cd01385 311 KLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 495 HMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHlgKSNNF-QKPKpa 572
Cdd:cd01385 391 HIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAKFKQQH--KDNKYyEKPQ-- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 573 kgKPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKS--------------AMKTLALL--FVGATGAEAEAGG 636
Cdd:cd01385 466 --VMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSssafvreligidpvAVFRWAVLraFFRAMAAFREAGR 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 637 GKKGGKKKGSSFQ------------------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLR 698
Cdd:cd01385 544 RRAQRTAGHSLTLhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLR 623
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115527082 699 CNGVLEGIRICRKGFPSRILYADFKQRYKVLnasaIPEGQfIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd01385 624 YTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
101-770 |
6.59e-160 |
|
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: 506.21 E-value: 6.59e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEvtsgkmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTGK 260
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVNQRRNNLVTE------------QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQI---MSNKKPDLIEMLlittNPYDYAFVSQG-EITVPSIDDQEELMATD 336
Cdd:cd01387 149 IVGAITSQYLLEKSRIVTQAKNERNYHVFYELlagLPAQLRQKYGLQ----EAEKYFYLNQGgNCEIAGKSDADDFRRLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 337 SAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEpdGTEVADKA-----AYLQNLNSADLLKALCYPRVKVGN 411
Cdd:cd01387 225 AAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQE--GVSVGSDAeiqwvAHLLQISPEGLQKALTFKVTETRR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 412 EYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 491
Cdd:cd01387 303 ERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 492 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 570
Cdd:cd01387 383 FNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 571 paKGKPEahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgatgAEAEAGGGKKGGKKKGSSF-- 648
Cdd:cd01387 461 --MPLPE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLF-----SSHRAQTDKAPPRLGKGRFvt 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 649 -----QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFK 723
Cdd:cd01387 532 mkprtPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFI 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 115527082 724 QRYKVLNASAIPEGQFIDSKKA-SEKLLGSIDIDhtQYKFGHTKVFFK 770
Cdd:cd01387 612 DRYRCLVALKLPRPAPGDMCVSlLSRLCTVTPKD--MYRLGATKVFLR 657
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
100-768 |
6.74e-160 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 505.86 E-value: 6.74e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAY------RGKKRQEAPPHIFSISDNAYQFMLTDRE-- 171
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 172 --NQSILITGESGAGKTVNTKRVIQYFATIAvTGEKKKEEVTSgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVS-SATTHGQNATE---RENVRDRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNP-YDYAFVSQGEITVPSIDD 328
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEeYKYLNSSQCYDRRDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 329 QEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAY-LQNLNSADLLKALCYPRV 407
Cdd:cd14901 237 SVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 408 KVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 486 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKSN 564
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 565 NFQKPKPAKGKpeAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLAllfvgatgaeaeagggkkggkkk 644
Cdd:cd14901 475 SFSVSKLQQGK--RQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS----------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 645 gssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 724
Cdd:cd14901 530 ----STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVH 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 115527082 725 RYKVLNAS------AIPEGQFIDSKKASEKLLGSIDIDHTQykFGHTKVF 768
Cdd:cd14901 606 TYSCLAPDgasdtwKVNELAERLMSQLQHSELNIEHLPPFQ--VGKTKVF 653
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-770 |
2.70e-159 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 503.35 E-value: 2.70e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIavtgekkkeevtsGKMQ-GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVL-------------GKANnRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI---MSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDD--QEELM 333
Cdd:cd01379 148 GAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIyagLAEDK-KLAKYKLPENKPPRYLQNDGLTVQDIVNNSgnREKFE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 334 ATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQ----AEPDGTEVADKAAYLQNLNSADLLKALCYPRVKV 409
Cdd:cd01379 227 EIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 410 GNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQP---RQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 486
Cdd:cd01379 307 RGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSasdEPLSIGILDIFGFENFQKNSFEQLCINIANE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 487 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFG-----MDLaacieLIEKPMGIFSILEEECMFPKATDTSFKNKLyEQHLg 561
Cdd:cd01379 387 QIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKF-HNNI- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 562 KSNNFQKPKpakgKPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLAllfvgatgaeaeagggkkgg 641
Cdd:cd01379 460 KSKYYWRPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR-------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 642 kkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 721
Cdd:cd01379 516 -------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFAD 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 115527082 722 FKQRYKVL--NASAIPEGqfidSKKASEKLLGSIDIDHtqYKFGHTKVFFK 770
Cdd:cd01379 589 FLKRYYFLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
106-770 |
7.96e-156 |
|
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: 495.05 E-value: 7.96e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRG--KKRQEAPPHIFSISDNAYQFMLTDR----ENQSILIT 178
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTPQSIVVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 179 GESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14892 87 GESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPyDYAFVSQGE-ITVPSIDDQEELMATDS 337
Cdd:cd14892 167 GRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAE-SFLFLNQGNcVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 338 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAD--KAAYLQNLNSADLLKALCYpRVKVGneyvT 415
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFKLVT-QTTST----A 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 416 KGQ------TVQQVYNAVGALAKAVYDKMFLWMVTRIN----QQL------DTKQPRQYFIGVLDIAGFEIFDFNSLEQL 479
Cdd:cd14892 321 RGSvleiklTAREAKNALDALCKYLYGELFDWLISRINachkQQTsgvtggAASPTFSPFIGILDIFGFEIMPTNSFEQL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 480 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFP-KATDTSFKNKLYE 557
Cdd:cd14892 401 CINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTIYHQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 558 QHLGKSNNFQKPKPAKgkpeAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMktlallfvgatgaeaeaggg 637
Cdd:cd14892 480 THLDKHPHYAKPRFEC----DEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK-------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 638 kkggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRI 717
Cdd:cd14892 536 -----------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRR 598
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 718 LYADFKQRYKVL-------NASAIPEGQFIDSKKASEKLLGSIDIDHTQykFGHTKVFFK 770
Cdd:cd14892 599 QFEEFYEKFWPLarnkagvAASPDACDATTARKKCEEIVARALERENFQ--LGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
101-770 |
1.06e-152 |
|
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: 486.22 E-value: 1.06e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIAvtgeKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVIS----QQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQ-GEITVPSIDDQEELMATDSA 338
Cdd:cd14873 158 NIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 339 IEILGFTSDERVSIYKLTGAVMHYGNMKFkqkqreeqAEPDGTEVADK-----AAYLQNLNSADLLKALCYPRVKVGNEY 413
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLRGEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 414 VTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQyFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14873 309 ILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 494 HHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgkSNN--FQKPKP 571
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH---ANNhfYVKPRV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 572 AkgkpEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAGGGKKGGKKKgssfQTV 651
Cdd:cd14873 464 A----VNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRR----PTV 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 652 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL-N 730
Cdd:cd14873 536 SSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLmR 615
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 115527082 731 ASAIPEgqfiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14873 616 NLALPE----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-770 |
4.81e-147 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 469.94 E-value: 4.81e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKK-RQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVIQYFATIavtgekkkeevtSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKL------------SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEEL-----MAT 335
Cdd:cd14897 151 LLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELeyyrqMFH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 336 DSaIEIL---GFTSDERVSIYKLTGAVMHYGNMKFkqkqrEEQAEPDGTEVADK-----AAYLQNLNSADLLKALCYPRV 407
Cdd:cd14897 230 DL-TNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 408 KVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYF-----IGVLDIAGFEIFDFNSLEQLCIN 482
Cdd:cd14897 304 TIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCIN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 483 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLyEQHLG 561
Cdd:cd14897 384 LSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 562 KSNNFQKPKpaKGKPEahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgatgaeaeagggkkgg 641
Cdd:cd14897 462 ESPRYVASP--GNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF----------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 642 kkkgssfqtvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 721
Cdd:cd14897 521 ----------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYED 590
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 115527082 722 FKQRYKVL-----NASAIPEGQFIDSKKasekllgsiDIDHTQYKFGHTKVFFK 770
Cdd:cd14897 591 FVKRYKEIcdfsnKVRSDDLGKCQKILK---------TAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
102-729 |
2.63e-142 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 456.69 E-value: 2.63e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAY-----------RGKKRQEAPPHIFSISDNAYQFM--- 166
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 167 -LTDRENQSILITGESGAGKTVNTKRVIQYFATiaVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQ--AGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 246 RFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMllittnpydyafvsqgeitvps 325
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR---------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 326 iDDQEELMAtdsAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA-------DKAAYLQNLNSADL 398
Cdd:cd14900 219 -DMYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 399 LKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQL-----DTKQPRQYFIGVLDIAGFEIFDF 473
Cdd:cd14900 295 EKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 474 NSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFK 552
Cdd:cd14900 375 NSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 553 NKLYEQhLGKSNNFQKPKPAKGKpeAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMktlallfvgatgaea 632
Cdd:cd14900 454 SKLYRA-CGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYGLQ--------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 633 eagggkkggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKG 712
Cdd:cd14900 516 ----------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAG 573
|
650
....*....|....*..
gi 115527082 713 FPSRILYADFKQRYKVL 729
Cdd:cd14900 574 FPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-770 |
1.05e-140 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 453.72 E-value: 1.05e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRG--KKRQEA------PPHIFSISDNAYQFMLTDREN 172
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiIQNGEYfdikkePPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 173 QSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVT-------SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTltssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 246 RFGKFIRIHFG-TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNP--YDYAFVSQGE-I 321
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLsgDRYDYLKKSNcY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 322 TVPSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQNLNSADLL 399
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 400 KALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQL--------DTKQPRQYFIGVLDIAGFEIF 471
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 472 DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF--IDFgMDLAACIELIEK-PMGIFSILEEECMFPKATD 548
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 549 TSFKNKLYEQHLGKSNNFQKPKPAKGKpeahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGAT 628
Cdd:cd14907 482 EKLLNKIKKQHKNNSKLIFPNKINKDT----FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGED 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 629 GAEAEAGGGKKGGKKKGssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRI 708
Cdd:cd14907 558 GSQQQNQSKQKKSQKKD---KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRV 634
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115527082 709 CRKGFPSRILYADFKQRYKVLNasaipegqfidskkasekllgsididhTQYKFGHTKVFFK 770
Cdd:cd14907 635 RKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
100-770 |
2.08e-137 |
|
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: 444.00 E-value: 2.08e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 179 GESGAGKTVNTKRVIQYFATIAvtGEKKKEEVtsgkmqgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA--GGRKDKTI----------AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDS 337
Cdd:cd14904 149 GKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 338 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAdKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 417
Cdd:cd14904 229 SLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLS-QVAKMLGLPTTRIEEALCNRSVVTRNESVTVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 418 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14904 308 LAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQH--LGKSNNFQKPKPAKg 574
Cdd:cd14904 388 FKTVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 575 kpeAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgaTGAEAEAGGGKKGGKKKGSSFQTVSAL 654
Cdd:cd14904 466 ---TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF---GSSEAPSETKEGKSGKGTKAPKSLGSQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 655 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAI 734
Cdd:cd14904 540 FKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSM 619
|
650 660 670
....*....|....*....|....*....|....*..
gi 115527082 735 PEGqfiDSKKASEKLLGSIDIDHT-QYKFGHTKVFFK 770
Cdd:cd14904 620 HSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
102-770 |
9.94e-137 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 442.42 E-value: 9.94e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFML----TDRENQSILI 177
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 178 TGESGAGKTVNTKRVIQYFAtiavtgekkkeEVTSGKMQgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgT 257
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIM-----------ELCRGNSQ--LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-R 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 258 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEML-LITTNPYDYAFVSQGEITVPSI--DDQEELMa 334
Cdd:cd14889 149 NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYgLLDPGKYRYLNNGAGCKREVQYwkKKYDEVC- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 335 tdSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEY 413
Cdd:cd14889 228 --NAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 414 VTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLdtkQPRQYF------IGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd14889 306 IQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQACINLANEQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 488 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIEL-IEKPMGIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNF 566
Cdd:cd14889 383 LQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 567 QKPKPAKGKpeahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAGGGKKGGKKKGS 646
Cdd:cd14889 461 GKSRSKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSD 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 647 SF-----QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 721
Cdd:cd14889 537 NFnstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAE 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 115527082 722 FKQRYKVLnasaIPEGQFIDSKKASEKLLGSIDIdhTQYKFGHTKVFFK 770
Cdd:cd14889 617 FAERYKIL----LCEPALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
42-829 |
3.80e-134 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 440.62 E-value: 3.80e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 42 DPKESFVKATVQ-SREGGKVTAK---TEAGATVTVKDDQVF----PMNPPKYDkieDMAMMTHLHEPAVLYNLKERYAAW 113
Cdd:PTZ00014 47 DPDLMFAKCLVLpGSTGEKLTLKqidPPTNSTFEVKPEHAFnansQIDPMTYG---DIGLLPHTNIPCVLDFLKHRYLKN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 114 MIYTYSGLFCVTVNPYKWLPVYNAEVVTAYR-GKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRV 192
Cdd:PTZ00014 124 QIYTTADPLLVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 193 IQYFATIAvtgekkkeevtSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLE 272
Cdd:PTZ00014 204 MRYFASSK-----------SGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 273 KSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIEILGFTSDERVSI 352
Cdd:PTZ00014 273 KSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 353 YKLTGAVMHYGNMKFKQKQREEQAE-----PDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAV 427
Cdd:PTZ00014 352 FSILSGVLLLGNVEIEGKEEGGLTDaaaisDESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLK 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 428 GALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKE 507
Cdd:PTZ00014 432 DSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDE 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 508 GI-----EWTfidfgmDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKSNNFqkpKPAKGKPEAHFS 581
Cdd:PTZ00014 512 GIsteelEYT------SNESVIDLLcGKGKSVLSILEDQCLAPGGTDEKFVSSCNTN-LKNNPKY---KPAKVDSNKNFV 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 582 LIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgatgaeaeagGGKKGGKKKGSSFQTVSALFRENLNK 661
Cdd:PTZ00014 582 IKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLF-----------EGVEVEKGKLAKGQLIGSQFLNQLDS 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 662 LMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAsAIPEGQFID 741
Cdd:PTZ00014 651 LMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDL-AVSNDSSLD 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 742 SKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDEKLAQ---LITRTQAMCRGFLARveyQKMVERRESIFCI 818
Cdd:PTZ00014 730 PKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwepLVSVLEALILKIKKK---RKVRKNIKSLVRI 806
|
810
....*....|.
gi 115527082 819 QYNVRAFMNVK 829
Cdd:PTZ00014 807 QAHLRRHLVIA 817
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
100-770 |
6.00e-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: 428.31 E-value: 6.00e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAA--WMIYTYSGLFCVTVNPYKWLPvyNAEVvTAYRGKKRQEAPPHIFSISDNAYQFMLTDRE---NQS 174
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 175 ILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQG------TLEDQIISANPLLEAFGNAKTVRNDNSSRFG 248
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 249 KFIRIHFGTTG-KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQ-GEITVPSI 326
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLL-LSPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 327 DDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREE----QAEPDGTEVADKAAYLQNLNSADLLKAL 402
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 403 CYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFD-FNSLEQLCI 481
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 482 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHl 560
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 561 GKSNNFQKPKPaKGKPEAhFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMktlallfvgatgaeaeagggkkg 640
Cdd:cd14891 475 KRHPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSAK----------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 641 gkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 720
Cdd:cd14891 530 --------------FSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYA 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 115527082 721 DFKQRYKVLNASAI------PEGQFIdskkasEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14891 596 ELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
100-727 |
4.15e-131 |
|
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: 428.54 E-value: 4.15e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYR--------GKKRQEAPPHIFSISDNAYQFML-TD 169
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTledQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVEIGK---RILQTNPILESFGNAQTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEmLLITTNPYDYAFVSQGEIT-----VP 324
Cdd:cd14902 158 FIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD-LLGLQKGGKYELLNSYGPSfarkrAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 325 SIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKqkqrEEQAEPDGTEVA-------DKAAYLQNLNSAD 397
Cdd:cd14902 237 ADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFT----AENGQEDATAVTaasrfhlAKCAELMGVDVDK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 398 LLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-------TKQPRQYF--IGVLDIAGF 468
Cdd:cd14902 313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsISDEDEELatIGILDIFGF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 469 EIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKAT 547
Cdd:cd14902 393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 548 DTSFKNKLYEQHLgksnnfqkpkpakgkPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGA 627
Cdd:cd14902 472 NQALSTKFYRYHG---------------GLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 628 TGAEAEAGGGKKGGKKKGSSFQ-TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGI 706
Cdd:cd14902 537 NRDSPGADNGAAGRRRYSMLRApSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAV 616
|
650 660
....*....|....*....|.
gi 115527082 707 RICRKGFPSRILYADFKQRYK 727
Cdd:cd14902 617 RIARHGYSVRLAHASFIELFS 637
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
100-770 |
1.25e-130 |
|
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: 425.86 E-value: 1.25e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYR--GKKRQ---EAP----PHIFSISDNAYQFMLTD- 169
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELG-KLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIM---SNKKPDLIEMLLITTN----PYDYAFVSQGEI- 321
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggDEEEHEKYEFHDGITGglqlPNEFHYTGQGGAp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 322 TVPSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQRE---EQAEPDGTEVADKAAYLQNLNSADL 398
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDgaaEIAEEGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 399 LKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNK 554
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 555 LYEQHLGKSNN-------FQKPKPAKGKpeAHFSLIHYAGTVDYNI-AGWLDKNKDPLNETVVGLYQKSAMktlallfvg 626
Cdd:cd14908 479 LYETYLPEKNQthsentrFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESGQQ--------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 627 atgaeaeagggkkggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGI 706
Cdd:cd14908 548 ----------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAV 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 707 RICRKGFPSRILYADFKQRYKVLnASAIPE----------------GQFIDSKKASEKLLGSIDID----HTQYKFGHTK 766
Cdd:cd14908 600 RVARSGYPVRLPHKDFFKRYRML-LPLIPEvvlswsmerldpqklcVKKMCKDLVKGVLSPAMVSMknipEDTMQLGKSK 678
|
....
gi 115527082 767 VFFK 770
Cdd:cd14908 679 VFMR 682
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
100-770 |
4.93e-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: 406.30 E-value: 4.93e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRG-KKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 179 GESGAGKTVNTKRVIQYFATIAvtgekkkeevtSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAK-----------SGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTnPYDYAFVSQGEITVPSIDDQEELMATDSA 338
Cdd:cd14876 150 GGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLG-LKEYKFLNPKCLDVPGIDDVADFEEVLES 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 339 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQ-----AEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEY 413
Cdd:cd14876 229 LKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 414 VTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14876 309 IEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 494 HHMFVLEQEEYKKEGI-----EWTfidfgmDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKSNnfq 567
Cdd:cd14876 389 DIVFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSNG--- 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 568 KPKPAKGKPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgatgaeaeagGGKKGGKKKGSS 647
Cdd:cd14876 459 KFKPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALF-----------EGVVVEKGKIAK 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 648 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14876 528 GSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFK 607
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 115527082 728 VLNAsAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14876 608 FLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-770 |
6.88e-123 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 404.72 E-value: 6.88e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNaevVTAYRGK--KRQEAPPHIFSISDNAYQFMLT-------D 169
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 170 RENQSILITGESGAGKTVNTKRVIQYfatIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNY---LAESSKHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 250 FIRIHFG-----TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPD-LIEMLLITTNPYDYAFVSQGEITV 323
Cdd:cd14895 155 FVRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGGQCYQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 324 --PSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA----------------- 384
Cdd:cd14895 235 rnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqh 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 385 -DKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQY----- 458
Cdd:cd14895 315 lDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 459 ------FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPM 531
Cdd:cd14895 395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 532 GIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKpaKGKPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGL 611
Cdd:cd14895 474 GIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 612 YQKSAMKTLALLFVGATGAEAEAGGGKKGGKKKGSSFQT---VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAM 688
Cdd:cd14895 551 LGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSsvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQF 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 689 EHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASaipegQFIDSKKASEkLLGSIDIDHTQykFGHTKVF 768
Cdd:cd14895 631 DMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAA-----KNASDATASA-LIETLKVDHAE--LGKTRVF 702
|
..
gi 115527082 769 FK 770
Cdd:cd14895 703 LR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
100-770 |
1.96e-119 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 392.99 E-value: 1.96e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIavtgEKKKEEVTSGKMQGTLedqiisanPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 259
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----YQDQTEDRLRQPEDVL--------PILESFGHAKTILNANASRFGQVLRLHL-QHG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEI-TVPSIDDQEELMATDSA 338
Cdd:cd14896 148 VIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 339 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQ---AEPDGTEVADKAAYLQnlNSADLLKALCYPRVKVGN-EYV 414
Cdd:cd14896 227 LQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevaAVSSWAEIHTAARLLQ--VPPERLEGAVTHRVTETPyGRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 415 TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYF--IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 492
Cdd:cd14896 305 SRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 493 NHHMFVLEQEEYKKEGIEWTFIDfGMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKp 571
Cdd:cd14896 385 SQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQ- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 572 akgKPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAGGGKkggkkkgssfqTV 651
Cdd:cd14896 462 ---LPLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP-----------TL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 652 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 731
Cdd:cd14896 528 ASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGS 607
|
650 660 670
....*....|....*....|....*....|....*....
gi 115527082 732 SAIPEgqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14896 608 ERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-729 |
1.03e-112 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 374.19 E-value: 1.03e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKR-QEAPPHIFSISDNAYQFMLTDRE--NQSILI 177
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 178 TGESGAGKTVNTKRVIQYFATIAVTgekkKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 257
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAAS----PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 258 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPyDYAFVSQGEITVpsidDQEELMATDS 337
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGA-AFSWLPNPERNL----EEDCFEVTRE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 338 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEyv 414
Cdd:cd14880 234 AMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQ-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 415 tkgqtvQQVYNAV----------GALAKAVYDKMFLWMVTRINQQLDTKQPR-QYFIGVLDIAGFEIFDFNSLEQLCINF 483
Cdd:cd14880 312 ------QQVFKKPcsraecdtrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 484 TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGK 562
Cdd:cd14880 386 ANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 563 SNNFQKPKPAKgkpEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgatGAEAEAGGGKKGGK 642
Cdd:cd14880 465 NPCLGHNKLSR---EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLF----PANPEEKTQEEPSG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 643 KKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 722
Cdd:cd14880 538 QSRAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNF 617
|
....*..
gi 115527082 723 KQRYKVL 729
Cdd:cd14880 618 VERYKLL 624
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-732 |
1.35e-109 |
|
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: 367.38 E-value: 1.35e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKR-QEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFatIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTT 258
Cdd:cd14906 83 ESGSGKTEASKTILQYL--INTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 259 GKLASADIETYLLEKSRVTFQL-KAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQ-------- 329
Cdd:cd14906 161 GKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFKSQssnknsnh 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 330 -------EELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQ---REEQAEPDGTEVADKAAYLQNLNSADLL 399
Cdd:cd14906 241 nnktesiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 400 KALCYPRVKVGNE--YVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRIN----QQLDTKQPRQY-------FIGVLDIA 466
Cdd:cd14906 321 QALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINrkfnQNTQSNDLAGGsnkknnlFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 467 GFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPK 545
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 546 ATDTSFKNKlYEQHLGKSNNFQKPKPAKGKpeahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFv 625
Cdd:cd14906 480 GSEQSLLEK-YNKQYHNTNQYYQRTLAKGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLF- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 626 gatgaeAEAGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEG 705
Cdd:cd14906 554 ------QQQITSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNT 627
|
650 660
....*....|....*....|....*..
gi 115527082 706 IRICRKGFPSRILYADFKQRYKVLNAS 732
Cdd:cd14906 628 IKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
106-770 |
3.85e-108 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 360.74 E-value: 3.85e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQ-----EAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVtsgkmqgtledqIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTDVQSL------------ILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYdYAFVSQGEI-TVPSIDDQEELMATDSA 338
Cdd:cd14886 155 GLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASKCyDAPGIDDQKEFAPVRSQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 339 IEILgFTSDERVSIYKLTGAVMHYGNMKFKQKQR---EEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVT 415
Cdd:cd14886 234 LEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETII 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 416 KGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 495
Cdd:cd14886 313 SPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 496 MFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLyEQHLgKSNNFQkpkPAKG 574
Cdd:cd14886 393 VFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSFI---PGKG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 575 KpEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgatgaeaeaGGGKKGGKKKGSSFqtVSAL 654
Cdd:cd14886 467 S-QCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAF----------SDIPNEDGNMKGKF--LGST 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 655 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL---NA 731
Cdd:cd14886 534 FQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 115527082 732 SAIPEGQfiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14886 614 SSQNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
101-727 |
4.45e-105 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 354.02 E-value: 4.45e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAY----------RGKKRQEAPPHIFSISDNAYQFMLTD 169
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKM-----QGTLEDQIISANPLLEAFGNAKTVRNDNS 244
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPpaspsRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 245 SRFGKFIRIHF-GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNK----KPDLIEMLLITTNPYDYAFVSQG 319
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 320 EITV--PSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQ--KQREEQAEPDGTEVA----------D 385
Cdd:cd14899 242 LCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 386 KAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQL--------------- 450
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 451 DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-K 529
Cdd:cd14899 402 DDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 530 PMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVV 609
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 610 GLYQKSAMKTLALLFVGATGAEAEAGGGKKGGKKKGSSFQ-------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNET 682
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAksaiaavSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 115527082 683 KTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-770 |
1.41e-102 |
|
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: 345.26 E-value: 1.41e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 102 VLYNLKERYAAWMI-YTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEA-PPHIFSISDNAY-QFMLTDRENQSILIT 178
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 179 GESGAGKTVNTKRVIQYFAtiavtgeKKKEEVTSGKMQGTLEDQIIS----ANPLLEAFGNAKTVRNDNSSRFGKFIRIH 254
Cdd:cd14875 83 GESGSGKTENAKMLIAYLG-------QLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 255 F-GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITV------PSID 327
Cdd:cd14875 156 FdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 328 DQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQnLNSADLLKalCYpRV 407
Cdd:cd14875 236 DAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFLTACRLLQ-LDPAKLRE--CF-LV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 408 KVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQ----QLDTKQPRqyFIGVLDIAGFEIFDFNSLEQLCINF 483
Cdd:cd14875 312 KSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNAsitpQGDCSGCK--YIGLLDIFGFENFTRNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 484 TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGK 562
Cdd:cd14875 390 ANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 563 SNNFQKPKPAKGKpeaHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFVGATGAEAEAgggkkggk 642
Cdd:cd14875 469 SPYFVLPKSTIPN---QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRK-------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 643 kkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 722
Cdd:cd14875 538 ------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQF 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 115527082 723 -KQRYKVLNASAIPEGQFIDSKKASEKLLGS----IDIDHTQYKFGHTKVFFK 770
Cdd:cd14875 612 cRYFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-770 |
2.95e-101 |
|
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: 341.98 E-value: 2.95e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 182 GAGKTVNTKRVIQYFATIAVTGEKKkeeVTSGKMQgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAGSVGGV---LSVEKLN--------AALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFvsqgeITVPSIDDQE------ELMAT 335
Cdd:cd01386 152 ASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF-----GIVPLQKPEDkqkaaaAFSKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 336 DSAIEILGFTSDERVSIYKLTGAVMHYGN---MKFKQKQREEQAEPdgtEVADKAAYLQNLNSADLLKALCYPRVKVGNE 412
Cdd:cd01386 227 QAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 413 YVT---------------KGQTVQQvynAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN--- 474
Cdd:cd01386 304 QSTtssgqesparsssggPKLTGVE---ALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsq 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 475 ---SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---------------PMGIFSI 536
Cdd:cd01386 381 rgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 537 LEEECMFPKATDTSFKNKLYeQHLGKS--NNFQKPKPAKGKPEaHFSLIHYAGT--VDYNIAGWLDKNK-DPLNETVVGL 611
Cdd:cd01386 461 LDEEALYPGSSDDTFLERLF-SHYGDKegGKGHSLLRRSEGPL-QFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQL 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 612 YQKSAMKTLALlfvgatgaeaeagggkkggkkKGSSFqtvSALFRENLNKLMTNLRSTHPHFVRCIIPN------ETKTP 685
Cdd:cd01386 539 LQESQKETAAV---------------------KRKSP---CLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTS 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 686 GAMEHELVLH------QLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL----NASAIPEGQFIDSKKASEKLLGSIDI 755
Cdd:cd01386 595 SPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLapplTKKLGLNSEVADERKAVEELLEELDL 674
|
730
....*....|....*
gi 115527082 756 DHTQYKFGHTKVFFK 770
Cdd:cd01386 675 EKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
101-770 |
5.40e-92 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 314.06 E-value: 5.40e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYR---GKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 177
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 178 TGESGAGKTVNTKRVIQYFATiavtgekkkeevTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 257
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTC------------RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 258 TGK-LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQGE----ITVPSIDDQEEL 332
Cdd:cd14878 150 RKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTMredvSTAERSLNREKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 333 MATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNE 412
Cdd:cd14878 229 AVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 413 YVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRIN----QQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14878 309 MIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclqSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 489 QQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSNN-- 565
Cdd:cd14878 389 HHYINEVLFLQEQTECVQEGVTMeTAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKL--QSLLESSNtn 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 566 --FQKPKPAKGKPE-----AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgatgaeaeagggk 638
Cdd:cd14878 467 avYSPMKDGNGNVAlkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF-------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 639 kggkkkGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 718
Cdd:cd14878 533 ------QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLS 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 115527082 719 YADFKQRYKVLnASAIPEGQfidsKKASEKLLGSIDIDHTQ---YKFGHTKVFFK 770
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 ... |
101-733 |
2.93e-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: 309.52 E-value: 2.93e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKwlPVYNAEVVTAYRgKKRQEAPPHIFSISDNAYQFMLTdRENQSILITGE 180
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVIQYFatiavtgekkkeeVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgtTGK 260
Cdd:cd14898 78 SGSGKTENAKLVIKYL-------------VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpdliemLLITTNPYDYAFVSQGEITVpsIDDQEELMATDSAIE 340
Cdd:cd14898 143 ITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSAMK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 341 ILGFTSDErvSIYKLTGAVMHYGNMKFKQkqrEEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd14898 215 SLGIANFK--SIEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 421 QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQyfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14898 290 KQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAK 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 501 QEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKAT--DTSFKNKLYEQHLGKSNNFQKPKpakgkpea 578
Cdd:cd14898 368 QGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNGFINTKARDKIK-------- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 579 hfsLIHYAGTVDYNIAGWLDKNKDPLNETVVGlyqksamktlallfvgatgaeaeagggkKGGKKKGSSFQTVSALFREN 658
Cdd:cd14898 439 ---VSHYAGDVEYDLRDFLDKNREKGQLLIFK----------------------------NLLINDEGSKEDLVKYFKDS 487
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115527082 659 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 733
Cdd:cd14898 488 MNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-770 |
8.94e-87 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 298.08 E-value: 8.94e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYnaevVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 182 GAGKTVNTKRVIQYFatiaVTGEKKKEEVTSgkmqgTLEDqiisANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14937 79 GSGKTEASKLVIKYY----LSGVKEDNEISN-----TLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEE---LMATDSA 338
Cdd:cd14937 146 VSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDfgnLMISFDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 339 IEIlgftSDERVSIYKLTGAVMHYGNMKFKQ-----KQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEY 413
Cdd:cd14937 225 MNM----HDMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 414 VTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14937 301 IEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 494 HHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIEKPMGIFSILEEECMFPKATDTSFKNkLYEQHLGKSNNFQKPKPAK 573
Cdd:cd14937 381 YIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESIVS-VYTNKFSKHEKYASTKKDI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 574 GKpeaHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgatgaeaeaggGKKGGKKKGSSFQTVSA 653
Cdd:cd14937 459 NK---NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLY------------EDVEVSESLGRKNLITF 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 654 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRIcRKGFPSRILYADFKQRYKVLNASA 733
Cdd:cd14937 524 KYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYST 602
|
650 660 670
....*....|....*....|....*....|....*..
gi 115527082 734 IPEGQFIDSKKASEKLLGSIDIDhtQYKFGHTKVFFK 770
Cdd:cd14937 603 SKDSSLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
100-770 |
9.68e-86 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 297.72 E-value: 9.68e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAA--------WMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRE 171
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 172 NQSILITGESGAGKTVNTKRVIQYFAtiAVTGEKKkeevtsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 251
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLA--AVSDRRH------GADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKML 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 252 RIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtnpYDYafvsqgeitvPSIDDQEE 331
Cdd:cd14887 153 LLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAG---EGD----------PESTDLRR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 332 LMATDSAIEILGftsDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADK---AAYLQNLNS----- 395
Cdd:cd14887 220 ITAAMKTVGIGG---GEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADrshSSEVKCLSSglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 396 -------ADLLKALCYPRVKVGNEYVTKGQTVQQV------YNAVGALA------KAVYDKMFLWMVTRINQQLDTKQPR 456
Cdd:cd14887 297 easrkhlKTVARLLGLPPGVEGEEMLRLALVSRSVretrsfFDLDGAAAardaacKNLYSRAFDAVVARINAGLQRSAKP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 457 QY--------------FIGVLDIAGFEIF---DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFI----D 515
Cdd:cd14887 377 SEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsafP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 516 FGMDLAAC--------IELIEKP--------------MGIFSILEEE-CMFPKATDTSFKNKLYEQHLGK----SNNFQK 568
Cdd:cd14887 457 FSFPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKN 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 569 PKPAKGKPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYqkSAMKTLALLfvgatgaeaEAGGGKKGGKKKGSSF 648
Cdd:cd14887 537 ITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF--LACSTYTRL---------VGSKKNSGVRAISSRR 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 649 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd14887 606 STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYET 685
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 115527082 729 LNASAIPEgqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14887 686 KLPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
106-769 |
1.28e-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: 292.15 E-value: 1.28e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 106 LKERYAAWMIYTY---SGLfcVTVNPYKWLPVYNAEVVTAYR-------GKKRQEAPPHIFSISDNAYQFMLTDRENQSI 175
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 176 LITGESGAGKTVNTKRVIQYFATIAVTGEKkkeevtsgkmqGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 254
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSSHSKK-----------GTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 255 FGTTGKLASADIETYLLEKSRVTfQLKA-ERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFV--SQGEITV--PSIDDQ 329
Cdd:cd14879 157 FNERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGL-DDPSDYALLasYGCHPLPlgPGSDDA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 330 E---ELMAtdsAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQNLNSADLLKALCY 404
Cdd:cd14879 235 EgfqELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 405 PRVKVGNEYVTkgqtvqqVY-NAVGA------LAKAVYDKMFLWMVTRINQQL-DTKQPRQYFIGVLDIAGFEIFD---F 473
Cdd:cd14879 312 KTKLVRKELCT-------VFlDPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSstgG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 474 NSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEEC-MFPKATDTSF 551
Cdd:cd14879 385 NSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDEQM 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 552 KNKLYEQHLGKSNNFQKPKPAKGKPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNetvvglyqksamktlallfvgatgae 631
Cdd:cd14879 464 LEALRKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLS-------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 632 aeagggkkggkkkgSSFqtVSAL-----FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGI 706
Cdd:cd14879 518 --------------PDF--VNLLrgatqLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELA 581
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115527082 707 RICRKGFPSRILYADFKQRYKvlnasaiPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFF 769
Cdd:cd14879 582 ARLRVEYVVSLEHAEFCERYK-------STLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
100-718 |
1.92e-75 |
|
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: 266.39 E-value: 1.92e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEA-------PPHIFSISDNAYQFMLTDRE 171
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 172 NQSILITGESGAGKTVNTKRVIQYFATIavtgekkkeevtSGKMQGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKF 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI------------QTDSQMTeRIDKLIYINNILESMSNATTIKNNNSSRCGRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 251 IRIHFGT---------TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGE- 320
Cdd:cd14884 149 NLLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEs 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 321 -----------ITVPSIDDQEELMATDSA-----IEILGFTS-DERV--SIYKLTGAVMHYGNMKFKQkqreeqaepdgt 381
Cdd:cd14884 229 hqkrsvkgtlrLGSDSLDPSEEEKAKDEKnfvalLHGLHYIKyDERQinEFFDIIAGILHLGNRAYKA------------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 382 evadkAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRIN---------QQLDT 452
Cdd:cd14884 297 -----AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekDESDN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 453 KQPRQY---FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDfgmdLAACIELIEK 529
Cdd:cd14884 372 EDIYSIneaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDV----APSYSDTLIF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 530 PMGIFSILEEECMFP----KATDTSFKNKLY----EQHLGKSNNFQK--PKPAKGKPEAH------FSLIHYAGTVDYNI 593
Cdd:cd14884 448 IAKIFRRLDDITKLKnqgqKKTDDHFFRYLLnnerQQQLEGKVSYGFvlNHDADGTAKKQnikkniFFIRHYAGLVTYRI 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 594 AGWLDKNKDPLNETVVGLYQKSAMKTLallfvgatgaeaeaggGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHF 673
Cdd:cd14884 528 NNWIDKNSDKIETSIETLISCSSNRFL----------------REANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYY 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 115527082 674 VRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 718
Cdd:cd14884 592 IRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
101-750 |
3.02e-70 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 249.65 E-value: 3.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPvyNAEVVTAYRGKKRQeapPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 181 SGAGKTVNTKRVI-QYFatiavtgekkkeEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 259
Cdd:cd14881 77 SGSGKTYASMLLLrQLF------------DVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPD-LIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 338
Cdd:cd14881 144 ALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEeRVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 339 IEILG--FTSDERVsiyklTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLqNLNSADLLKALcYPRVKVgneyvTK 416
Cdd:cd14881 224 LGILGipFLDVVRV-----LAAVLLLGNVQFIDGGGLEVDVKGETELKSVAALL-GVSGAALFRGL-TTRTHN-----AR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 417 GQTVQQVYNA------VGALAKAVYDKMFLWMVTRINQQLD-----TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd14881 292 GQLVKSVCDAnmsnmtRDALAKALYCRTVATIVRRANSLKRlgstlGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 486 EKLQQFFNHHMFVLEQEEYKKEGIEwTFIDFG-MDLAACIELIEK-PMGIFSILEEECMfPKATDTSFKNKLYEQHlgKS 563
Cdd:cd14881 372 ETMQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQH--RQ 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 564 NN-FQKPKPAKGKpeaHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKtlallFvgatgaeaeagggkkggk 642
Cdd:cd14881 448 NPrLFEAKPQDDR---MFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCN-----F------------------ 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 643 kkgsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 722
Cdd:cd14881 502 ----GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAF 577
|
650 660
....*....|....*....|....*...
gi 115527082 723 KQRYKVLnASAIPEGQFIDSKKASEKLL 750
Cdd:cd14881 578 NARYRLL-APFRLLRRVEEKALEDCALI 604
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
101-729 |
1.49e-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: 235.54 E-value: 1.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYrgkkrqeappHIFSISDNAYQFMLTDREN-QSILITG 179
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 180 ESGAGKTVNTKRVIQYFATiavtgeKKKEEVTSgkmqgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14874 72 ESGSGKSYNAFQVFKYLTS------QPKSKVTT--------KHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14874 138 LTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLEDAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 340 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKqREEQAEPDGTEVADKA-----AYLQNLNSADLLKALCyPRVKVGNEYv 414
Cdd:cd14874 217 HVLGFSDDHCISIYKIISTILHIGNIYFRTK-RNPNVEQDVVEIGNMSevkwvAFLLEVDFDQLVNFLL-PKSEDGTTI- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 415 tkgqTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLdtKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14874 294 ----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHL--KCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 494 HHMFVLEQEEYKKEGIEwtfIDFGM----DLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSnNFQK 568
Cdd:cd14874 368 KHSFHDQLVDYAKDGIS---VDYKVpnsiENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-SYGK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 569 pkpAKGKPEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgatgaeaeagggKKGGKKKGSSF 648
Cdd:cd14874 444 ---ARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLF-------------ESYSSNTSDMI 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 649 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd14874 508 VSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRC 587
|
.
gi 115527082 729 L 729
Cdd:cd14874 588 L 588
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
102-770 |
1.32e-64 |
|
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: 233.09 E-value: 1.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 182 GAGKTVNTKRVIQYFATIavtgekkkeevtsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14882 83 YSGKTTNARLLIKHLCYL-------------GDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMS--NKKPDLIEMLLITTNPYDYAFVSQGeiTVPSI------DDQEELM 333
Cdd:cd14882 150 SGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPE--VPPSKlkyrrdDPEGNVE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 334 ATDSAIEIL---GFTSDERVSIYKLTGAVMHYGNMKFKQKQREeqAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVG 410
Cdd:cd14882 228 RYKEFEEILkdlDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLIKG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 411 NEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTkqPR-----QYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd14882 306 GSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVNTLN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 486 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEecmfpkaTDTSFKNKLYEQHLGKSNN 565
Cdd:cd14882 384 EQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-------ASRSCQDQNYIMDRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 566 FQKPKPAKGKpeaHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLALLFvgatgaeaeagggkkgGKKKG 645
Cdd:cd14882 457 SQFVKKHSAH---EFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMF----------------TNSQV 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 646 SSFQTVSALFR----ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 721
Cdd:cd14882 518 RNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQE 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 115527082 722 FKQRYKVLnasAIPEGQFIDSKKASEKLLgSIDIDHTQYKFGHTKVFFK 770
Cdd:cd14882 598 FLRRYQFL---AFDFDETVEMTKDNCRLL-LIRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
106-713 |
1.50e-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: 233.83 E-value: 1.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 184
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 185 KTVNTKRVIQYFATIAVTGEKkkeevtsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASA 264
Cdd:cd14905 85 KSENTKIIIQYLLTTDLSRSK------------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 265 DIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPDLIEMLLITTNPYDYaFVSQGEITVPSIDDQEELMATDSAIEILG 343
Cdd:cd14905 153 KLYSYFLDENRVTYQNKGERNFHIFYQFLKGiTDEEKAAYQLGDINSYHY-LNQGGSISVESIDDNRVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 344 FTSDERVSIYKLTGAVMHYGNMKFKQKQREeqaepdgTEVADKAAYlqnlnsADLLKALCYPRVKVGNEYVT-KGQTVQQ 422
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRTLI------ESLSHNITFDSTKLENILISdRSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 423 VYNAVGALAKAVYDKMFLWMVTRINQQLdtkQPRQY--FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14905 299 AVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 501 QEEYKKEGIEW-TFIDFgMDLAACIELIEKpmgIFSILEEECMFPKATDTSFKNKLyEQHLGKSNNFQKpKPAKgkpeah 579
Cdd:cd14905 376 QREYQTERIPWmTPISF-KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL-QNFLSRHHLFGK-KPNK------ 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 580 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSAMKTLAL---LFVGATGAEAEAGGGKKGGKKKGSSFQTVSALFR 656
Cdd:cd14905 444 FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSrdgVFNINATVAELNQMFDAKNTAKKSPLSIVKVLLS 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 657 ------ENLNK-----------------------LMTNLRSTHP---------HFVRCIIPNETKTPGAMEHELVLHQLR 698
Cdd:cd14905 524 cgsnnpNNVNNpnnnsgggggggnsgggsgsggsTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIK 603
|
650
....*....|....*
gi 115527082 699 CNGVLEGIRICRKGF 713
Cdd:cd14905 604 SLCLLETTRIQRFGY 618
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
103-727 |
3.84e-63 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 231.40 E-value: 3.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQ----------EAPPHIFSISDNAYQFMLTDREN 172
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 173 QSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIR 252
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 253 IHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKK--PDLIEMLLITTNPYDYAFVSQG--EITVPSID- 327
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFALDa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 328 -DQEELMATDSAIEIlgfTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDG--TEVADKAAYL-----QNLNSADLL 399
Cdd:cd14893 244 rDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGAnsTTVSDAQSCAlkdpaQILLAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 400 KAlcYPRV------------KVGNEYVT--KGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQL----DTKQPRQYFIG 461
Cdd:cd14893 321 EV--EPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVIN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 462 -----VLDIAGFEIFD--FNSLEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEG--IEWTFIDFGMDLAACIELI 527
Cdd:cd14893 399 sqgvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 528 E-KPMGIFSILEEECMFPKATDTSFKNKLYEQH-----LGKSNNFQKPKPAKGKPEAHFSLI----HYAGTVDYNIAGWL 597
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNeavggLSRPNMGADTTNEYLAPSKDWRLLfivqHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 598 DKNKDPLNETVVGLYQKSAMKTLALLFVGA--TGAEAEAGGGKKGGKKKGSSFQTVSALFRENLN--------------K 661
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVGAAQmaAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadA 638
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115527082 662 LMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
122-253 |
9.01e-61 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 206.04 E-value: 9.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 122 FCVTVNPYKWLPVYNAEVV-TAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIA 200
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 115527082 201 VTGEKKKEE---VTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 253
Cdd:cd01363 81 FNGINKGETegwVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-768 |
1.17e-44 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 174.64 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYR-GKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 179 GESGAGKTVNTKRVIQYFA-----------TIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAyqvkgsrrlptNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 248 GKFIRIHFGTTgKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSID 327
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFL-KNIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 328 DQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGN-------------MKFKQKQRE----------EQAEPDGTEVA 384
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 385 DKAAYL-QNLNSADLLKALCYPRVK-VGNEYV-TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYF-- 459
Cdd:cd14938 319 VKNLLLaCKLLSFDIETFVKYFTTNyIFNDSIlIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININtn 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 460 -IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM--GIFSI 536
Cdd:cd14938 399 yINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFSL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 537 LEEECMfPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKPEAhFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSA 616
Cdd:cd14938 479 LENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 617 ---MKTLALLF--------VGATGAEAEAGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTP 685
Cdd:cd14938 557 neyMRQFCMFYnydnsgniVEEKRRYSIQSALKLFKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKRE 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 686 -GAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAsaipegqfiDSKKASEKLLGSIDIDHTQYKFGH 764
Cdd:cd14938 637 lCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMIGN 707
|
....
gi 115527082 765 TKVF 768
Cdd:cd14938 708 NMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1177-1935 |
4.82e-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: 4.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1177 KMRRdlEEATLQHEATAATLrKKHADSVAELGEQIDNLQRVKQKLEKEKsEMKMEIDDLASNMETVSKakgnlekmcRAL 1256
Cdd:TIGR02168 171 KERR--KETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERYK-ELKAELRELELALLVLRL---------EEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1257 EDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEeikaksalaha 1336
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI----------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1337 LQSSRHDcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKK------LAQRLQDAEEHVEA 1410
Cdd:TIGR02168 307 LRERLAN---LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaeleeLESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1411 VNAKCASLEKTKQRLQNEVEDLMIDVERtnaacaaLDKKQRNFDKILAEWKQKCEEthAELEASQKESRSLSTELFKIKN 1490
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLER-------LEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1491 AYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEA----------SLEHEEG 1560
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlseLISVDEG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1561 kiLRIQLE------LNQV---KSEVDRKIAEKDEEIDQMKR---------------NHIRIVESMQSTLDAEIRSRNDAI 1616
Cdd:TIGR02168 535 --YEAAIEaalggrLQAVvveNLNAAKKAIAFLKQNELGRVtflpldsikgteiqgNDREILKNIEGFLGVAKDLVKFDP 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1617 RLKKKMEGDLNEMEI--QLNHANRMAAEALRNYRNtqAILKDTQLHLDDAL-------------RSQE--DLKEQLAMVE 1679
Cdd:TIGR02168 613 KLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRI--VTLDGDLVRPGGVItggsaktnssileRRREieELEEKIEELE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1680 RRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEeka 1759
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE--- 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1760 kkaitdaammaEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELEGEVESEQKRNVE 1839
Cdd:TIGR02168 768 -----------ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-ALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1840 AVKGLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNVNLSKFRRIQHELEEAEERADIAES 1919
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
810
....*....|....*.
gi 115527082 1920 QVNKLRVKSREVHTKI 1935
Cdd:TIGR02168 916 ELEELREKLAQLELRL 931
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1028-1881 |
2.05e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 125.17 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1028 KIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQEStmdiendkQQLDEKLKKKEFEMSGLQSKIEDEQALgmQ 1107
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERY--------KELKAELRELELALLVLRLEELREELE--E 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1108 LQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATS---AQIEMNKKREAEFQKMRRDLEE 1184
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1185 ATLQHEATaatlRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIK 1264
Cdd:TIGR02168 324 QLEELESK----LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1265 TKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDtlvsqlsrgKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRhdc 1344
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELEELQEELERLEEALEELR--- 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1345 DLLREQYEEEQEAKAELQRAMSKANSEVAQwRTKYETDAIQRTEELEEAKKK------LAQRLQDAEEHVEAVNAKCASl 1418
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERL-QENLEGFSEGVKALLKNQSGLsgilgvLSELISVDEGYEAAIEAALGG- 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1419 ektkqRLQNEVedlMIDVERTNAACAALDKKQRNFDKILAE---WKQKCEETHAELEASQKESRSLSTELFKIKNAYE-- 1493
Cdd:TIGR02168 546 -----RLQAVV---VENLNAAKKAIAFLKQNELGRVTFLPLdsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRka 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1494 -----------ESLDQLETLKRENK-------------------------------NLQQEISDLTEQIAEGGKRIHELE 1531
Cdd:TIGR02168 618 lsyllggvlvvDDLDNALELAKKLRpgyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAELE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1532 KIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRkiaeKDEEIDQMKRNHIRIVESMQSTLDAEIRS 1611
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEAEIEELEERLEEA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1612 RNDAIRLKKKMEgdlnEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEE 1691
Cdd:TIGR02168 774 EEELAEAEAEIE----ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1692 LRATLEQtersrkiAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAE 1771
Cdd:TIGR02168 850 LSEDIES-------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1772 ELKKEQdtsAHLERMKKNLEQTVKDL--QHRLDEAEQLALK-GGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHE 1848
Cdd:TIGR02168 923 KLAQLE---LRLEGLEVRIDNLQERLseEYSLTLEEAEALEnKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELK 999
|
890 900 910
....*....|....*....|....*....|...
gi 115527082 1849 RKVKELTYQTEEDRKNILRLQDLVDKLQAKVKS 1881
Cdd:TIGR02168 1000 ERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
867-1746 |
2.78e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 121.70 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 867 LAKTEAKRKELEEKMVTlmqekndlqLQVQAEAdsladAEercdQLIKTKIQLEAKIKEV-TERAEDEEEINAELTAKKR 945
Cdd:TIGR02168 188 LDRLEDILNELERQLKS---------LERQAEK-----AE----RYKELKAELRELELALlVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 946 KLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLT 1025
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1026 KAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQALG 1105
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1106 MQLQKKIKELQarieeleeeIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEA 1185
Cdd:TIGR02168 410 ERLEDRRERLQ---------QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1186 TLQHEATAATLrkkhaDSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKmcrALEDQLSEIKT 1265
Cdd:TIGR02168 481 ERELAQLQARL-----DSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEA---ALGGRLQAVVV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1266 KEEEQQRLINDLTAQ----RARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSR 1341
Cdd:TIGR02168 553 ENLNAAKKAIAFLKQnelgRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLD 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1342 HDCDLLREQYEEEQEAKAELQR-----AMSKANSEVAQWRTKYET---DAIQRTEELEEAKKKLAQRLQDAEEHVEAVNA 1413
Cdd:TIGR02168 633 NALELAKKLRPGYRIVTLDGDLvrpggVITGGSAKTNSSILERRReieELEEKIEELEEKIAELEKALAELRKELEELEE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1414 KCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYE 1493
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1494 ESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVK 1573
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1574 SEVDRKIAEKDEEIDQMKRnhiriVESMQSTLDAEIRSRNDAIRlkkKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAI 1653
Cdd:TIGR02168 873 SELEALLNERASLEEALAL-----LRSELEELSEELRELESKRS---ELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1654 L-KDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEEL-RATLEqtersrkiAEQELLDASERVQLLHTQNTSLINTK 1731
Cdd:TIGR02168 945 LsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgPVNLA--------AIEEYEELKERYDFLTAQKEDLTEAK 1016
|
890
....*....|....*
gi 115527082 1732 KKLETDISQIQGEME 1746
Cdd:TIGR02168 1017 ETLEEAIEEIDREAR 1031
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
869-1593 |
2.79e-27 |
|
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: 121.33 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 869 KTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAED--EEEINA------EL 940
Cdd:TIGR02169 220 KREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRvkekigEL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 941 TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDK 1020
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1021 VNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIED 1100
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1101 EQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLS------------------------RELEEISER--- 1153
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEervrggraveevlkasiqgvhgtvAQLGSVGERyat 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1154 -LEEAGGA------------TSAQIEMNKKREA------EFQKMRRDLEEATLQHEATAAtlrkKHADSVAELGEQIDNL 1214
Cdd:TIGR02169 540 aIEVAAGNrlnnvvveddavAKEAIELLKRRKAgratflPLNKMRDERRDLSILSEDGVI----GFAVDLVEFDPKYEPA 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1215 QR-------VKQKLEKEKSEM---KM-----EIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTA 1279
Cdd:TIGR02169 616 FKyvfgdtlVVEDIEAARRLMgkyRMvtlegELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQS 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1280 QRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKA 1359
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1360 ELQRAMSKANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERT 1439
Cdd:TIGR02169 776 KLEEALNDLEARLSHSRIPEIQAEL---SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1440 NAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQ 1519
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1520 IAEGGKRIHELEKIK------KQVEQEKSELQAALEEAE-----ASLEHEEGKILRIQLELNQVKSEVDRK-IAEKDEEI 1587
Cdd:TIGR02169 933 LSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEpvnmlAIQEYEEVLKRLDELKEKRAKLEEERKaILERIEEY 1012
|
....*.
gi 115527082 1588 DQMKRN 1593
Cdd:TIGR02169 1013 EKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1314-1915 |
5.20e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.88 E-value: 5.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1314 QQIEELKRQ---------LEEEIKAKSALAHALQSsrhdcDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYEtdai 1384
Cdd:COG1196 200 RQLEPLERQaekaeryreLKEELKELEAELLLLKL-----RELEAELEELEAELEELEAELEELEAELAELEAELE---- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1385 qrteELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKC 1464
Cdd:COG1196 271 ----ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1465 EETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSEL 1544
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1545 QAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRsRNDAIRLKKKMEG 1624
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-LLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1625 DLNE------------------MEIQLNHANRMAAEALRNYRNTQAILKDTQlhldDALRSQEDLKEQLAmveRRANLLQ 1686
Cdd:COG1196 506 FLEGvkaalllaglrglagavaVLIGVEAAYEAALEAALAAALQNIVVEDDE----VAAAAIEYLKAAKA---GRATFLP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1687 AEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTkkkLETDISQIQGEMEDIIQEARNAEEKAKKA---- 1762
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL---LGRTLVAARLEAALRRAVTLAGRLREVTLegeg 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1763 ITDAAMMAEELKKEQDTSahLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVK 1842
Cdd:COG1196 656 GSAGGSLTGGSRRELLAA--LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115527082 1843 GLRKHERKVKELTYQTEEDRKNILRLQDLvDKLQAKVKSYKRQAEEAEeqsNVNLskfRRIQhELEEAEERAD 1915
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDL-EELERELERLEREIEALG---PVNL---LAIE-EYEELEERYD 798
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1145-1935 |
7.58e-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: 113.62 E-value: 7.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1145 RELEEISERLEEAggatsaQIEMNKKREaEFQKMRRDLEEAtlqhEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKE 1224
Cdd:TIGR02169 177 EELEEVEENIERL------DLIIDEKRQ-QLERLRREREKA----ERYQALLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1225 KSEMKMEIDDLASNMEtvskakgNLEKMCRALEDQLSEIKTK-----EEEQQRL---INDLTAQRARLQTESGEYSRQLD 1296
Cdd:TIGR02169 246 LASLEEELEKLTEEIS-------ELEKRLEEIEQLLEELNKKikdlgEEEQLRVkekIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1297 EKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRamskansEVAQWR 1376
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-------ELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1377 TKYEtDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVErtnaacaALDKKQRNFDKI 1456
Cdd:TIGR02169 392 EKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK-------KQEWKLEQLAAD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1457 LAEWKQKCEETHAELEASQKESRSLSTELfkiknayeeslDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELekiKKQ 1536
Cdd:TIGR02169 464 LSKYEQELYDLKEEYDRVEKELSKLQREL-----------AEAEAQARASEERVRGGRAVEEVLKASIQGVHGT---VAQ 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1537 VEQEKSELQAALEEAEAS------LEHEEGKILRIQ------------LELNQVKSE-VDRKIAEKDE---------EID 1588
Cdd:TIGR02169 530 LGSVGERYATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrrkagratfLPLNKMRDErRDLSILSEDGvigfavdlvEFD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1589 QMKRNHIR-------IVESMQSTldaeiRSRNDAIRLKKkMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHL 1661
Cdd:TIGR02169 610 PKYEPAFKyvfgdtlVVEDIEAA-----RRLMGKYRMVT-LEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERL 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1662 DDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVqllhtqntslintkKKLETDISQI 1741
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL--------------EELEEDLSSL 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1742 QGEMEdiiqearNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMkknleqtvkDLQHRLDEAEQLALKGgKKQIQKLEA 1821
Cdd:TIGR02169 750 EQEIE-------NVKSELKELEARIEELEEDLHKLEEALNDLEAR---------LSHSRIPEIQAELSKL-EEEVSRIEA 812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1822 RVRELEGEVESEQKRNVEAVKGLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNVNLSKFR 1901
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
810 820 830
....*....|....*....|....*....|....
gi 115527082 1902 RIQHELEEAEERADIAESQVNKLRVKSREVHTKI 1935
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
921-1807 |
9.86e-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: 113.24 E-value: 9.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 921 AKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKdIDDLELTLAKVE-----KEKHATENKVKNLTEEMAGLDETIAK 995
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 996 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAK-IKLEQQVDDLEGSLEQekkirmdlerakrkLEGDLKLAQESTMDIE 1074
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAEIAS--------------LERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1075 NDKQQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERL 1154
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1155 EEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRkkhaDSVAELGEQIDNLQRVKQKLEKEKSEMkmeidd 1234
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE----DKALEIKKQEWKLEQLAADLSKYEQEL------ 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1235 lasnmetvskakgnlekmcRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEkdtlvsqLSRGKQAFTQ 1314
Cdd:TIGR02169 472 -------------------YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEV-------LKASIQGVHG 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1315 QIEELKRQLEEEIKA-KSALAHALQSSRHDCDLLRE---QYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEEL 1390
Cdd:TIGR02169 526 TVAQLGSVGERYATAiEVAAGNRLNNVVVEDDAVAKeaiELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1391 EEAKKKLAQRLQDAEEHVEAVNakcaSLEkTKQRLQNEVEDLMID---VERTNAACAALDKKQRNFDKILAEwKQKCEET 1467
Cdd:TIGR02169 606 VEFDPKYEPAFKYVFGDTLVVE----DIE-AARRLMGKYRMVTLEgelFEKSGAMTGGSRAPRGGILFSRSE-PAELQRL 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1468 HAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAA 1547
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1548 LEEAEASLEHEEGKILRIQLELNQVKSEVDR-KIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDL 1626
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1627 NEM-EIQLNHANRMAAEALRN--YRNTQAILKDTQLHLddalrsqEDLKEQLAMVERRANLLQAEIEELRATLEQTERSR 1703
Cdd:TIGR02169 840 EQRiDLKEQIKSIEKEIENLNgkKEELEEELEELEAAL-------RDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1704 KIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQgeMEDIIQEARNAEEKAKKAITDAAMMA-EELKKEQDTSAH 1782
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL--SLEDVQAELQRVEEEIRALEPVNMLAiQEYEEVLKRLDE 990
|
890 900
....*....|....*....|....*
gi 115527082 1783 LERMKKNLEQTVKDLQHRLDEAEQL 1807
Cdd:TIGR02169 991 LKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
844-1612 |
2.73e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 111.69 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 844 LKSAETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKI 923
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 924 KEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKAL 1003
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1004 QEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQ---- 1079
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQeele 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1080 -LDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISER----- 1153
Cdd:TIGR02168 458 rLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDegyea 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1154 -LEEAGGATSAQIEMNKKREAefqkmrRDLEEATLQHEATAATL----RKKHADSVAELGEQIDNLQRVKQKL-EKEKSE 1227
Cdd:TIGR02168 538 aIEAALGGRLQAVVVENLNAA------KKAIAFLKQNELGRVTFlpldSIKGTEIQGNDREILKNIEGFLGVAkDLVKFD 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1228 MKME------------IDDLASNMETVSK---------------------AKGNLEKMCRALEDQlSEIKTKEEEQQRLI 1274
Cdd:TIGR02168 612 PKLRkalsyllggvlvVDDLDNALELAKKlrpgyrivtldgdlvrpggviTGGSAKTNSSILERR-REIEELEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1275 NDLTAQRARLQtesgEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEE 1354
Cdd:TIGR02168 691 EKIAELEKALA----ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1355 QEAKAELQRAMSKANSEVAQWRtkyetdaiQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMI 1434
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELE--------AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1435 DVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEIS 1514
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1515 DLTEQIAEGGKRIHELE-KIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR-------------KI 1580
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEvRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaieeyeEL 998
|
810 820 830
....*....|....*....|....*....|....*
gi 115527082 1581 AEKDEEIDQMKRNHIRIVESMQST---LDAEIRSR 1612
Cdd:TIGR02168 999 KERYDFLTAQKEDLTEAKETLEEAieeIDREARER 1033
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1123-1913 |
1.23e-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: 109.39 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1123 EEEIEAERASRAKAEKQRSDLSRELEEISERLEEaggatsAQIEMNKKReaEFQKMRRDLEEAtlqhEATAATLRKKHAD 1202
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLER------LRREREKAE--RYQALLKEKREY----EGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1203 svaelgEQIDNLQRVKQKLEKEKSEMKMEIDDlasnmetvskakgnLEKMCRALEDQLSEIKTK-----EEEQQRL---I 1274
Cdd:TIGR02169 237 ------RQKEAIERQLASLEEELEKLTEEISE--------------LEKRLEEIEQLLEELNKKikdlgEEEQLRVkekI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1275 NDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEE 1354
Cdd:TIGR02169 297 GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1355 QEAKAELQRamskansEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMI 1434
Cdd:TIGR02169 377 DKEFAETRD-------ELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1435 DVErtnaacaALDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTElfkiknayeesLDQLETLKRENKNLQQEIS 1514
Cdd:TIGR02169 449 EIK-------KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE-----------LAEAEAQARASEERVRGGR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1515 DLTEQIAEGGKRIHELekiKKQVEQEKSELQAALEEAEAS------LEHEEGKILRIQ------------LELNQVKSE- 1575
Cdd:TIGR02169 511 AVEEVLKASIQGVHGT---VAQLGSVGERYATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrrkagratfLPLNKMRDEr 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1576 VDRKIAEKDE---------EIDQMKRNHIR-------IVESMQS-----------TLDAEI-----------RSRNDAIR 1617
Cdd:TIGR02169 588 RDLSILSEDGvigfavdlvEFDPKYEPAFKyvfgdtlVVEDIEAarrlmgkyrmvTLEGELfeksgamtggsRAPRGGIL 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1618 LKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLE 1697
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1698 QTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDIS-----QIQGEMEDIIQEARNAEEKAKKaiTDAAMMAEE 1772
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLRE--IEQKLNRLT 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1773 LKKEQdtsahLERMKKNLEQTVKDLQHRLDE--AEQLALKGGKK----QIQKLEARVRELEGEVESEQKRNVEAVKGLRK 1846
Cdd:TIGR02169 826 LEKEY-----LEKEIQELQEQRIDLKEQIKSieKEIENLNGKKEeleeELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115527082 1847 HERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNVNLSkFRRIQHELEEAEER 1913
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
980-1798 |
1.67e-23 |
|
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: 108.99 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 980 KNLTEEMAGldetIAKLTKEKKalqEAHQQ---TLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIR------- 1049
Cdd:TIGR02168 158 RAIFEEAAG----ISKYKERRK---ETERKlerTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRelelall 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1050 -MDLERAKRKLE---GDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEE 1125
Cdd:TIGR02168 231 vLRLEELREELEelqEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1126 IEAERASRAKAEKQRSDLSR---ELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKhad 1202
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESkldELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK--- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1203 sVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKmcRALEDQLSEIKTKEEEQQRLINDLTAQRA 1282
Cdd:TIGR02168 388 -VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1283 RLQTESGEYSRQLDEKDTLVSQLsRGKQAFTQQIEELKRQLEEEIKAksALAHALQSSRHDcDLLREQYEeeqeAKAELQ 1362
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSEGVKA--LLKNQSGLSGIL-GVLSELIS----VDEGYE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1363 RAMSKANSEVAQW-RTKYETDAIQRTEELEEAKK--------------KLAQRLQDAEEHVEAVNAKCASLEKTKQRLQN 1427
Cdd:TIGR02168 537 AAIEAALGGRLQAvVVENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRK 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1428 EVEDLMIDV----------------------------------------ERTNAACAALDKKQRNFDKILAEWKQKCEET 1467
Cdd:TIGR02168 617 ALSYLLGGVlvvddldnalelakklrpgyrivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAEL 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1468 HAELEASQKESRSLSTELFKIKNAYEESLDQL--------------ETLKRENKNLQQEISDLTEQIAEGGKRIHELEKI 1533
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQIsalrkdlarleaevEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1534 KKQVEQEKSELQAALEEAEASLEheegKILRIQLELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRN 1613
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELK----ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1614 DAIRLKKKMEG---DLNEMEIQLNHAnrmaaealrnyrntQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIE 1690
Cdd:TIGR02168 853 DIESLAAEIEEleeLIEELESELEAL--------------LNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1691 ELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKK-KLETDISQIQGEMEDIiqearnaeEKAKKAITDAAMM 1769
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEnKIEDDEEEARRRLKRL--------ENKIKELGPVNLA 990
|
890 900 910
....*....|....*....|....*....|
gi 115527082 1770 A-EELKKEQDTSAHLERMKKNLEQTVKDLQ 1798
Cdd:TIGR02168 991 AiEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1139-1752 |
4.96e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.33 E-value: 4.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1139 QRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHAdSVAELGEQIDNLQRVK 1218
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA-ELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1219 QKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEE-QQRLINDLTAQRARLQTESGEYSRQLDE 1297
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEaEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1298 KDTLVSQLSRGKQAfTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRT 1377
Cdd:COG1196 392 LRAAAELAAQLEEL-EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1378 KYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVE---DLMIDVE---------RTNAACAA 1445
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgavAVLIGVEaayeaaleaALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1446 LDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGK 1525
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1526 RIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEidqmkrnhirivesmqstL 1605
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE------------------E 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1606 DAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLL 1685
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115527082 1686 QAEIEEL-----RAtleqtersrkiaEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEA 1752
Cdd:COG1196 773 EREIEALgpvnlLA------------IEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLET 832
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
871-1600 |
7.44e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.07 E-value: 7.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 871 EAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLED- 949
Cdd:PTZ00121 1204 AARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADEl 1283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 950 ECSELKKDIDDLEltlaKVEKEKHATENKVKnlTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEdkvntltKAKI 1029
Cdd:PTZ00121 1284 KKAEEKKKADEAK----KAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE-------AAKA 1350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1030 KLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQ 1109
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK 1430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1110 KKIKELQARIEELEeeieaerasRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEfqKMRRDLEEATLQ- 1188
Cdd:PTZ00121 1431 KKADEAKKKAEEAK---------KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD--EAKKKAEEAKKKa 1499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1189 HEATAATLRKKHADSVAELGEQidnlqrvKQKLEKEKSEMKMEIDDlASNMETVSKAkgnlEKMCRALEDQLSEIKTKEE 1268
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEA-------KKADEAKKAEEAKKADE-AKKAEEKKKA----DELKKAEELKKAEEKKKAE 1567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1269 EQQRlindlTAQRARLQTESGEYSRQLDEKdTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSalAHALQSSRHDCDLLR 1348
Cdd:PTZ00121 1568 EAKK-----AEEDKNMALRKAEEAKKAEEA-RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE--LKKAEEEKKKVEQLK 1639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1349 EQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAiQRTEEL---EEAKKKLAQRLQDAEEH---VEAVNAKCASLEKTK 1422
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaEEDEKKAAEALKKEAEEakkAEELKKKEAEEKKKA 1718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1423 QRLQNEVEDLMIDVERTnaacaaldKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAY-EESLDQLET 1501
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAViEEELDEEDE 1790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1502 LKR-ENKNLQQEISDLTEQIAEGGKRIHELekIKKQVEQEKSELQAALEEAEASLEhEEGKILRIQLELNQVKSEVDRKI 1580
Cdd:PTZ00121 1791 KRRmEVDKKIKDIFDNFANIIEGGKEGNLV--INDSKEMEDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKE 1867
|
730 740
....*....|....*....|
gi 115527082 1581 AEKDEEIDQMKRNHIRIVES 1600
Cdd:PTZ00121 1868 ADFNKEKDLKEDDEEEIEEA 1887
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1204-1832 |
8.77e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.48 E-value: 8.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1204 VAELGEQIDNLQR----------VKQKL-EKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQR 1272
Cdd:COG1196 195 LGELERQLEPLERqaekaeryreLKEELkELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1273 LINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYE 1352
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1353 EEQEAKAELQRAMSKANSEVAQWRtkyetdaiqrtEELEEAKKKLAQRLQDAEEhveavnakcasLEKTKQRLQNEVEDL 1432
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAE-----------EELEELAEELLEALRAAAE-----------LAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1433 MIDVERTNAACAALDKKQrnfdkilaewkqkcEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQE 1512
Cdd:COG1196 413 LERLERLEEELEELEEAL--------------AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1513 ISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKILRiqlelnqvkseVDRKIAEKDEEIDQMKR 1592
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI-----------GVEAAYEAALEAALAAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1593 NHIRIVESMQSTLDAeirsrndAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLK 1672
Cdd:COG1196 548 LQNIVVEDDEVAAAA-------IEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1673 EQLAMVERRANLLQAeiEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEA 1752
Cdd:COG1196 621 TLLGRTLVAARLEAA--LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1753 RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVES 1832
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
867-1433 |
1.96e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.32 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 867 LAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRK 946
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 947 LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTK 1026
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1027 AKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQALGM 1106
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1107 QLQKKIKELQARIEELEEEIEAERASRAKAEKQR---------SDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQK 1177
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavliGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1178 MRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRvkqklEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALE 1257
Cdd:COG1196 568 AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS-----DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1258 DQLSEIKTKEEEQQRLINDLTAQRARLQTEsgeysrQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHAL 1337
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLA------ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1338 QSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAqwrtKYETDAIQRTEELEEAKKKLAQRLQD-------AEEHVEA 1410
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEE 792
|
570 580
....*....|....*....|...
gi 115527082 1411 VNAKCASLEKTKQRLQNEVEDLM 1433
Cdd:COG1196 793 LEERYDFLSEQREDLEEARETLE 815
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
223-715 |
9.30e-21 |
|
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: 99.82 E-value: 9.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 223 IISANPLLEAFGNAKTVRNDNSSRFGKF--IRIHFGTTG---KLASADIETYLLEKSRVTFQL------KAERSYHIFYQ 291
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 292 IMS--NKKP--------------DLIEMLLITTNPYDYA-FVSQGEITVPSIDDQEELMatdSAIEILGFTSDERVSIYK 354
Cdd:cd14894 329 MVAgvNAFPfmrllakelhldgiDCSALTYLGRSDHKLAgFVSKEDTWKKDVERWQQVI---DGLDELNVSPDEQKTIFK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 355 LTGAVMHYGNMKFKQKQREEQAEPDGT---EVADKAAYLQNLNSADLL-KALCYPRVKVGNEYVTKGQTVQ--QVYNAVG 428
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLeRMLMTKSVSLQSTSETFEVTLEkgQVNHVRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 429 ALAKAVYDKMFLWMVTRINQ--------------QLDTKQPRQYFIGVL---DIAGFEIFDFNSLEQLCINFTNEKLqqF 491
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEatkmsalstdgnkhQMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINYLSEKL--Y 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 492 FNHHMFVLEQEEYKKEGIEWtfiDFGMDLaacIELIEKPMGIFSILEEECMFPKATDTSF-----KNKLYEQHLGKSNNF 566
Cdd:cd14894 564 AREEQVIAVAYSSRPHLTAR---DSEKDV---LFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIYDRNSS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 567 QKPKPAKGKPEAH-----------FSLIHYAGTVDYNIAGWLDKNKDPL-NETVVGLYQKSAMKTLALLFVGATG--AEA 632
Cdd:cd14894 638 RLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLNESSQLgwSPN 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 633 EAGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKG 712
Cdd:cd14894 718 TNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNS 797
|
...
gi 115527082 713 FPS 715
Cdd:cd14894 798 SSS 800
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1171-1915 |
1.32e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.83 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1171 REAEFQKMRRDLEEATLQHEATAATLRKKHADSVAElgeqidnlqrvkqklEKEKSEMKMEIDDLASNMETVSKAKG--N 1248
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAE---------------EARKAEEAKKKAEDARKAEEARKAEDarK 1141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1249 LEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARlqteSGEYSRQLDEkdtlVSQLSRGKQAFTQQIEELKRQLEEEIK 1328
Cdd:PTZ00121 1142 AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK----KAEAARKAEE----VRKAEELRKAEDARKAEAARKAEEERK 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1329 AKSALAHALQSSRHDCDLLREQYEEEQEAK-AELQRAmskaNSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEH 1407
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKkAEEERN----NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK 1289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1408 VEAVNAKCASLEKTKQRLQNEVEDLMIDVErtnaacaaLDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELfk 1487
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKADE--------AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA-- 1359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1488 ikNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKilriql 1567
Cdd:PTZ00121 1360 --EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK------ 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1568 elnqvKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEAlrnY 1647
Cdd:PTZ00121 1432 -----KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA---K 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1648 RNTQAILKDTQLHLDDALRSQEDLKEqlAMVERRANLLQAEIEELRA-TLEQTERSRKIAEQELLDASERVQllHTQNTS 1726
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKK--AEEAKKADEAKKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAE--EDKNMA 1579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1727 LINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAiTDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQ 1806
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1807 LALKGG--KKQIQKLEARVRELEGEvESEQKRNVEAVKGLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKR 1884
Cdd:PTZ00121 1659 NKIKAAeeAKKAEEDKKKAEEAKKA-EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
730 740 750
....*....|....*....|....*....|....
gi 115527082 1885 QAEEAE---EQSNVNLSKFRRIQHELEEAEERAD 1915
Cdd:PTZ00121 1738 EAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1172-1935 |
1.12e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 96.68 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1172 EAEFQKMRRDLEEATLQHEATAATLRkkhadsvaELGEQIDNLQRVKQKLEKEKsEMKMEIDDLASNMetvskakgnLEK 1251
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIID--------EKRQQLERLRREREKAERYQ-ALLKEKREYEGYE---------LLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1252 MCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQ-AFTQQIEELKRQLEEEIKAK 1330
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1331 SALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDA------IQRTEELEEAKKKLAQRLQDA 1404
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeeledlRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1405 EEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDkilaewkqkceethAELEASQKESRSLSTE 1484
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE--------------EEKEDKALEIKKQEWK 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1485 LFKIKnayeeslDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKILr 1564
Cdd:TIGR02169 457 LEQLA-------ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVA- 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1565 iqlELNQVKSEVDRKIaekdeEIDQMKRNHIRIVESmqsTLDAEirsrnDAIRLKKKMEGD------LNEMEIQLNHANR 1638
Cdd:TIGR02169 529 ---QLGSVGERYATAI-----EVAAGNRLNNVVVED---DAVAK-----EAIELLKRRKAGratflpLNKMRDERRDLSI 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1639 MAAEAL-----------RNYRNTQA-ILKDTQLhlddaLRSQEDLKEQlaMVERRANLLQAEIEELRATLEQTERSRKIA 1706
Cdd:TIGR02169 593 LSEDGVigfavdlvefdPKYEPAFKyVFGDTLV-----VEDIEAARRL--MGKYRMVTLEGELFEKSGAMTGGSRAPRGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1707 E-------QELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKEQDT 1779
Cdd:TIGR02169 666 IlfsrsepAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1780 SAHLERMKKNLEQTVKDLQHRLDEAEqLALKGGKKQIQKLEAR-----VRELEGEVESEQKRNVEAVKGLRKHERKVKEL 1854
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELE-EDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1855 TYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNVNLSKFRRIQHELEEAEERADIAESQVNKLRVKSREVHTK 1934
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
.
gi 115527082 1935 I 1935
Cdd:TIGR02169 905 I 905
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1077-1927 |
3.10e-19 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 95.19 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1077 KQQLDEKLKKKEFEMSGLQSKIEDEQALGMQ----LQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISE 1152
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKqkfyLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1153 RLEeagGATSAQIEMNKKREAEFQKMRRDLeeatLQHEATAATLRKKHADSVAELGEQI---DNL------------QRV 1217
Cdd:pfam15921 153 ELE---AAKCLKEDMLEDSNTQIEQLRKMM----LSHEGVLQEIRSILVDFEEASGKKIyehDSMstmhfrslgsaiSKI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1218 KQKLEKEKSEMKMEIDDLASNMETV-SKAKGNLEKMCRALEDQLSEIKTKEEEQqrlINDLT--AQRARLQTESGE---- 1290
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALkSESQNKIELLLQQHQDRIEQLISEHEVE---ITGLTekASSARSQANSIQsqle 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1291 ------------YSRQLDEKDTLVSQ----LSRGKQAFTQQIEELKRQLeeeIKAKSALAHALQSsrhdcdllREQYEEE 1354
Cdd:pfam15921 303 iiqeqarnqnsmYMRQLSDLESTVSQlrseLREAKRMYEDKIEELEKQL---VLANSELTEARTE--------RDQFSQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1355 --------QEAKAELQRAMSKANSEVAQWRTKYETDA-------------------IQRTEELEEAKKKLAQ-------- 1399
Cdd:pfam15921 372 sgnlddqlQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitidhlrrelddrnmeVQRLEALLKAMKSECQgqmerqma 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1400 RLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLmidvertNAACAALDKKQRNFDKILAEWKQKceethaeleasQKESR 1479
Cdd:pfam15921 452 AIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTVSDLTASLQEK-----------ERAIE 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1480 SLSTELFKIKNAYEESLDQLETLKREN---KNLQQEISDLTEQIAEGGKRIhelEKIKKQVEQ------EKSELQAALEE 1550
Cdd:pfam15921 514 ATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEKDKVI---EILRQQIENmtqlvgQHGRTAGAMQV 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1551 AEASLEHE-EGKILRIQlELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLdaeiRSRNDairLKKKMEGDLNEM 1629
Cdd:pfam15921 591 EKAQLEKEiNDRRLELQ-EFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERL----RAVKD---IKQERDQLLNEV 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1630 EIQLNHANRMAAE---ALRNYRNTQAILKDTQLHLDDALRSQEDLKEQ----LAMVE-------RRANLLQAEIEELRAT 1695
Cdd:pfam15921 663 KTSRNELNSLSEDyevLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQtrntLKSMEgsdghamKVAMGMQKQITAKRGQ 742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1696 LEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKakkaitdAAMMAEELKK 1775
Cdd:pfam15921 743 IDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEK-------VANMEVALDK 815
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1776 EQDTSAHLERMKKNLEQ-TVK-DLQHRLDEAEqlaLKG-GKKQIQKLEARVreLEGEVESEQKRNVEAVKG----LRKHE 1848
Cdd:pfam15921 816 ASLQFAECQDIIQRQEQeSVRlKLQHTLDVKE---LQGpGYTSNSSMKPRL--LQPASFTRTHSNVPSSQStasfLSHHS 890
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115527082 1849 RKVKELTYQTEEDRKNIlrLQDLVDKLQAKVKSYKRQAEEAEEQSNVNLSKfRRIQHELEEAEERADIAESQVNKLRVK 1927
Cdd:pfam15921 891 RKTNALKEDPTRDLKQL--LQELRSVINEEPTVQLSKAEDKGRAPSLGALD-DRVRDCIIESSLRSDICHSSSNSLQTE 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
840-1432 |
4.89e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.23 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 840 IKPLLKSAETEKEMANMKEEFEKTKEELAKteAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLiktKIQL 919
Cdd:COG1196 202 LEPLERQAEKAERYRELKEELKELEAELLL--LKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL---RLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 920 EAKIKEVTERAEDEEEINAELtakkRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKE 999
Cdd:COG1196 277 EELELELEEAQAEEYELLAEL----ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1000 KKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQ 1079
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1080 LDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAeKQRSDLSRELEEISERLEEAGG 1159
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-AARLLLLLEAEADYEGFLEGVK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1160 ATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNM 1239
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1240 E---TVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQI 1316
Cdd:COG1196 592 LargAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1317 EELKRQLEEEIKAKSALAHALQSSRHdcDLLREQYEEEQEAKAELQRAMSKANSEVAQwRTKYETDAIQRTEELEEAKKK 1396
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEE--ALLAEEEEERELAEAEEERLEEELEEEALE-EQLEAEREELLEELLEEEELL 748
|
570 580 590
....*....|....*....|....*....|....*.
gi 115527082 1397 LAQRLQDAEEHVEAvnakcASLEKTKQRLQNEVEDL 1432
Cdd:COG1196 749 EEEALEELPEPPDL-----EELERELERLEREIEAL 779
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1074-1804 |
8.34e-19 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 93.16 E-value: 8.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1074 ENDKQQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISER 1153
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1154 LEeaggatsAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADsVAELGEQIDNLQRVKQKLEKEKSEMKMEID 1233
Cdd:TIGR04523 112 IK-------NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1234 DLASNMEtvskakgNLEKMCRALEDQLSEIKTKEEEQQRL---INDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQ 1310
Cdd:TIGR04523 184 NIQKNID-------KIKNKLLKLELLLSNLKKKIQKNKSLesqISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1311 AFTQQIEELKRQLEEEIKaksalahalQSSRHDcDLLREQYEEEQEAKAELQRAMSKANSEvaqWRTKYETDAIQRTEEL 1390
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQK---------ELEQNN-KKIKELEKQLNQLKSEISDLNNQKEQD---WNKELKSELKNQEKKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1391 EEAKKKLAQrlqdAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAE 1470
Cdd:TIGR04523 324 EEIQNQISQ----NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1471 LEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEE 1550
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1551 AEASLEHEEGKILRIQ---LELNQVKSEVDRKIAEKDEEIDQMKRNhIRIVESMQSTLDAEIRSRNDAIrLKKKMEGDLN 1627
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEkelKKLNEEKKELEEKVKDLTKKISSLKEK-IEKLESEKKEKESKISDLEDEL-NKDDFELKKE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1628 EMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAE 1707
Cdd:TIGR04523 558 NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1708 QELLDASERVQLLHTQNTSLINTK-------KKLETDISQIQGEMEDIIQEARNAEEKA---KKAITDAAMMAEELKKEQ 1777
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKEIRNKWpeiikkiKESKTKIDDIIELMKDWLKELSLHYKKYitrMIRIKDLPKLEEKYKEIE 717
|
730 740
....*....|....*....|....*..
gi 115527082 1778 DTSAHLERMKKNLEQTVKDLQHRLDEA 1804
Cdd:TIGR04523 718 KELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1390-1930 |
1.44e-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: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1390 LEEA--------KKKLA-QRLQDAEEHVEAVNAKCASLEKTKQRLQNEVE------DLMIDVERTNAACAAL-----DKK 1449
Cdd:COG1196 161 IEEAagiskykeRKEEAeRKLEATEENLERLEDILGELERQLEPLERQAEkaeryrELKEELKELEAELLLLklrelEAE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1450 QRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHE 1529
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1530 LEKIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEI 1609
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1610 RSRNDAIRLKKKmEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEI 1689
Cdd:COG1196 401 QLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1690 EELRATLEQTERSRKIAEQELLDASERVQLlhTQNTSLINTKKKLETDISQIQG---EMEDIIQEARNAEEKAK--KAIT 1764
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEG--VKAALLLAGLRGLAGAVAVLIGveaAYEAALEAALAAALQNIvvEDDE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1765 DAAMMAEELKKEQD---TSAHLERMKKNLEQTVKDLQHRLDEA---------------------------EQLALKGGKK 1814
Cdd:COG1196 558 VAAAAIEYLKAAKAgraTFLPLDKIRARAALAAALARGAIGAAvdlvasdlreadaryyvlgdtllgrtlVAARLEAALR 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1815 QIQKLEARVRELEGEVESEQKRNVEAvkglrkhERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSN 1894
Cdd:COG1196 638 RAVTLAGRLREVTLEGEGGSAGGSLT-------GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
570 580 590
....*....|....*....|....*....|....*.
gi 115527082 1895 VNLSKFRRIQHELEEAEERADIAESQVNKLRVKSRE 1930
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
845-1439 |
6.28e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 91.36 E-value: 6.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 845 KSAETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVtlmQEKNDLQlqvqaEADSLADAEERCDQLIKTKIQLEAKIK 924
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKA---EEKKKAD-----EAKKKAEEAKKADEAKKKAEEAKKKAD 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 925 EVTERAEDEEEIN--AELTAKKRKLEDECSELKKDIDDLEltlaKVEKEKHATENKVKnlTEEMAGLDETIAKLTKEKKA 1002
Cdd:PTZ00121 1333 AAKKKAEEAKKAAeaAKAEAEAAADEAEAAEEKAEAAEKK----KEEAKKKADAAKKK--AEEKKKADEAKKKAEEDKKK 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1003 LQEAHQQTLDDLQAEEdkvntlTKAKIKLEQQVDDLEGSLEQEKKIrmdlERAKRKLEGDLKlaqestmdIENDKQQLDE 1082
Cdd:PTZ00121 1407 ADELKKAAAAKKKADE------AKKKAEEKKKADEAKKKAEEAKKA----DEAKKKAEEAKK--------AEEAKKKAEE 1468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1083 KLKKKEFEMSGLQSKIEDEqalgmqLQKKIKELQarieELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATS 1162
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADE------AKKKAEEAK----KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1163 AQIEMNKKREAEFQKMR--RDLEEATLQHEATAATLRKKHADSVAELGEQIDNlQRVKQKLEKEKSEMKMEIDDLASNME 1240
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE-ARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1241 TVSKAKgnlekmcraledqlsEIKtKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELK 1320
Cdd:PTZ00121 1618 AKIKAE---------------ELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1321 RQLEEEIKAKSALAHALQSSRhDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAiQRTEEL---EEAKKKL 1397
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEAkkdEEEKKKI 1759
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 115527082 1398 AQRLQDAEEHVEAVNAKCASLekTKQRLQNEVEDLMIDVERT 1439
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKK 1799
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1087-1864 |
2.20e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.43 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1087 KEFEMSGLQSKIEDEQAlgMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIE 1166
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEAT--EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1167 MNKKREAEFQKMR--RDLEEATLQHEA-TAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEmKMEIDDLASNMETVS 1243
Cdd:PTZ00121 1155 EIARKAEDARKAEeaRKAEDAKKAEAArKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1244 KAKGNLEKMCRALEDQLSEIKTKEEEQQrlINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQL 1323
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEAR--MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1324 EEEIKAKSALAHAlQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRteelEEAKKKLAQRLQD 1403
Cdd:PTZ00121 1312 EEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK----EEAKKKADAAKKK 1386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1404 AEEHVEAVNAKcasleKTKQRLQNEVEDLMIDVERTNAACAAldKKQRNFDKILAEWKQKCEETHAELEASQKESRSLST 1483
Cdd:PTZ00121 1387 AEEKKKADEAK-----KKAEEDKKKADELKKAAAAKKKADEA--KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA 1459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1484 ELFKIKNAYEESLDQLETlKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQ-EKSELQAALEEAEASLEHEEGKI 1562
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKK-KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADE 1538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1563 LRiqlelnqvKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAE 1642
Cdd:PTZ00121 1539 AK--------KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1643 ALRnyRNTQAILKDTQLHLDDALRSQ-EDLKEQLAMVERRANLLQAEIEELRATLEQTERSrkiAEQElldaservqllh 1721
Cdd:PTZ00121 1611 EAK--KAEEAKIKAEELKKAEEEKKKvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK---AEED------------ 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1722 tqntslintKKKLEtDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRL 1801
Cdd:PTZ00121 1674 ---------KKKAE-EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115527082 1802 DEAEQLAL-KGGKKQIQKLEARVRELEGEVESEQKRNVEavKGLRKHERKVKELTYQTEEDRKN 1864
Cdd:PTZ00121 1744 KKAEEAKKdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVDKKIKDIFD 1805
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
841-1704 |
2.52e-17 |
|
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: 88.88 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 841 KPLLKSAETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEadsladaEERCDQLIKTKIQLE 920
Cdd:pfam02463 150 MKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAK-------KALEYYQLKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 921 AKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEK 1000
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1001 KALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLE--QEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQ 1078
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKelEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1079 QLDEKLKKKEFEMS-GLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEA 1157
Cdd:pfam02463 383 SERLSSAAKLKEEElELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1158 GGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLAS 1237
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1238 NMETVSKAKGNLEKMCRALEDQ----------LSEIKTKEEEQQRLINDLTAQ-------RARLQTESGEYSRQLDEKDT 1300
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQklvraltelpLGARKLRLLIPKLKLPLKSIAvleidpiLNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1301 LVSQLSRGKQAFTQQIEELKRQLEEEIKAKSaLAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYE 1380
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGLRKGVS-LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1381 TDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVErtnaacaALDKKQRNFDKILAEW 1460
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK-------KEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1461 KQKCEETHAELEASQKESRSLSTEL-FKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQ 1539
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKAQeEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1540 EKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQMKR--NHIRIVESMQSTLDAEIRSRNDAIR 1617
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQklNLLEEKENEIEERIKEEAEILLKYE 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1618 LKKKMEGDLNEMEIQLNHANRMAAEaLRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLE 1697
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKEEEE-ERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIE 1013
|
....*..
gi 115527082 1698 QTERSRK 1704
Cdd:pfam02463 1014 ETCQRLK 1020
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1137-1629 |
1.10e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 86.63 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1137 EKQRSDLSRELEEISERLEEAG---GATSAQIEMNKKREAEFQKMRRDLEEATlqhEATAATLRKKhadsvAELGEQIDN 1213
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARetrDEADEVLEEHEERREELETLEAEIEDLR---ETIAETERER-----EELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1214 LQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSR 1293
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1294 QLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVA 1373
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1374 QWRTKYE-------------TDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTK------QRLQNEVEDL-- 1432
Cdd:PRK02224 444 EAEALLEagkcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaedriERLEERREDLee 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1433 MID-----VERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEeSLDQLETLKRENK 1507
Cdd:PRK02224 524 LIAerretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERIRTLLAAIA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1508 NLQQEISDLTEQIAEggkrIHELEKIKKQVEQEKSELQAALEEA--EASLEHEEGKILRIQLELNQVKSEVDRKIAEKDE 1585
Cdd:PRK02224 603 DAEDEIERLREKREA----LAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLDELREERDD 678
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115527082 1586 ----------EIDQMKR-------------------NHIRIVESMQSTLDAEIRSRNDAirlkkKMEGDLNEM 1629
Cdd:PRK02224 679 lqaeigavenELEELEElrerrealenrvealealyDEAEELESMYGDLRAELRQRNVE-----TLERMLNET 746
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1295-1909 |
1.82e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 86.12 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1295 LDEKDTLvSQLSRGKQAFtQQIEELKRQLEEEIKAKSALAHALQssrhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQ 1374
Cdd:COG4913 218 LEEPDTF-EAADALVEHF-DDLERAHEALEDAREQIELLEPIRE--------LAERYAAARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1375 wrTKYETdAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKtkQRLQN---EVEDLMIDVERTNAACAALDKKQR 1451
Cdd:COG4913 288 --RRLEL-LEAELEELRAELARLEAELERLEARLDALREELDELEA--QIRGNggdRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1452 NFDKILAEWKQKCEETHAELEASQKESRslstelfkiknayeeslDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELE 1531
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAA-----------------ALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1532 KIKKQVEQEKS----ELQAALEEAEASLEHEEGKiLRIQLELNQVKSE--------------------VD-RKIAEKDEE 1586
Cdd:COG4913 426 AEIASLERRKSnipaRLLALRDALAEALGLDEAE-LPFVGELIEVRPEeerwrgaiervlggfaltllVPpEHYAAALRW 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1587 IDQMK-RNHIRIvESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNH--ANRMA------AEALRNYRntQAILKDT 1657
Cdd:COG4913 505 VNRLHlRGRLVY-ERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAelGRRFDyvcvdsPEELRRHP--RAITRAG 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1658 QLH-------LDDALRSQEDL------KEQLAMVERRANLLQAEIEELRATLEQTERSRKiAEQELLDASERVQllhTQN 1724
Cdd:COG4913 582 QVKgngtrheKDDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLA---EYS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1725 TSLINTkKKLETDISQIQGEMEDIiqearnaeEKAKKAITDAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEA 1804
Cdd:COG4913 658 WDEIDV-ASAEREIAELEAELERL--------DASSDDLAALEEQLEELEAELEE---LEEELDELKGEIGRLEKELEQA 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1805 EQlalkggkkQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERKVKELTYQTEEDRKNIL-RLQDLVDKLQAKVKSYK 1883
Cdd:COG4913 726 EE--------ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRaRLNRAEEELERAMRAFN 797
|
650 660
....*....|....*....|....*....
gi 115527082 1884 RQ--AEEAEEQSNV-NLSKFRRIQHELEE 1909
Cdd:COG4913 798 REwpAETADLDADLeSLPEYLALLDRLEE 826
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
896-1763 |
2.63e-16 |
|
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: 85.48 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 896 QAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDdleltlakvekekHAT 975
Cdd:TIGR00606 244 ENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNH 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 976 ENKVKNLTEEMAGLDETIAKLTKEKKALQEAH-----QQTLDDLQAEEDKVNTLTKAKIKLEQQ----VDDLEGSLEQEK 1046
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKtellvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1047 KIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQALgmqLQKKIKELQARIEELEeei 1126
Cdd:TIGR00606 391 QIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEI---LEKKQEELKFVIKELQ--- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1127 eaerasraKAEKQRSDLSRELEEISERLEEAGGA-TSAQIEMNKKREAEFQKMRRDLEEaTLQHEATAATLRKKHADSVA 1205
Cdd:TIGR00606 465 --------QLEGSSDRILELDQELRKAERELSKAeKNSLTETLKKEVKSLQNEKADLDR-KLRKLDQEMEQLNHHTTTRT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1206 ELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVskakgnlekmcRALEDQLSEIKTKEEEQQRLINDLTAQRARLQ 1285
Cdd:TIGR00606 536 QMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNK-----------KQLEDWLHSKSKEINQTRDRLAKLNKELASLE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1286 TESGEYSRQLDEKDTLVSQLSR------GKQAFTQQIEELKRQLEEEIKAKSALAHALQssrhdcdlLREQYEEEQEAKa 1359
Cdd:TIGR00606 605 QNKNHINNELESKEEQLSSYEDklfdvcGSQDEESDLERLKEEIEKSSKQRAMLAGATA--------VYSQFITQLTDE- 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1360 elqramSKANSEVAQwrtkyetDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERT 1439
Cdd:TIGR00606 676 ------NQSCCPVCQ-------RVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1440 NAACAALDKKQRNFDKILAEWKQKCEETHAELE---ASQKESRSLSTELFKIKNAYEEsldqletLKRENKNLQQEISDL 1516
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtimPEEESAKVCLTDVTIMERFQME-------LKDVERKIAQQAAKL 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1517 teQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEvDRKIAEKDEEIDQMKRNHIR 1596
Cdd:TIGR00606 816 --QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE-KLQIGTNLQRRQQFEEQLVE 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1597 IVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKE-QL 1675
Cdd:TIGR00606 893 LSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDdYL 972
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1676 AMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLI--NTKKKLETDISQIQGEM-EDIIQEA 1752
Cdd:TIGR00606 973 KQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKreNELKEVEEELKQHLKEMgQMQVLQM 1052
|
890
....*....|.
gi 115527082 1753 RNAEEKAKKAI 1763
Cdd:TIGR00606 1053 KQEHQKLEENI 1063
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
943-1634 |
4.20e-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: 84.30 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 943 KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVN 1022
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1023 TLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQ 1102
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1103 ALGMQLQKKIKELQarieeleeeieaerasrakaekqrsdlsreleeiserleeaggatsAQIEMNKKREAEFQkmrrDL 1182
Cdd:TIGR04523 194 NKLLKLELLLSNLK----------------------------------------------KKIQKNKSLESQIS----EL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1183 EEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSkakgNLEKMCRALEDQLSE 1262
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK----ELEKQLNQLKSEISD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1263 IKtkEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLsrgkqafTQQIEELKRQLEEeikaksalahalqsSRH 1342
Cdd:TIGR04523 300 LN--NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL-------NEQISQLKKELTN--------------SES 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1343 DCDLLREQYEEEQEAKAELQRAMSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTK 1422
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEI---------------KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1423 QRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETL 1502
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1503 KRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHE--EGKILRIQLELNQVKSE---VD 1577
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTqksLK 581
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 115527082 1578 RKIAEKDEEIDQMKRNhIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLN 1634
Cdd:TIGR04523 582 KKQEEKQELIDQKEKE-KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
847-1459 |
1.15e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.58 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 847 AETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEV 926
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 927 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN-------LTEEMAGLDETIAKLTKE 999
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGgraveevLKASIQGVHGTVAQLGSV 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1000 K----KALQEAHQQTLDDLQAEED--------------------------KVNTLTKAKIKLEQQVDDLEGSLEQEKKIR 1049
Cdd:TIGR02169 534 GeryaTAIEVAAGNRLNNVVVEDDavakeaiellkrrkagratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPKYE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1050 -------------MDLERAKR--------KLEGDL--------------KLAQESTMDIENDKQQLDEKLKKKEFEMSGL 1094
Cdd:TIGR02169 614 pafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGELfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1095 QSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqIEMNKKREAE 1174
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV-------KSELKELEAR 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1175 FQKMRRDLEEATLQHEATAATLRkkhadsvaelGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCR 1254
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLS----------HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1255 ALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEeikaksala 1334
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE--------- 907
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1335 halqssrhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQ-----WRTKYETDAIQRTEELEEAKKKLAQRLQD------ 1403
Cdd:TIGR02169 908 ------------LEAQIEKKRKRLSELKAKLEALEEELSEiedpkGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnm 975
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115527082 1404 -AEEHVEAVNAKCASLEKTKQRLQNEVEDL-----MIDVERTNAACAALDKKQRNFDKILAE 1459
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 ... |
1073-1932 |
1.84e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 82.71 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1073 IENDKQQLDEKLKKKEFEMSGLQSKIEDEQALgmqlqKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISE 1152
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEEAAGSRLKRKKKEAL-----KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1153 RLEEAGGATSAQIEmnkKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDnlqrvkqKLEKEKSEMKMEI 1232
Cdd:pfam02463 219 LELEEEYLLYLDYL---KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK-------EEEKEKKLQEEEL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1233 DDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSrgkqaf 1312
Cdd:pfam02463 289 KLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE------ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1313 tqQIEELKRQLEEEIKAKSALAHALQSSRhdcdllreqyEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEE 1392
Cdd:pfam02463 363 --KLQEKLEQLEEELLAKKKLESERLSSA----------AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1393 AKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQ---KCEETHA 1469
Cdd:pfam02463 431 ILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQkesKARSGLK 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1470 ELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENkNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALE 1549
Cdd:pfam02463 511 VLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIST-AVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKL 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1550 EAeasLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEM 1629
Cdd:pfam02463 590 PL---KSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1630 EIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTErsRKIAEQE 1709
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEE--LKLLKQK 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1710 LLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEA--RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK 1787
Cdd:pfam02463 745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKveEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1788 KNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQK--RNVEAVKGLRKHERKVKELTYQTEEDRKNI 1865
Cdd:pfam02463 825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELllKEEELEEQKLKDELESKEEKEKEEKKELEE 904
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115527082 1866 LRLQDLVDKLQAKVKSYKRQAEEAEEQSNVNLSKFRRIQHELEEAEERADIAESQVNKLRVKSREVH 1932
Cdd:pfam02463 905 ESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEE 971
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
908-1589 |
2.47e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 82.32 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 908 RCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAT----ENKVKNLT 983
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERkqvlEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 984 EEMAGLDETIAKLTKEKKALQEAH--QQTLDDLQAEEDKVNTLTKA------KIKLEQQVDDLEGSLEQEKKIRMDLERA 1055
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAVleetqeRINRARKAAPLAAHIKAVTQIEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1056 KRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQAlgMQLQKKIKELQARIEELEEEIEAERASRAK 1135
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA--HEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1136 AEKQRSDLSRELEEISERLEEAGGATSAQIEMNK-----KREAEFQKMRRDLEEATLQHEATAATLRKKHADSVA----E 1206
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGqlahaKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAqslkE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1207 LGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSK----------AKGNLEKMCRALEDQLSEIKTKEEEQQRLIND 1276
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGscihpnparqDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1277 LTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQA---FTQQIEELKRQLEEEIKAKSALAhalqssrhdcDLLREQYEE 1353
Cdd:TIGR00618 551 LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDipnLQNITVRLQDLTEKLSEAEDMLA----------CEQHALLRK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1354 EQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLm 1433
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML- 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1434 idvERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEA-------SQKESRSLS-TELFKIKNAYEESLDQLETLKRE 1505
Cdd:TIGR00618 700 ---AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAredalnqSLKELMHQArTVLKARTEAHFNNNEEVTAALQT 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1506 NKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDE 1585
Cdd:TIGR00618 777 GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEE 856
|
....
gi 115527082 1586 EIDQ 1589
Cdd:TIGR00618 857 CSKQ 860
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1221-1807 |
3.71e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.62 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1221 LEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEqqrlINDLTAQRARLQTESGEYSRQL----- 1295
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAE----IEDLRETIAETEREREELAEEVrdlre 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1296 ------DEKDTLVSQLSRG----------KQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKA 1359
Cdd:PRK02224 287 rleeleEERDDLLAEAGLDdadaeavearREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1360 ELQRAMSKANSEVAQWRTkyetdaiqRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVErt 1439
Cdd:PRK02224 367 ELESELEEAREAVEDRRE--------EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR-- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1440 naacaALDKKQRNFDKILAEwkQKCEETHAELEASQkesrslstelfkIKNAYEESLDQLETLKRENKNLQQEISDLTEQ 1519
Cdd:PRK02224 437 -----TARERVEEAEALLEA--GKCPECGQPVEGSP------------HVETIEEDRERVEELEAELEDLEEEVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1520 IaEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKI--LRIQLELNQVKSEVDRKIAEKDEEIDQMKRNHIRI 1597
Cdd:PRK02224 498 L-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAeeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1598 VESMQSTLDAEIRSRNdairlkkKMEGDLNEMEiqlnhANRMAAEALRNYRNTQAILKDTQlhlddalrsqedlKEQLAM 1677
Cdd:PRK02224 577 LNSKLAELKERIESLE-------RIRTLLAAIA-----DAEDEIERLREKREALAELNDER-------------RERLAE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1678 VERRANLLQAEIEELRATLEQTERSRkiAEQELLDASERVQLLHTQntslintKKKLETDISQIQGEMEDIiqearnaee 1757
Cdd:PRK02224 632 KRERKRELEAEFDEARIEEAREDKER--AEEYLEQVEEKLDELREE-------RDDLQAEIGAVENELEEL--------- 693
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 115527082 1758 kakkaitdaammaEELKKEQDTsahlermkknLEQTVKDLQHRLDEAEQL 1807
Cdd:PRK02224 694 -------------EELRERREA----------LENRVEALEALYDEAEEL 720
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
919-1429 |
4.51e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.24 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 919 LEAKIKEVTERAE--DEEEINAELT--------AKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAG 988
Cdd:PRK02224 211 LESELAELDEEIEryEEQREQARETrdeadevlEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 989 LDETIAKLTKEkKALQEAHQQTLDDLQAEedkvntltkakikLEQQVDDLEGSLEQEkkiRMDLERAKRKLEGdlklAQE 1068
Cdd:PRK02224 291 LEEERDDLLAE-AGLDDADAEAVEARREE-------------LEDRDEELRDRLEEC---RVAAQAHNEEAES----LRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1069 STMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIeeleeeieaerasrAKAEKQRSDLSRELE 1148
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF--------------GDAPVDLGNAEDFLE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1149 EISERLEEAGGATsaqiemnKKREAEFQKMRRDLEEA-TLQHEATAATLRKK-----HADSVAELGEQIDnlqrvkqKLE 1222
Cdd:PRK02224 416 ELREERDELRERE-------AELEATLRTARERVEEAeALLEAGKCPECGQPvegspHVETIEEDRERVE-------ELE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1223 KEKSEMKMEIDDLASNMETVSKAKgnlekmcrALEDQLSEIKTKEEEQQRLINDltaQRARLQTESGEYSRQLDEKDTLV 1302
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAEDLV--------EAEDRIERLEERREDLEELIAE---RRETIEEKRERAEELRERAAELE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1303 SQLSRGKQAFTQQIEELKRQLEEEIKAKSALAhALQSSRHDCDLLREQYEEEQEAKAELQRAMSK--ANSEVAQWRTKYE 1380
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLA-ELKERIESLERIRTLLAAIADAEDEIERLREKreALAELNDERRERL 629
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 115527082 1381 TDAIQRTEELEE-----AKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEV 1429
Cdd:PRK02224 630 AEKRERKRELEAefdeaRIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
869-1588 |
5.33e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 80.83 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 869 KTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERcdqliktKIQLEAKIKEVTERaedEEEINAELTAKKRKLE 948
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEK-------INNSNNKIKILEQQ---IKDLNDKLKKNKDKIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 949 DECSELKKDIDDLeltlakvekeKHATENKVKNLTEemagldetIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTkak 1028
Cdd:TIGR04523 100 KLNSDLSKINSEI----------KNDKEQKNKLEVE--------LNKLEKQKKENKKNIDKFLTEIKKKEKELEKLN--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1029 ikleqqvddlegsleqeKKIRmDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQALGMQ- 1107
Cdd:TIGR04523 159 -----------------NKYN-DLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQi 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1108 --LQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEA 1185
Cdd:TIGR04523 221 seLKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1186 TLQheataatlrkKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLE----KMCRALEDQLS 1261
Cdd:TIGR04523 301 NNQ----------KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsensEKQRELEEKQN 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1262 EIKTKEEEQQRL---INDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQ---LEEEIKAKSALAH 1335
Cdd:TIGR04523 371 EIEKLKKENQSYkqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETiikNNSEIKDLTNQDS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1336 ALQSSRHDCDLLREQYEEEQEakaELQRAMSKANSEVaQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKC 1415
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLK---VLSRSINKIKQNL-EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1416 ASLEKTKQRLQNEVEDLMIDVErtnaacaaldkkqrnfdkilaewKQKCEETHAELEasqKESRSLSTELFKIKNAYEES 1495
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEDELN-----------------------KDDFELKKENLE---KEIDEKNKEIEELKQTQKSL 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1496 LDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVK-- 1573
Cdd:TIGR04523 581 KKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRnk 660
|
730
....*....|....*.
gi 115527082 1574 -SEVDRKIAEKDEEID 1588
Cdd:TIGR04523 661 wPEIIKKIKESKTKID 676
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
920-1789 |
6.98e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 80.79 E-value: 6.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 920 EAKIKEVTERAEDEEEINAEL-TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHatenkvknlteemagLDETIAKLTK 998
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL---------------NEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 999 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQ 1078
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1079 QLDEKLKKKEFEMSglqskiedeqalgmQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAG 1158
Cdd:pfam02463 325 KAEKELKKEKEEIE--------------ELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1159 GATSAQIEM--NKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLA 1236
Cdd:pfam02463 391 KLKEEELELksEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1237 SNmetvskakgnlekmcraleDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQI 1316
Cdd:pfam02463 471 ED-------------------LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1317 EELKRQLEEEIKAKSALAHALQSSRHD-CDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKK 1395
Cdd:pfam02463 532 GDLGVAVENYKVAISTAVIVEVSATADeVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1396 KLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERT--NAACAALDKKQRNFDKILAEWKQKCEETHAELEA 1473
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEegLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1474 SQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEA 1553
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1554 SLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQMKRNH--IRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEI 1631
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEeaELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1632 QLNHANRMAAEalrnyrNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELL 1711
Cdd:pfam02463 852 AEEELERLEEE------ITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE 925
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115527082 1712 DASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKN 1789
Cdd:pfam02463 926 EAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
839-1519 |
8.10e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.96 E-value: 8.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 839 KIKPLLKSAEtEKEMANmkeefektkeelaktEAKRKELEEKmvtlmqEKNDLQLQVQAEADSLADAEERCDQLIKTKIQ 918
Cdd:PTZ00121 1303 KADEAKKKAE-EAKKAD---------------EAKKKAEEAK------KKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 919 LEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLEltlAKVEKEKHATENKVKnlTEEMAGLDETIAKLTK 998
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK---KKADELKKAAAAKKK--ADEAKKKAEEKKKADE 1435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 999 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIrmdlERAKRKLEGDLKLAQESTMDIENDKQ 1078
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA----DEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1079 QLDEKL---KKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLE 1155
Cdd:PTZ00121 1512 ADEAKKaeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE 1591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1156 EAGGATSAQIEMNKKREAEfqKMRRDLEEATLQHEATAATLRKKhadSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDL 1235
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAE--EAKKAEEAKIKAEELKKAEEEKK---KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1236 ASNMETvSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQ 1315
Cdd:PTZ00121 1667 AKKAEE-DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1316 IEELKRQLEEEIK----AKSALAHALQSSRHDCDLLREQYEEEQEA-KAELQRAM--SKANSEVAQWRTKYETDAIQRTE 1388
Cdd:PTZ00121 1746 AEEAKKDEEEKKKiahlKKEEEKKAEEIRKEKEAVIEEELDEEDEKrRMEVDKKIkdIFDNFANIIEGGKEGNLVINDSK 1825
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1389 ELEEAKKKlaqrlqdaeehvEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNaacaaldkKQRNFDK---ILAEWKQKCE 1465
Cdd:PTZ00121 1826 EMEDSAIK------------EVADSKNMQLEEADAFEKHKFNKNNENGEDGN--------KEADFNKekdLKEDDEEEIE 1885
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 115527082 1466 ETHAELEASQKE-SRSLSTELFKIKN--AYEESLDQLETLKRENKNLQQEISDLTEQ 1519
Cdd:PTZ00121 1886 EADEIEKIDKDDiEREIPNNNMAGKNndIIDDKLDKDEYIKRDAEETREEIIKISKK 1942
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1212-1911 |
8.15e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 80.78 E-value: 8.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1212 DNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLiNDLTAQRARLQTESGEY 1291
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1292 SRQLDEKDTLVSQLSRgkqafTQQIEELKRQLEEEIKAKSALAHALQssrhdcdllreqyeEEQEAKAELQRAMSKANSE 1371
Cdd:TIGR00618 266 RARIEELRAQEAVLEE-----TQERINRARKAAPLAAHIKAVTQIEQ--------------QAQRIHTELQSKMRSRAKL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1372 VAQWRtkyetdAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTK-------QRLQNEVEDLMIDVERTNAACA 1444
Cdd:TIGR00618 327 LMKRA------AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIScqqhtltQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1445 ALDKKQRNFDKILAE------WKQKCEETHAELEASQKESRSLSTelfkiknAYEESLDQLETLKRENKNLQQEISDLTE 1518
Cdd:TIGR00618 401 ELDILQREQATIDTRtsafrdLQGQLAHAKKQQELQQRYAELCAA-------AITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1519 QIAEGgKRIHELEKIKKQVEQEKSELQAALE-EAEASLEHEEGK-------------ILRIQLELNQVKSEVDRKIAEKD 1584
Cdd:TIGR00618 474 QLQTK-EQIHLQETRKKAVVLARLLELQEEPcPLCGSCIHPNPArqdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1585 EEIDQMKRNHIRIVESMQSTLDAEI---RSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHL 1661
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1662 DDALRSQEDLKEQLAMVERRANLLQAEIEE-LRATLEQTERSRKIAEQELLDASERVQLLhTQNTSLINTKKKLETDISQ 1740
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTQERVREhALSIRVLPKELLASRQLALQKMQSEKEQL-TYWKEMLAQCQTLLRELET 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1741 IQGEMEDIIQEARNAEEKAKKAITD----AAMMAEELKKEQDTS-AHLERMKKNLEQTVKDLQHRLDEAEQLalkggkkq 1815
Cdd:TIGR00618 712 HIEEYDREFNEIENASSSLGSDLAAredaLNQSLKELMHQARTVlKARTEAHFNNNEEVTAALQTGAELSHL-------- 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1816 IQKLEARVRELEgEVESEQKRNVEAVKGLRKHERKVKELT-YQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSN 1894
Cdd:TIGR00618 784 AAEIQFFNRLRE-EDTHLLKTLEAEIGQEIPSDEDILNLQcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
730
....*....|....*..
gi 115527082 1895 VNLSKFRRIQHELEEAE 1911
Cdd:TIGR00618 863 QLTQEQAKIIQLSDKLN 879
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
844-1729 |
1.16e-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: 80.22 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 844 LKSAETEKEmanmkeefektkeelakteakRKELEEKMvtlmqekNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKI 923
Cdd:pfam01576 419 ARLSESERQ---------------------RAELAEKL-------SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 924 KEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKAL 1003
Cdd:pfam01576 471 QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1004 QEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLegDLKLAQESTmdiendkqqldek 1083
Cdd:pfam01576 551 QRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKF--DQMLAEEKA------------- 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1084 lkkkefemsgLQSKIEDEQalgmqlqkkikelqarieeleeeieaeraSRAKAEkqrsdlSREleeiserleeaggatsa 1163
Cdd:pfam01576 616 ----------ISARYAEER-----------------------------DRAEAE------ARE----------------- 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1164 qiemnkkREAEFQKMRRDLEEAtlqheataatlrkkhadsvaelgeqidnlQRVKQKLEKEKSEMKMEIDDLASNMETVS 1243
Cdd:pfam01576 634 -------KETRALSLARALEEA-----------------------------LEAKEELERTNKQLRAEMEDLVSSKDDVG 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1244 KAKGNLEKMCRALEDQLSEIKTKEEEqqrLINDLTA-QRARLQTESgeysrqldEKDTLVSQLSRGKQAFTQQIEELKRQ 1322
Cdd:pfam01576 678 KNVHELERSKRALEQQVEEMKTQLEE---LEDELQAtEDAKLRLEV--------NMQALKAQFERDLQARDEQGEEKRRQ 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1323 LEEEIKAKSAlahalqssrhdcdllreqyEEEQEAKaelQRAMSKAnsevaqwrtkyetdaiqrteeleeAKKKLAQRLQ 1402
Cdd:pfam01576 747 LVKQVRELEA-------------------ELEDERK---QRAQAVA------------------------AKKKLELDLK 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1403 DAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAAcaaldkkqrnFDKILAEWKQkceethaeleaSQKESRSLS 1482
Cdd:pfam01576 781 ELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARAS----------RDEILAQSKE-----------SEKKLKNLE 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1483 TELFKIKnayeeslDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKI 1562
Cdd:pfam01576 840 AELLQLQ-------EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1563 LRIQLELNQVKSEV--DRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAirLKKKMEGDLNEMEIQLNHANRMA 1640
Cdd:pfam01576 913 RKSTLQVEQLTTELaaERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKS--SIAALEAKIAQLEEQLEQESRER 990
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1641 AEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLL 1720
Cdd:pfam01576 991 QAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESM 1070
|
....*....
gi 115527082 1721 HTQNTSLIN 1729
Cdd:pfam01576 1071 NREVSTLKS 1079
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1030-1571 |
1.77e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.57 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1030 KLEQQVDDLEGSLEQEKKIRMDLERAKRKLE--GDLKLAQESTMDIENDKQQLDEklkkkefemsgLQSKIEDEQAlgmq 1107
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEY-----------LRAALRLWFA---- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1108 lQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIE-----MNKKRE------AEFQ 1176
Cdd:COG4913 287 -QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEreierLERELEererrrARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1177 KMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGN----LEKM 1252
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNiparLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1253 CRALEDQLS-------------EIKTKEEEQQ----RLINDltaQRARLQTESGEYSRQLDekdtLVSQLSRGKQAFTQQ 1315
Cdd:COG4913 446 RDALAEALGldeaelpfvgeliEVRPEEERWRgaieRVLGG---FALTLLVPPEHYAAALR----WVNRLHLRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1316 IEELKRQLEEEIKAKSALAHALQSSRHDC-DLLREQYEEEQ-----EAKAELQRA--------MSKANSEVAQ------W 1375
Cdd:COG4913 519 VRTGLPDPERPRLDPDSLAGKLDFKPHPFrAWLEAELGRRFdyvcvDSPEELRRHpraitragQVKGNGTRHEkddrrrI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1376 RTKYET--DAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQN--EVEDLMIDVERTNAACAALDKKQR 1451
Cdd:COG4913 599 RSRYVLgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1452 NFDK---ILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISdlTEQIAEGGKRIH 1528
Cdd:COG4913 679 RLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERFA 756
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 115527082 1529 ELeKIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQ 1571
Cdd:COG4913 757 AA-LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1385-1889 |
5.71e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.80 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1385 QRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKqrlqNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKC 1464
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1465 EETHaELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKqveqEKSEL 1544
Cdd:PRK03918 276 EELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK----KLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1545 QAALEEAEASLEHEEgKILRIQLELNQVKSEVD----RKIAEKDEEIDQMK---RNHIRIVESMQSTLDAEIRSRNDAI- 1616
Cdd:PRK03918 351 EKRLEELEERHELYE-EAKAKKEELERLKKRLTgltpEKLEKELEELEKAKeeiEEEISKITARIGELKKEIKELKKAIe 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1617 ----------------------RLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDtqlhlDDALRSQEDLKEQ 1674
Cdd:PRK03918 430 elkkakgkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-----ESELIKLKELAEQ 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1675 LAMVERRANLLQAEIEELRATLEQT--ERSRKIAEQ--ELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDI-- 1748
Cdd:PRK03918 505 LKELEEKLKKYNLEELEKKAEEYEKlkEKLIKLKGEikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgf 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1749 ---------IQEARNAEEK---AKKAITDAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQI 1816
Cdd:PRK03918 585 esveeleerLKELEPFYNEyleLKDAEKELEREEKELKKLEEE---LDKAFEELAETEKRLEELRKELEELEKKYSEEEY 661
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115527082 1817 QKLEARVRELEGEVESEQKRNVEAVKGLRKHERKVKELTYQTEEDRKNILRLQDL------VDKLQAKVKSYKRQAEEA 1889
Cdd:PRK03918 662 EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLekalerVEELREKVKKYKALLKER 740
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
33-77 |
6.34e-14 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 67.46 E-value: 6.34e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 115527082 33 DAKTSVFVVDPKESFVKATVQSREGGKVTAKTEAGATVTVKDDQV 77
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1041-1934 |
1.19e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 77.01 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1041 SLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKiEDEQALGMQLQKKIKELQARIE 1120
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY-ENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1121 ELEeeieAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREA-EFQKMRRDLEEATLQHEATAATLRKK 1199
Cdd:TIGR00606 266 KLD----NEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1200 HADSVAELGE-----QIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQ-------LSEIKTKE 1267
Cdd:TIGR00606 342 KTELLVEQGRlqlqaDRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEaktaaqlCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1268 EEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLL 1347
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1348 REQYeeEQEAKAELQRAMSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQDAE-EHVEAVNAKCA------SLEK 1420
Cdd:TIGR00606 502 EVKS--LQNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQIRKIKsRHSDELTSLLGyfpnkkQLED 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1421 TKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILaEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLE 1500
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNEL-ESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRA 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1501 TLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQV-------K 1573
Cdd:TIGR00606 657 MLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQ 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1574 SEVDRKIAEKDEEIDQMK---------RNHIRIVESMQSTLDAEIRSRND-----AIRLKKKMEGDLNEMEIQLNHANRM 1639
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQkvnrdiqrlKNDIEEQETLLGTIMPEEESAKVcltdvTIMERFQMELKDVERKIAQQAAKLQ 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1640 AAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEEL---RATLEQTERSRKIAEQELLDASER 1716
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELkseKLQIGTNLQRRQQFEEQLVELSTE 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1717 VQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQearNAEEKAKKAITDAAMMAEELKK--------EQDTSAHLERMKK 1788
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS---SKETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDDYLK 973
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1789 NLEQTVKDLQHRLDEAEQlalkgGKKQIQKlEARVRELEGEVESEQKRNVEAVKGLRKHERKVKEL-----TYQTEEDRK 1863
Cdd:TIGR00606 974 QKETELNTVNAQLEECEK-----HQEKINE-DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVeeelkQHLKEMGQM 1047
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115527082 1864 NILRLQDLVDKLQAKVKSYKR-------QAEEAEEQSNVNLSKFRRIQHELEEAEERADIAESQVNKLRVKSREVHTK 1934
Cdd:TIGR00606 1048 QVLQMKQEHQKLEENIDLIKRnhvlalgRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYK 1125
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1259-1925 |
1.24e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 76.75 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1259 QLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQ-----------------LSRGKQAFTQQIEELKR 1321
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQlqaetelcaeaeemrarLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1322 QLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTeELEEAKKKLAQRL 1401
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNS-KLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1402 QDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKESRSL 1481
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1482 STELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGK 1561
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1562 ILRIQLELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAA 1641
Cdd:pfam01576 322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1642 EALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMverranlLQAEIEELRATLEQTE----RSRK---IAEQELLDAS 1714
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK-------LQSELESVSSLLNEAEgkniKLSKdvsSLESQLQDTQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1715 ERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTV 1794
Cdd:pfam01576 475 ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1795 KDLQHRLDEAEQlalkggkkQIQKLEARVRELEGEVES---EQKRNVEAVKGLRKHERKVKELtyqTEEDRKNILRLQDL 1871
Cdd:pfam01576 555 EALTQQLEEKAA--------AYDKLEKTKNRLQQELDDllvDLDHQRQLVSNLEKKQKKFDQM---LAEEKAISARYAEE 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 115527082 1872 VDKLQAkvksykrqaeEAEEQSNVNLSkfrrIQHELEEAEERADIAESQVNKLR 1925
Cdd:pfam01576 624 RDRAEA----------EAREKETRALS----LARALEEALEAKEELERTNKQLR 663
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1386-1935 |
2.43e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.72 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1386 RTEELEEakKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLqneveDLMIDVERTNAACAALDKKQRNFDKILAewkqkce 1465
Cdd:COG4913 214 REYMLEE--PDTFEAADALVEHFDDLERAHEALEDAREQI-----ELLEPIRELAERYAAARERLAELEYLRA------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1466 etHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAE-GGKR-------IHELEKIKKQV 1537
Cdd:COG4913 280 --ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRleqlereIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1538 EQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQMKRNH-------------IRIVESMQST 1604
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALrdlrrelreleaeIASLERRKSN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1605 LDAEIRSRNDAIR--LKKKME-----GDLneMEIQLNHAN-RMAAE-ALRNYRNTqaILKDTQlHLDDALR--SQEDLKE 1673
Cdd:COG4913 438 IPARLLALRDALAeaLGLDEAelpfvGEL--IEVRPEEERwRGAIErVLGGFALT--LLVPPE-HYAAALRwvNRLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1674 QLamverranllqaeieelratleQTERSRKIAEQELLDASERVQLLHtqntslintkkKLETDISQIQGEMEDIIQE-- 1751
Cdd:COG4913 513 RL----------------------VYERVRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLEAELGRrf 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1752 ----ARNAEE--KAKKAITDAAMMaeelkkeqdtsahlermKKNLEQTVKDLQHRLDEAEQLalkGG--KKQIQKLEARV 1823
Cdd:COG4913 560 dyvcVDSPEElrRHPRAITRAGQV-----------------KGNGTRHEKDDRRRIRSRYVL---GFdnRAKLAALEAEL 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1824 RELEGEVESEQKRnVEAVKGLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKvksykRQAEEAEEQSNvnlSKFRRI 1903
Cdd:COG4913 620 AELEEELAEAEER-LEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAEL-----EAELERLDASS---DDLAAL 690
|
570 580 590
....*....|....*....|....*....|..
gi 115527082 1904 QHELEEAEERADIAESQVNKLRVKSREVHTKI 1935
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKEL 722
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1574-1892 |
2.92e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.49 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1574 SEVDRKIAEKDEEIDQMKRNHIRIvesmqSTLDAEIRSRNDaiRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAI 1653
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERL-----DLIIDEKRQQLE--RLRREREKAERYQALLKEKREYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1654 LKDTQLHLDDALRSQEDLKEQL----------------------AMVERRANLLQAEIEELRATLEQTERSRKIAEQELL 1711
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEIselekrleeieqlleelnkkikDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1712 DASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKEQDTSA----HLERMK 1787
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyreKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1788 KNLEQTVKDLQHRLDEAEQLALKGG--KKQIQKLEARVRELEGEVESEQKRnveavkgLRKHERKVKELTYQTEEDRKNI 1865
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELAdlNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQEL 471
|
330 340
....*....|....*....|....*..
gi 115527082 1866 LRLQDLVDKLQAKVKSYKRQAEEAEEQ 1892
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
914-1630 |
3.95e-13 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 74.76 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 914 KTKIQLEAKIKEVTERAEDEEEINAELTAkkRKLEDECSELKKDIddleltlakveKEKHATENKVKNLTEEMAGLDETI 993
Cdd:pfam05483 105 ENKLQENRKIIEAQRKAIQELQFENEKVS--LKLEEEIQENKDLI-----------KENNATRHLCNLLKETCARSAEKT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 994 AKLTKEKkalqEAHQQTLDDLQAEEDKVNTLTKakiklEQQVDDLEGSLEQEKKIRMDLERAKRklegdlkLAQESTMDI 1073
Cdd:pfam05483 172 KKYEYER----EETRQVYMDLNNNIEKMILAFE-----ELRVQAENARLEMHFKLKEDHEKIQH-------LEEEYKKEI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1074 ENDKQQLDEKL---KKKEFEMSGLQSKIEDEQALGMQLQKKIKelqarieeleeeieAERASRAKAEKQRSDLSRELEEI 1150
Cdd:pfam05483 236 NDKEKQVSLLLiqiTEKENKMKDLTFLLEESRDKANQLEEKTK--------------LQDENLKELIEKKDHLTKELEDI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1151 SERLEEAggatsaqIEMNKKREAEFQKMRRDLEEATLQHEATAATLRK---KHADSVAELGEQIDNLQRV----KQKLEK 1223
Cdd:pfam05483 302 KMSLQRS-------MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKakaAHSFVVTEFEATTCSLEELlrteQQRLEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1224 EKSEMK---MEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKT---KEEEQQRLINDLTAQRARLQTESGEYSRQLDE 1297
Cdd:pfam05483 375 NEDQLKiitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHD 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1298 KDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAhalqssrHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRt 1377
Cdd:pfam05483 455 LEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELT-------AHCDKLLLENKELTQEASDMTLELKKHQEDIINCK- 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1378 KYETDAIQRTEELEEAKKKLAQRLQDAEEHV----EAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNF 1453
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENK 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1454 DKILaewkqkcEETHAELEASQKESRSLSTELfkikNAYEESLDQLETLKRENKNLQQEISDLTEQIAEgGKRIHElEKI 1533
Cdd:pfam05483 607 NKNI-------EELHQENKALKKKGSAENKQL----NAYEIKVNKLELELASAKQKFEEIIDNYQKEIE-DKKISE-EKL 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1534 KKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDqMKRNHIRIVESMQSTLDAEIRS-R 1612
Cdd:pfam05483 674 LEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG-LYKNKEQEQSSAKAALEIELSNiK 752
|
730
....*....|....*...
gi 115527082 1613 NDAIRLKKKMEGDLNEME 1630
Cdd:pfam05483 753 AELLSLKKQLEIEKEEKE 770
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
844-1428 |
5.60e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 74.31 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 844 LKSAETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADS---LADAEERCDQLIKTKIQLE 920
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERreeLETLEAEIEDLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 921 AKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV-------KNLTEEMAGLDETI 993
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLeecrvaaQAHNEEAESLREDA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 994 AKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQekkIRMDLERAKRKLEgdlklaqestmDI 1073
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD---APVDLGNAEDFLE-----------EL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1074 ENDKQQLDEKLKKKEFEMSGLQSKIEDEQALgmQLQKKIKEL--QARIEELEEEIEAERASRAKAEKQRSDLSRELEEIS 1151
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEAL--LEAGKCPECgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1152 ERLEEAGGATSAQIEMNKKREAefqkmRRDLEEATLQHEATAATLRKKHA---DSVAELGEQIDNLQRVKQKLEKEKSEM 1228
Cdd:PRK02224 496 ERLERAEDLVEAEDRIERLEER-----REDLEELIAERRETIEEKRERAEelrERAAELEAEAEEKREAAAEAEEEAEEA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1229 KMEIDDLASNMETVSKAKGNLEKmcraLEDQLSEIKTKEEEQQRLiNDLTAQRARLQTESGEYsrqLDEKdtlvsqlsrg 1308
Cdd:PRK02224 571 REEVAELNSKLAELKERIESLER----IRTLLAAIADAEDEIERL-REKREALAELNDERRER---LAEK---------- 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1309 kqaftqqiEELKRQLEEEIKAksALAHALQSSRHDCDLLREQYEEE----QEAKAELQRAMSKANSEvaqwrtkyetdaI 1384
Cdd:PRK02224 633 --------RERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKldelREERDDLQAEIGAVENE------------L 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 115527082 1385 QRTEELEEAKKKLAQRLQDaeehVEAVNAKCASLEKTKQRLQNE 1428
Cdd:PRK02224 691 EELEELRERREALENRVEA----LEALYDEAEELESMYGDLRAE 730
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1250-1939 |
6.63e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.33 E-value: 6.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1250 EKMCRALEDqLSEIKTKEEEQQRLINDLTAQRARLQTESG---EYSRQLDEK-DTLVSQLSRGKQAFTQQIEELKRQL-- 1323
Cdd:TIGR02169 170 RKKEKALEE-LEEVEENIERLDLIIDEKRQQLERLRREREkaeRYQALLKEKrEYEGYELLKEKEALERQKEAIERQLas 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1324 -EEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAE-----LQRAMSKANSEVAQWRtkyetDAIqrtEELEEAKKKL 1397
Cdd:TIGR02169 249 lEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrVKEKIGELEAEIASLE-----RSI---AEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1398 AQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKE 1477
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1478 SRSLSTELFKIknayeesLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEH 1557
Cdd:TIGR02169 401 INELKRELDRL-------QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1558 EEGKILRIQLELNQVKSEVDRKIAEKDEeIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGdlnemEIQLNHAN 1637
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARA-SEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYAT-----AIEVAAGN 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1638 RM----------AAEALrNYRNTQAILKDTQLHLDDaLRSQEDLKEQLAM---VERRANLLQAEiEELRATLEQTERSRK 1704
Cdd:TIGR02169 548 RLnnvvveddavAKEAI-ELLKRRKAGRATFLPLNK-MRDERRDLSILSEdgvIGFAVDLVEFD-PKYEPAFKYVFGDTL 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1705 IAEQelLDASERVQLLHTQNTslintkkkLETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKeqdtsahLE 1784
Cdd:TIGR02169 625 VVED--IEAARRLMGKYRMVT--------LEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEG-------LK 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1785 RMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELEGEVESEQKRnveavkgLRKHERKVKELTYQTEEDRKN 1864
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQ-ELSDASRKIGEIEKEIEQLEQEEEKLKER-------LEELEEDLSSLEQEIENVKSE 759
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115527082 1865 ILRLQDLVDKLQAKVKSYkrQAEEAEEQSNVNLSKFRRIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1939
Cdd:TIGR02169 760 LKELEARIEELEEDLHKL--EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
905-1432 |
7.87e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 905 AEERCDQLIKTKIQ-LEAKIKEVTERAEDEEEINAELtAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLT 983
Cdd:PRK03918 187 RTENIEELIKEKEKeLEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 984 EEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLtKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDL 1063
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1064 KLAQESTMDIE--NDKQQLDEKLKKKEFEMSGLQSKIEDEqalgmQLQKKIKELQarieeleeeieaerasraKAEKQRS 1141
Cdd:PRK03918 345 KKLKELEKRLEelEERHELYEEAKAKKEELERLKKRLTGL-----TPEKLEKELE------------------ELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1142 DLSRELEEISER---LEEAGGATSAQIEMNKKREAEFQKMRRDLEE---ATLQHEATAATlrKKHADSVAELGEQIDNLQ 1215
Cdd:PRK03918 402 EIEEEISKITARigeLKKEIKELKKAIEELKKAKGKCPVCGRELTEehrKELLEEYTAEL--KRIEKELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1216 RVKQKLEKEKS---------EMKMEIDDLAS-----NMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLiNDLTAQR 1281
Cdd:PRK03918 480 KELRELEKVLKkeseliklkELAEQLKELEEklkkyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL-EELKKKL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1282 ARLQTESGEYSRQLDEKDTLVSQLSRGK-QAFTQQIEELKRQLEEEIKAKSAlAHALQSSRHDCDLLREQYEEEQEAKAE 1360
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYNEYLELKDA-EKELEREEKELKKLEEELDKAFEELAE 637
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115527082 1361 LQRAMSKANSEVAQWRTKYETDaiqRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDL 1432
Cdd:PRK03918 638 TEKRLEELRKELEELEKKYSEE---EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1204-1710 |
8.56e-13 |
|
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: 73.62 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1204 VAELGEQIDNLQRVKQKLEKE----KSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQqrlindltA 1279
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEhkraRIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQ--------A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1280 QRARLQTESGE-YSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAK 1358
Cdd:pfam05557 76 ELNRLKKKYLEaLNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1359 AELQRAMSKAnsevaqwrtkyeTDAIQRTEELEeakKKLAQRLQDAEEhVEAVNAKCAS---LEKTKQRLQNEVEDLmid 1435
Cdd:pfam05557 156 QNLEKQQSSL------------AEAEQRIKELE---FEIQSQEQDSEI-VKNSKSELARipeLEKELERLREHNKHL--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1436 veRTNAACAALDKKQRNFDKILAEwkqKCEETHAELEASQKESRSLSTEL---FKIKNAYEESLDQLETLKRENKNLQQE 1512
Cdd:pfam05557 217 --NENIENKLLLKEEVEDLKRKLE---REEKYREEAATLELEKEKLEQELqswVKLAQDTGLNLRSPEDLSRRIEQLQQR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1513 ISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQlelnqvksevdRKIAEKDEEIDQMKr 1592
Cdd:pfam05557 292 EIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-----------RRVLLLTKERDGYR- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1593 nhiRIVESMQSTLDAEIRSRNDAIRLK------KKMEGDLNEMEIQLNHANRMAAEalrnyRNTQAILKDTQLhldDALR 1666
Cdd:pfam05557 360 ---AILESYDKELTMSNYSPQLLERIEeaedmtQKMQAHNEEMEAQLSVAEEELGG-----YKQQAQTLEREL---QALR 428
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 115527082 1667 SQEDLKEQLAMVERRANLLQaEIEELRATLEQTERSRKIAEQEL 1710
Cdd:pfam05557 429 QQESLADPSYSKEEVDSLRR-KLETLELERQRLREQKNELEMEL 471
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
839-1325 |
1.43e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 73.13 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 839 KIKPLLKSAETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQL------ 912
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIknkllk 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 913 -------IKTKIQ----LEAKI-----------KEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEK 970
Cdd:TIGR04523 199 lelllsnLKKKIQknksLESQIselkkqnnqlkDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 971 ekhaTENKVKNLTEEMAGLDETIAKLTKEKKalQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRM 1050
Cdd:TIGR04523 279 ----NNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1051 DLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAER 1130
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1131 ASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATL------RKKHADSV 1204
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkklneeKKELEEKV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1205 AELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMEtvskaKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARL 1284
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN-----KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEK 587
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 115527082 1285 QTESGEYSrqlDEKDTLVSQLSrgkqAFTQQIEELKRQLEE 1325
Cdd:TIGR04523 588 QELIDQKE---KEKKDLIKEIE----EKEKKISSLEKELEK 621
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
850-1544 |
3.05e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 72.31 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 850 EKEMANMKEEFEKTKEELAKTEAKRKELEEKMvTLMQEKNDLQLQVQ---AEADSLADAEERCDQLIKtKIQLEAKIKEV 926
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYLTQKREAQEEQL-KKQQLLKQLRARIEelrAQEAVLEETQERINRARK-AAPLAAHIKAV 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 927 TERAEDEEEINAELTAKKRKLEDE---CSELKKDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKAL 1003
Cdd:TIGR00618 303 TQIEQQAQRIHTELQSKMRSRAKLlmkRAAHVKQQSSIE-EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1004 QEAHQQtlddLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQldek 1083
Cdd:TIGR00618 382 HTLQQQ----KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQC---- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1084 LKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERleeagGATSA 1163
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNP-----GPLTR 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1164 QIEMNKKREAEFQKmrrdlEEATLQHEATAATLRkkhadsVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVS 1243
Cdd:TIGR00618 529 RMQRGEQTYAQLET-----SEEDVYHQLTSERKQ------RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1244 KAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQL 1323
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLAS 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1324 EEeikaksALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETdaiqRTEELEEAKKKLAQRLQD 1403
Cdd:TIGR00618 678 RQ------LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSS----LGSDLAAREDALNQSLKE 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1404 AEEhvEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAAcAALDKKQRNFDKILAEWKQKcEETHAELEASQKESRSLST 1483
Cdd:TIGR00618 748 LMH--QARTVLKARTEAHFNNNEEVTAALQTGAELSHLA-AEIQFFNRLREEDTHLLKTL-EAEIGQEIPSDEDILNLQC 823
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115527082 1484 ELFkiknayEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSEL 1544
Cdd:TIGR00618 824 ETL------VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1184-1761 |
3.34e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 71.68 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1184 EATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEiddLASNMETVSKAKGNLEKMCRALEDQLSEI 1263
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFK---LKEDHEKIQHLEEEYKKEINDKEKQVSLL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1264 KTKEEEQQRLINDLTAqrarLQTESGEYSRQLDEKDTLVS----QLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQ- 1338
Cdd:pfam05483 246 LIQITEKENKMKDLTF----LLEESRDKANQLEEKTKLQDenlkELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQi 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1339 SSRHDCDLLRE---QYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDAEEHVEavnakc 1415
Cdd:pfam05483 322 ATKTICQLTEEkeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QRLEKNEDQLKIITMELQKKSSELE------ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1416 aslEKTKQRLQNEVEdlMIDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEES 1495
Cdd:pfam05483 395 ---EMTKFKNNKEVE--LEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1496 LDQLETLKR---------------------ENKNLQQEISDLT-------EQIAEGGKRIHELEKIKKQVEQEKSELQAA 1547
Cdd:pfam05483 470 LKEVEDLKTelekeklknieltahcdklllENKELTQEASDMTlelkkhqEDIINCKKQEERMLKQIENLEEKEMNLRDE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1548 LEEAEASL--EHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEG- 1624
Cdd:pfam05483 550 LESVREEFiqKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENk 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1625 -------DLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANL-LQAEIEELRATL 1696
Cdd:pfam05483 630 qlnayeiKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKrCQHKIAEMVALM 709
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115527082 1697 EQTERS-RKIAEQElldaSERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKK 1761
Cdd:pfam05483 710 EKHKHQyDKIIEER----DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEK 771
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
871-1450 |
3.85e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 72.07 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 871 EAKRKELEEKMVTLMQEKNDLQLQVQAEAD----------SLADAEERCDQLIKTKIQLEAK------IKEVTERAEDEE 934
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQDRIEQLISEHEveitgltekaSSARSQANSIQSQLEIIQEQARnqnsmyMRQLSDLESTVS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 935 EINAELTAKKRKLEDECSELKKD--IDDLELTLAKVEKEKHATENkvKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLD 1012
Cdd:pfam15921 328 QLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKLLADLHKREKELSLEKEQNKRLWD 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1013 dlqaeEDKVNTLTkakikleqqVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLkkkefemS 1092
Cdd:pfam15921 406 -----RDTGNSIT---------IDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKV-------S 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1093 GLQSKIEDEQALgmqLQKKIKELqarieeleeeiEAERASRAKAEKQRSDLSRELEEISERLEeaggATSAQIEMNKKRE 1172
Cdd:pfam15921 465 SLTAQLESTKEM---LRKVVEEL-----------TAKKMTLESSERTVSDLTASLQEKERAIE----ATNAEITKLRSRV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1173 ----AEFQKMRRDLEE-ATLQHEATAATLRKKHADSVAE-LGEQIDNLQ-------RVKQKLEKEKSEMKMEIDDLASNM 1239
Cdd:pfam15921 527 dlklQELQHLKNEGDHlRNVQTECEALKLQMAEKDKVIEiLRQQIENMTqlvgqhgRTAGAMQVEKAQLEKEINDRRLEL 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1240 ETVSKAKGNLEKMCRALEDQLSEIKTKE-------EEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAF 1312
Cdd:pfam15921 607 QEFKILKDKKDAKIRELEARVSDLELEKvklvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNK 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1313 TQQIEELKRQLEEEIKAKSAlahALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYE------TDAIQR 1386
Cdd:pfam15921 687 SEEMETTTNKLKMQLKSAQS---ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQfleeamTNANKE 763
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115527082 1387 TEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTN---AACAALDKKQ 1450
Cdd:pfam15921 764 KHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASlqfAECQDIIQRQ 830
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
839-1273 |
7.08e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 7.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 839 KIKPLLKSAETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLMQEKNDLQLQVQaeadSLADAEERCDQLIKTKIQ 918
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 919 LEAKIKEVTERAEDEEEINAeLTAKKRKLEDECSELkkDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTK 998
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKA-KKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 999 EKKALQEAHQQ--TLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTM--DIE 1074
Cdd:PRK03918 427 AIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1075 NDKQQLD----EKLKKKEFEMSGLQSK---IEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRE- 1146
Cdd:PRK03918 507 ELEEKLKkynlEELEKKAEEYEKLKEKlikLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEs 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1147 LEEISERLEEAGGATSAQIEM-NKKREAEFQKMRRDLEEATLqhEATAATLRKKHADsVAELGEQIDNLQRV-----KQK 1220
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLELkDAEKELEREEKELKKLEEEL--DKAFEELAETEKR-LEELRKELEELEKKyseeeYEE 663
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 115527082 1221 LEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRL 1273
Cdd:PRK03918 664 LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL 716
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
891-1663 |
7.16e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 71.23 E-value: 7.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 891 LQLQVQAEADSL---ADAEERCDQLIKTKIqlEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAK 967
Cdd:TIGR00606 371 QSLATRLELDGFergPFSERQIKNFHTLVI--ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 968 VEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAhqqtldDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKK 1047
Cdd:TIGR00606 449 LEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEREL------SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQ 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1048 IRMDLERAKRKLEGDLKLAQESTmdieNDKQQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIE 1127
Cdd:TIGR00606 523 EMEQLNHHTTTRTQMEMLTKDKM----DKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNK 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1128 AERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEmnkkrEAEFQKMRRDLEEATLQhEATAATLRKKHADSVAEL 1207
Cdd:TIGR00606 599 ELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE-----ESDLERLKEEIEKSSKQ-RAMLAGATAVYSQFITQL 672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1208 GEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTaqrarlqte 1287
Cdd:TIGR00606 673 TDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKE--------- 743
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1288 sgeysRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLeEEIKAKSALAHALQSsrhDCDLLREQYEEEQEAKAELQRAMSK 1367
Cdd:TIGR00606 744 -----KEIPELRNKLQKVNRDIQRLKNDIEEQETLL-GTIMPEEESAKVCLT---DVTIMERFQMELKDVERKIAQQAAK 814
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1368 ANSeVAQWRTKYETDaiQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALD 1447
Cdd:TIGR00606 815 LQG-SDLDRTVQQVN--QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLV 891
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1448 KKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGgkri 1527
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDG---- 967
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1528 heLEKIKKQVEQEKSELQAALEEAEASLE----------------HEEGKILRIQLELNQVKS---EVDRKIAEKDEEID 1588
Cdd:TIGR00606 968 --KDDYLKQKETELNTVNAQLEECEKHQEkinedmrlmrqdidtqKIQERWLQDNLTLRKRENelkEVEEELKQHLKEMG 1045
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115527082 1589 QMKRNHIRIV-ESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEAlrNYRNTQAILKDTQLHLDD 1663
Cdd:TIGR00606 1046 QMQVLQMKQEhQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEE--KYREMMIVMRTTELVNKD 1119
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1215-1892 |
1.18e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.05 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1215 QRVKQKLEKEKSEMK---MEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEY 1291
Cdd:TIGR04523 36 KQLEKKLKTIKNELKnkeKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1292 SRQLDEKDTLVSQLSRGKQaftqQIEELKRQLEEEIKAKSALahaLQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSE 1371
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKK----ENKKNIDKFLTEIKKKEKE---LEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1372 VAQWRTKYetdaiQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQR 1451
Cdd:TIGR04523 189 IDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1452 NFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLD-----QLETLKRENKNLQQEISDLTEQIAEGGKR 1526
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNkelksELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1527 IHELEKIKKQVEQEKSELQAALEEAEASLEHE----EGKILRIQlELNQVKSEVDRKIaEKDEEIDQMKRNHIRIVESMQ 1602
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLkkenQSYKQEIK-NLESQINDLESKI-QNQEKLNQQKDEQIKKLQQEK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1603 STLDAEIRsrndairlkkkmegDLNEMEIQLNhanrmaaEALRNYRNTQAILKDTQLHLDdalRSQEDLKEQLAMVERRA 1682
Cdd:TIGR04523 422 ELLEKEIE--------------RLKETIIKNN-------SEIKDLTNQDSVKELIIKNLD---NTRESLETQLKVLSRSI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1683 NLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIiqearnaEEKAKKa 1762
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL-------EDELNK- 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1763 itdaamMAEELKKEQdtsahLERMKKNLEQTVKDLQHrldeaeqlalkggkkQIQKLEARVRELEGEVESEQKRNVEAVK 1842
Cdd:TIGR04523 550 ------DDFELKKEN-----LEKEIDEKNKEIEELKQ---------------TQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 115527082 1843 GLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQ 1892
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1202-1701 |
1.99e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.56 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1202 DSVAELGEQIDNLQRVKQKLEKEKSEMKM--EIDDLASNMETVSKAKGNLEKMCRALEDQLSEikTKEEEQQRLINDLTA 1279
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1280 QRARLQTESGEYSRQLDEKDTLVSQLSRGKQAF-TQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAK 1358
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1359 AELQRAMSKANSEVAQWRTKYE---TDAIQRTEELEEAKKKLAQRLQDAE-------EHVEAV-NAKCASLEKTKQRL-- 1425
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEealAEAEAALRDLRRELRELEAEIASLErrksnipARLLALrDALAEALGLDEAELpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1426 --------------QNEVE--------DLMIDVERTNAACAALDK---KQR-NFDKIlaewkqkcEETHAELEASQKESR 1479
Cdd:COG4913 463 vgelievrpeeerwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1480 SLSTELFKIKNAYEESLDQL-------------ETLKRENKNLQQeisdlTEQIAEGGKR-------------------- 1526
Cdd:COG4913 535 SLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRAITR-----AGQVKGNGTRhekddrrrirsryvlgfdnr 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1527 --IHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVD-----RKIAEKDEEIDQMKRNHIRiVE 1599
Cdd:COG4913 610 akLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaeREIAELEAELERLDASSDD-LA 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1600 SMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVE 1679
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
570 580
....*....|....*....|..
gi 115527082 1680 RRanlLQAEIEELRATLEQTER 1701
Cdd:COG4913 769 EN---LEERIDALRARLNRAEE 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1448-1939 |
2.46e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1448 KKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAY---EESLDQLETLKRENKNLQQEISDLTEQIAEGG 1524
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVkelEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1525 KRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKIlriqlELNQVKSEVDRKIAEKDEEIDQMKRnHIRIVESMQST 1604
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE-----EYLDELREIEKRLSRLEEEINGIEE-RIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1605 LDaEIRSRndairlKKKMEGDLNEMEiqlnhanrmaaEALRNYRNTQAILKDTQ-LHLDDALRSQEDLKEQLAMVERRAN 1683
Cdd:PRK03918 340 LE-ELKKK------LKELEKRLEELE-----------ERHELYEEAKAKKEELErLKKRLTGLTPEKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1684 LLQAEIEEL---RATLEQTERSRKIAEQELLDASERVQLLHTQNTSliNTKKKLetdISQIQGEMEDIIQEARNAEEKAK 1760
Cdd:PRK03918 402 EIEEEISKItarIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE--EHRKEL---LEEYTAELKRIEKELKEIEEKER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1761 KAITDAAMMAEELKKEQDtsahLERMKKNLEQtVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVESeQKRNVEA 1840
Cdd:PRK03918 477 KLRKELRELEKVLKKESE----LIKLKELAEQ-LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS-LKKELEK 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1841 VKGLRKHERKVKELTYQTEEDRKNILR---------LQDLVDKLQAKVKSYKR--QAEEAEEQSNVNLSKFRRIQHELEE 1909
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKeleelgfesVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDK 630
|
490 500 510
....*....|....*....|....*....|
gi 115527082 1910 AEERADIAESQVNKLRVKSREVHTKIISEE 1939
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEEE 660
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1263-1877 |
2.52e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1263 IKTKEEEQQRLINDLTaQRARLQtesgEYSRQLDEKDTLVSQLSRGKQaftQQIEELKRQLEE-EIKAKSALAHALQSSR 1341
Cdd:PRK02224 144 INATPSDRQDMIDDLL-QLGKLE----EYRERASDARLGVERVLSDQR---GSLDQLKAQIEEkEEKDLHERLNGLESEL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1342 HDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRtkyetdaiQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKT 1421
Cdd:PRK02224 216 AELDEEIERYEEQREQARETRDEADEVLEEHEERR--------EELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1422 KQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLET 1501
Cdd:PRK02224 288 LEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1502 LKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLE--HEEGKILRIQLElnqvksEVDRK 1579
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDelREREAELEATLR------TARER 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1580 IAEKDEEIDQMKrnhirIVESMQSTLDAEIRSRNDAIRLKK-KMEGDLNEMEIQLNHANRmAAEALRNYRNTQAILKDTQ 1658
Cdd:PRK02224 442 VEEAEALLEAGK-----CPECGQPVEGSPHVETIEEDRERVeELEAELEDLEEEVEEVEE-RLERAEDLVEAEDRIERLE 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1659 LHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLEtDI 1738
Cdd:PRK02224 516 ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RI 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1739 SQIQGEMEDIIQEARNAEEKAKKaitdaamMAEELKKEQDTSAHLERMKKNLEQTVKDlqHRLDEAEQlALKGGKKQIQK 1818
Cdd:PRK02224 595 RTLLAAIADAEDEIERLREKREA-------LAELNDERRERLAEKRERKRELEAEFDE--ARIEEARE-DKERAEEYLEQ 664
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 115527082 1819 LEARVRELEGEVESEQKRnVEAVkglrkhERKVKELtyqtEEDRKNILRLQDLVDKLQA 1877
Cdd:PRK02224 665 VEEKLDELREERDDLQAE-IGAV------ENELEEL----EELRERREALENRVEALEA 712
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1090-1700 |
2.69e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.10 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1090 EMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERL-------EEAGGATS 1162
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELngelsaaDAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1163 AQIEMNKKREAEFQKMrrDLEEATlQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEI--------DD 1234
Cdd:pfam12128 322 SELEALEDQHGAFLDA--DIETAA-ADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNnrdiagikDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1235 LASNMETVSK----AKGNLEKMCRALEDQLSEIKTKEEEQQRLInDLTAQRARLQTESGEYSRQLDE-KDTLVSQLSRGK 1309
Cdd:pfam12128 399 LAKIREARDRqlavAEDDLQALESELREQLEAGKLEFNEEEYRL-KSRLGELKLRLNQATATPELLLqLENFDERIERAR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1310 QAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRA----MSKANSEVAQWRtkyetDAIQ 1385
Cdd:pfam12128 478 EEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQagtlLHFLRKEAPDWE-----QSIG 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1386 RTeeleeAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNevedlmIDVERTNAACAALDKKQRNFDKILAEWKQKCE 1465
Cdd:pfam12128 553 KV-----ISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKR------IDVPEWAASEEELRERLDKAEEALQSAREKQA 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1466 ETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISD-LTEQIAEGGKRIHELEKIKKQVEQEkseL 1544
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKaLAERKDSANERLNSLEAQLKQLDKK---H 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1545 QAALEEA-EASLEHEEGKilriQLELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRN-DAIRLKKkM 1622
Cdd:pfam12128 699 QAWLEEQkEQKREARTEK----QAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGvDPDVIAK-L 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1623 EGDLNEMEIQLNHANRMAAEALRN---YRNTQAILKDT-QLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQ 1698
Cdd:pfam12128 774 KREIRTLERKIERIAVRRQEVLRYfdwYQETWLQRRPRlATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEK 853
|
..
gi 115527082 1699 TE 1700
Cdd:pfam12128 854 QQ 855
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
887-1562 |
2.90e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.10 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 887 EKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEA---KIKEVTERAEDEEEINAELTAKKRkledecSELKKDIDDLEL 963
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHlhfGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 964 TLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAE-----------EDKVNTLT------K 1026
Cdd:pfam12128 302 KRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSElenleerlkalTGKHQDVTakynrrR 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1027 AKIKlEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKlAQESTMDIENDKQQLDEKLKKKEF-----EMSGLQSKIEDE 1101
Cdd:pfam12128 382 SKIK-EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQ-ALESELREQLEAGKLEFNEEEYRLksrlgELKLRLNQATAT 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1102 QALGMQLQKKIKEL---QARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKM 1178
Cdd:pfam12128 460 PELLLQLENFDERIeraREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHF 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1179 RR----DLEEATLQHEATAATLRKK-HADSVAELGEQIDNLQRVKQKLEK-EKSEMKMEIDDLASNMETVSKAKGNLEKM 1252
Cdd:pfam12128 540 LRkeapDWEQSIGKVISPELLHRTDlDPEVWDGSVGGELNLYGVKLDLKRiDVPEWAASEEELRERLDKAEEALQSAREK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1253 CRALEDQLSEIKTKEEEQQRlinDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKaksA 1332
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASR---EETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLK---Q 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1333 LAHALQS-SRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEE-AKKKLAQRLQDaeehvea 1410
Cdd:pfam12128 694 LDKKHQAwLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETwYKRDLASLGVD------- 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1411 vnakcaslEKTKQRLQNEVEDLmidvERTNAACAALDKKQRNFDKI---------------LAEWKQKCEETHAELEASQ 1475
Cdd:pfam12128 767 --------PDVIAKLKREIRTL----ERKIERIAVRRQEVLRYFDWyqetwlqrrprlatqLSNIERAISELQQQLARLI 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1476 KESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQiAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASL 1555
Cdd:pfam12128 835 ADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKED-ANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYV 913
|
....*..
gi 115527082 1556 EHEEGKI 1562
Cdd:pfam12128 914 EHFKNVI 920
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1458-1805 |
8.75e-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: 67.40 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1458 AEWKQKCEETHAELEASQKESRSLSTELfkiknayEESLDQLETLKREnKNLQQEISDLTEQIAEggKRIHELEKIKKQV 1537
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLII-------DEKRQQLERLRRE-REKAERYQALLKEKRE--YEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1538 EQEKSELQAALEEAEASLEHEEGKILRIQLELNqvksEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIR 1617
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLE----EIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1618 LKKKMEGDLNEMEIQLN---HANRMAAEALRNYRNTQAILKDT-QLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELR 1693
Cdd:TIGR02169 312 EKERELEDAEERLAKLEaeiDKLLAEIEELEREIEEERKRRDKlTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1694 ATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAitdAAMMAEEL 1773
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL---AADLSKYE 468
|
330 340 350
....*....|....*....|....*....|..
gi 115527082 1774 KKEQDTSAHLERMKKNLEQtvkdLQHRLDEAE 1805
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSK----LQRELAEAE 496
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1471-1918 |
1.12e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1471 LEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEe 1550
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1551 aeasleheegkilriQLELNQVKSEVDRKIAEKDEEIDQmkrnhirivesmqstLDAEIRSRNDAIRLKKKMEGDLNEME 1630
Cdd:COG4717 127 ---------------LLPLYQELEALEAELAELPERLEE---------------LEERLEELRELEEELEELEAELAELQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1631 IQLNHANRMAAEAlrnyrnTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQEL 1710
Cdd:COG4717 177 EELEELLEQLSLA------TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1711 LDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKK 1788
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1789 NLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGE---------VESEQK--RNVEAVKGLRKHERKVKELTYQ 1857
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaallaeagVEDEEElrAALEQAEEYQELKEELEELEEQ 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115527082 1858 TEEDRKNILRLQDLVDK--LQAKVKSYKRQAEEAEEQSNVNLSKFRRIQHELEEAEERADIAE 1918
Cdd:COG4717 411 LEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1537-1934 |
1.14e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.99 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1537 VEQEKSELQAALEEAEASLEHEEGKILRIQL-ELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQS---------TLD 1606
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEIERYEEQREQARETRDEADEVLEEheerreeleTLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1607 AEIRSRNDAIRLKKKMEGDLNEmEIQlnhANRMAAEALRNYRNtqAILKDTQLhlDDAlrSQEDLKEQLAMVERRANLLQ 1686
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAE-EVR---DLRERLEELEEERD--DLLAEAGL--DDA--DAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1687 AEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDA 1766
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1767 AMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLaLKGGK---------------------KQIQKLEARVRE 1825
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-LEAGKcpecgqpvegsphvetieedrERVEELEAELED 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1826 LEGEVESEQKRnVEAVKGLRKHERKVKELtyqtEEDRKNilrLQDLVDKLQAKVKSYKRQAEEAEEQSNvnlskfrRIQH 1905
Cdd:PRK02224 487 LEEEVEEVEER-LERAEDLVEAEDRIERL----EERRED---LEELIAERRETIEEKRERAEELRERAA-------ELEA 551
|
410 420
....*....|....*....|....*....
gi 115527082 1906 ELEEAEERADIAESQVNKLRVKSREVHTK 1934
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1201-1417 |
1.65e-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: 65.17 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1201 ADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLS----EIKTKEEEQQRLIND 1276
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAaleaELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1277 LTAQRARLQTESGEYSR--QLDEKDTLVS-----QLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLRE 1349
Cdd:COG4942 99 LEAQKEELAELLRALYRlgRQPPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115527082 1350 QYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCAS 1417
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1224-1806 |
1.70e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1224 EKSEMKMEIDDLASNMETVSKAKGNLEKMcRALEDQLSEIKTKEEEQQRLINDLTAQRARLQT-ESGEYSRQLDEKDTLV 1302
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDA-REQIELLEPIRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1303 SQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSrhdcdllreQYEEEQEAKAELQRAMSKANsEVAQWRTKYETD 1382
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGN---------GGDRLEQLEREIERLERELE-ERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1383 AIQ-------RTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLmiDVERtnaacAALDKKQRNFD- 1454
Cdd:COG4913 368 LAAlglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL--EAEI-----ASLERRKSNIPa 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1455 ---KILAEWKQKCEETHAELE--AsqkesrslstELFKIKNAYEESLDQLETLKR--------ENKNLQQeISDLTEQIA 1521
Cdd:COG4913 441 rllALRDALAEALGLDEAELPfvG----------ELIEVRPEEERWRGAIERVLGgfaltllvPPEHYAA-ALRWVNRLH 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1522 EGGkRIHeLEKIKKQVEQEkselqAALEEAEASLEHeegkilRIQLELNQVKSEVDRKIAEKD-----EEIDQMKRNHIR 1596
Cdd:COG4913 510 LRG-RLV-YERVRTGLPDP-----ERPRLDPDSLAG------KLDFKPHPFRAWLEAELGRRFdyvcvDSPEELRRHPRA 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1597 IVESMQSTLDAE---------IRSRN----DAIRLKKKMEGDLNEMEIQLNHANRmAAEALRNYRNTQAILKDTQLHLDD 1663
Cdd:COG4913 577 ITRAGQVKGNGTrhekddrrrIRSRYvlgfDNRAKLAALEAELAELEEELAEAEE-RLEALEAELDALQERREALQRLAE 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1664 ALRSQEDLKEQLAMVERranlLQAEIEELRAT---LEQTERSRKIAEQELLDASERVQLLHTQntslintKKKLETDISQ 1740
Cdd:COG4913 656 YSWDEIDVASAEREIAE----LEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGE-------IGRLEKELEQ 724
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115527082 1741 IQgemEDIIQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQ 1806
Cdd:COG4913 725 AE---EELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1008-1592 |
1.88e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 66.08 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1008 QQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAqestmdiENDKQQLDEKLKKk 1087
Cdd:PRK01156 172 KDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNA-------MDDYNNLKSALNE- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1088 efemsgLQSKIEDEQALGMQLqkkikelqarieeleeeieaerasrAKAEKQRSDLSRELEEISERLEEAGGATSAQIEM 1167
Cdd:PRK01156 244 ------LSSLEDMKNRYESEI-------------------------KTAESDLSMELEKNNYYKELEERHMKIINDPVYK 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1168 NKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKleKEKSEMKMEIDDLASNMETVSKAKG 1247
Cdd:PRK01156 293 NRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKK--SRYDDLNNQILELEGYEMDYNSYLK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1248 NLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLE--- 1324
Cdd:PRK01156 371 SIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmln 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1325 -EEIKAKSALAHALQSSRHdcdlLREQYEEE----QEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQ 1399
Cdd:PRK01156 451 gQSVCPVCGTTLGEEKSNH----IINHYNEKksrlEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIES 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1400 -------------RLQDAEEHVEAVNAKCASLEKTKQRLQNEvEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKCEE 1466
Cdd:PRK01156 527 aradledikikinELKDKHDKYEEIKNRYKSLKLEDLDSKRT-SWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1467 THAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQA 1546
Cdd:PRK01156 606 IEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKK 685
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 115527082 1547 ALEEAEASLEHEEGKILRIQLELNQVkSEVDRKIAEKDEEIDQMKR 1592
Cdd:PRK01156 686 SRKALDDAKANRARLESTIEILRTRI-NELSDRINDINETLESMKK 730
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1198-1775 |
4.13e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.92 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1198 KKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDdlasnmeTVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDL 1277
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYN-------NAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1278 TAQRARLQTESG---EYSRQLDEKDTLVSQLSRGKQAFTQQIEElKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEE 1354
Cdd:PRK01156 266 SMELEKNNYYKEleeRHMKIINDPVYKNRNYINDYFKYKNDIEN-KKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1355 QEAKAELqramskaNSEVAQWRTkYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMI 1434
Cdd:PRK01156 345 KSRYDDL-------NNQILELEG-YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINV 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1435 DVERTNAACAALDKKQRNfdkiLAEWKQKCEETHAELEASQKE---SRSLSTE-LFKIKNAYEESLDQLETLKREnknLQ 1510
Cdd:PRK01156 417 KLQDISSKVSSLNQRIRA----LRENLDELSRNMEMLNGQSVCpvcGTTLGEEkSNHIINHYNEKKSRLEEKIRE---IE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1511 QEISDLTEQIAEGGKRIHELEKikKQVEQEKSELQAaLEEAEASLEHEEGKILRIQlELNQVKSEVDRKIAEKDEEIDQM 1590
Cdd:PRK01156 490 IEVKDIDEKIVDLKKRKEYLES--EEINKSINEYNK-IESARADLEDIKIKINELK-DKHDKYEEIKNRYKSLKLEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1591 KRNHIRIVESMQSTLDAE-IRSRNDAIRLK-KKMEGDLNEMEIQLNHAN-------RMAAEALRNYRNTQAILKDTQLHL 1661
Cdd:PRK01156 566 KRTSWLNALAVISLIDIEtNRSRSNEIKKQlNDLESRLQEIEIGFPDDKsyidksiREIENEANNLNNKYNEIQENKILI 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1662 DDALRSQEDLKEQLAMVERRanllQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQI 1741
Cdd:PRK01156 646 EKLRGKIDNYKKQIAEIDSI----IPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDI 721
|
570 580 590
....*....|....*....|....*....|....
gi 115527082 1742 QGEMEDIiqearnaeEKAKKAITDAAMMAEELKK 1775
Cdd:PRK01156 722 NETLESM--------KKIKKAIGDLKRLREAFDK 747
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1483-1913 |
7.43e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 7.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1483 TELFKIKNAYEESLDQLETLKRENKNLQQEIS---DLTEQIAEGGKR-------IHELEKIKKQVEQEKSELQAALEEAE 1552
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKrteNIEELIKEKEKEleevlreINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1553 ------ASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQMKrnhirivesmqstldaEIRSRNDAIRLKKKMEGDL 1626
Cdd:PRK03918 235 elkeeiEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE----------------EKVKELKELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1627 NEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQA---EIEELRATLEQTERSR 1703
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEErheLYEEAKAKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1704 K-IAEQELLDASERVQLLHTQNTSLINTKKKLETDIsqiqGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKEqdtsaH 1782
Cdd:PRK03918 379 KrLTGLTPEKLEKELEELEKAKEEIEEEISKITARI----GELKKEIKELKKAIEELKKAKGKCPVCGRELTEE-----H 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1783 LERMKKNLEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVRELEGEVESEQK--RNVEAVKGLRKHERKVKELTYQT-E 1859
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIE--------EKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEElE 521
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 115527082 1860 EDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNvnlsKFRRIQHELEEAEER 1913
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEE 571
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1230-1703 |
8.51e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 8.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1230 MEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGK 1309
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1310 QAFT--QQIEELKRQLEEEIKAKSALAHALQSSRHdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRT 1387
Cdd:COG4717 126 QLLPlyQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1388 EELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQ--NEVEDLMIDVERTNAACAALDKKQRNFDKI--------- 1456
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLIltiagvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1457 ------LAEWKQKCEETHAELEASQKESRSLSTELfkiknAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHEL 1530
Cdd:COG4717 282 vlgllaLLFLLLAREKASLGKEAEELQALPALEEL-----EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1531 EKIKKQVEQEKSELQAALEEAEASLEHEEGkiLRIQLELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQ-STLDAEI 1609
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAEAGVEDEEE--LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeEELEEEL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1610 RSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRnyrntqailkdtqlhLDDALRSQEDLKEQLAMVERRANLLQAEI 1689
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEEDGE---------------LAELLQELEELKAELRELAEEWAALKLAL 499
|
490
....*....|....
gi 115527082 1690 EELRATLEQTERSR 1703
Cdd:COG4717 500 ELLEEAREEYREER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
867-1286 |
1.40e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 867 LAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEAD--SLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKK 944
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 945 RKLEDECSEL----KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLtkEKKALQEAHQQTLDDLQAeedk 1020
Cdd:COG4717 177 EELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL--ENELEAAALEERLKEARL---- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1021 VNTLTKAKIKLEQQVDDLEGSLEQEKKIRM-----------DLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEF 1089
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVLFlvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1090 emsglqsKIEDEQALGMQLQKKIKELQarieeleeeieaERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNK 1169
Cdd:COG4717 331 -------PPDLSPEELLELLDRIEELQ------------ELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1170 KREAEFQKMRRDLEEATLQ-HEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKakgn 1248
Cdd:COG4717 392 EQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE---- 467
|
410 420 430
....*....|....*....|....*....|....*...
gi 115527082 1249 lekmcralEDQLSEIKTKEEEQQRLINDLTAQRARLQT 1286
Cdd:COG4717 468 --------DGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
869-1520 |
1.83e-09 |
|
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: 62.73 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 869 KTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLE 948
Cdd:TIGR04523 121 KLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 949 DECSELKKDIDdleltlakvekekhatenKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAK 1028
Cdd:TIGR04523 201 LLLSNLKKKIQ------------------KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1029 IKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKlaqestmDIENDKQQ-----LDEKLKKKEFEMSGLQSKIEDEQA 1103
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS-------DLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISQNNK 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1104 LGMQLQKKIKELqarieeleeeieaerasrakaEKQRSDLSRELEEISERLEEaggaTSAQIEMNKKreaEFQKMRRDLE 1183
Cdd:TIGR04523 336 IISQLNEQISQL---------------------KKELTNSESENSEKQRELEE----KQNEIEKLKK---ENQSYKQEIK 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1184 EATLQHEATAATLRKKHADSvAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEI 1263
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLN-QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1264 KTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELK---RQLEEEIKAKSALAHALQS- 1339
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKekiEKLESEKKEKESKISDLEDe 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1340 -----SRHDCDLLREQYEEEQEAKAEL---QRAMSKANSEVAQWRTKYET---DAIQRTEELEEAKKKLAQRLQDAEEHV 1408
Cdd:TIGR04523 547 lnkddFELKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQELIDQKEKekkDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1409 EAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKE---SRSLSTEL 1485
Cdd:TIGR04523 627 EKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKyitRMIRIKDL 706
|
650 660 670
....*....|....*....|....*....|....*
gi 115527082 1486 FKIKNAYEESLDQLETLKRENKNLQQEISDLTEQI 1520
Cdd:TIGR04523 707 PKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKF 741
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1095-1341 |
2.26e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1095 QSKIEDEQALGMQLQKKIKELQARieeleeeieaerasRAKAEKQRSDLSRELEEISERLEeaggATSAQIemnKKREAE 1174
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKE--------------LAALKKEEKALLKQLAALERRIA----ALARRI---RALEQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1175 FQKMRRDLEEATLQHEAtaatLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCR 1254
Cdd:COG4942 78 LAALEAELAELEKEIAE----LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1255 ALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALA 1334
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*..
gi 115527082 1335 HALQSSR 1341
Cdd:COG4942 234 AEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
918-1118 |
2.42e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 918 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 997
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 998 KEKK----ALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDI 1073
Cdd:COG4942 104 EELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 115527082 1074 ENDKQQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQAR 1118
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1664-1893 |
2.62e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1664 ALRSQEDLKEQLamvERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQG 1743
Cdd:COG4942 14 AAAAQADAAAEA---EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1744 EMEDIIQEARNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNLEQTVKDLQHRLDE--AEQLALKGGKKQIQ 1817
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115527082 1818 KLEARVRELEGEVESEQKRNVEAVKglrKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQS 1893
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
922-1458 |
4.39e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.84 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 922 KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT---K 998
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSsleD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 999 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDD--------------LEGSLEQEKKIRMDLERAKRKLEGDLK 1064
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDpvyknrnyindyfkYKNDIENKKQILSNIDAEINKYHAIIK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1065 LAQestmDIENDKQQLDEKLKKKE---FEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRS 1141
Cdd:PRK01156 330 KLS----VLQKDYNDYIKKKSRYDdlnNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1142 DLSRELEEISERLEE-AGGATSAQIEMNKKREAEfQKMRRDLEE----------ATLQHEATAATLRKKHADSVAELGEQ 1210
Cdd:PRK01156 406 AIKKELNEINVKLQDiSSKVSSLNQRIRALRENL-DELSRNMEMlngqsvcpvcGTTLGEEKSNHIINHYNEKKSRLEEK 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1211 IDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRA----LEDQLSEIKTKEEEQQRLINDLTAQRAR-LQ 1285
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARAdledIKIKINELKDKHDKYEEIKNRYKSLKLEdLD 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1286 TESGEYSRQLDEKDTL-VSQLSRGKQAFTQQIEELKRQLEEEI----KAKSALAHALQSSRHDCDLLREQYEEEQEAKae 1360
Cdd:PRK01156 565 SKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRLQEIEigfpDDKSYIDKSIREIENEANNLNNKYNEIQENK-- 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1361 lqRAMSKANSEVAQWRTKyetdaIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTN 1440
Cdd:PRK01156 643 --ILIEKLRGKIDNYKKQ-----IAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELS 715
|
570
....*....|....*...
gi 115527082 1441 AACAALDKKQRNFDKILA 1458
Cdd:PRK01156 716 DRINDINETLESMKKIKK 733
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
867-1355 |
6.11e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 867 LAKTEAKRKELEEKMVTLMQEKNDLQlQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEInAELTAKKRK 946
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAEL-AELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 947 LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMagldetiakltkekkalQEAHQQTLDDLQAEEDKVNTLTK 1026
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT-----------------EEELQDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1027 AKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIendKQQLDEKLKKKEFEMSGLQSKIEDEQALGM 1106
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLA---LLGLGGSLLSLILTIAGVLFLVLGLLALLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1107 Q-LQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEA 1185
Cdd:COG4717 291 LlLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1186 TLQheataATLRKKHADSVAELGEQIDNLQRvKQKLEKEKSEMKMEIDDLASNMETVSkAKGNLEkmcrALEDQLSEIKT 1265
Cdd:COG4717 371 EIA-----ALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELL-EALDEE----ELEEELEELEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1266 KEEEQQRLINDLTAQRARLQTEsgeySRQLDEKDTLVSQLsrgkqaftQQIEELKRQLEEEIKAKSALAHALQSSRHdcd 1345
Cdd:COG4717 440 ELEELEEELEELREELAELEAE----LEQLEEDGELAELL--------QELEELKAELRELAEEWAALKLALELLEE--- 504
|
490
....*....|
gi 115527082 1346 lLREQYEEEQ 1355
Cdd:COG4717 505 -AREEYREER 513
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1389-1831 |
7.38e-09 |
|
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: 60.47 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1389 ELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAE--------- 1459
Cdd:pfam05622 4 EAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEEnfrletard 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1460 -WKQKCEETHA----------ELEASQKESRSLSTELFKIKNA-------------YEESLDQLETLKRENKNLQQEISD 1515
Cdd:pfam05622 84 dYRIKCEELEKevlelqhrneELTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1516 LTEQIAEGGKRIHELEKIKKQVEQEKSELQaaleEAEASLEHEEGKILRIQLELNQ-------VKSEVDRKIAEKD---E 1585
Cdd:pfam05622 164 YMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKleekleaLQKEKERLIIERDtlrE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1586 EIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQaiLKDTQLHLDDAL 1665
Cdd:pfam05622 240 TNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRER--LTELQQLLEDAN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1666 RSQEDLKEQLAMVERRANLLQAEIEELRATLeqtersrkiaeqelldaservQLLHTQNTSLINTKKKLETDISQIQGEM 1745
Cdd:pfam05622 318 RRKNELETQNRLANQRILELQQQVEELQKAL---------------------QEQGSKAEDSSLLKQKLEEHLEKLHEAQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1746 EDIIQEARNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNLEQ---TVKDLQHRLDEAEQLALKGGKKQIQ 1817
Cdd:pfam05622 377 SELQKKKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPASPPEIQALKNQLL 456
|
490
....*....|....
gi 115527082 1818 KLEARVRELEGEVE 1831
Cdd:pfam05622 457 EKDKKIEHLERDFE 470
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1166-1939 |
8.45e-09 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 61.22 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1166 EMNKKREAEFQKMRrDLEEATLQ-HEATAATLRKKHADSVAEL-----GEQIDNLQRVKQKLEKEKSEMKMEIDDLASNM 1239
Cdd:TIGR01612 700 DLKSKIDKEYDKIQ-NMETATVElHLSNIENKKNELLDIIVEIkkhihGEINKDLNKILEDFKNKEKELSNKINDYAKEK 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1240 ETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINdltaqrarlqtESGEYSRQLDEKDTLVSQLsrgkqaftqqIEEL 1319
Cdd:TIGR01612 779 DELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYD-----------KSKEYIKTISIKEDEIFKI----------INEM 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1320 KrQLEEEIKAKSALAHALQSSRhdcdllREQYEEEQEAKAELqraMSKANSEVAQWR-TKYETDAIQRTEELEEAKKKLA 1398
Cdd:TIGR01612 838 K-FMKDDFLNKVDKFINFENNC------KEKIDSEHEQFAEL---TNKIKAEISDDKlNDYEKKFNDSKSLINEINKSIE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1399 QRLQD------AEEHVEAVNAKCASLEK--TKQRLQNEVEDLMIDV-ERTNaacaALDKKQRN-FDKILAEWKQKCEETH 1468
Cdd:TIGR01612 908 EEYQNintlkkVDEYIKICENTKESIEKfhNKQNILKEILNKNIDTiKESN----LIEKSYKDkFDNTLIDKINELDKAF 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1469 AELEASQKESRslSTELFKIKNAYEESL---------DQLETLKRENKNLQQEISDLTEQIAEGGKRIH--------ELE 1531
Cdd:TIGR01612 984 KDASLNDYEAK--NNELIKYFNDLKANLgknkenmlyHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHtsiyniidEIE 1061
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1532 K-IKKQVEQEKSELqaaLEEAEASLEHEEGkiLRIQLELNQVKSEVDRKIAEKDEEIDQMKRNhiriVESMQSTLDAEIr 1610
Cdd:TIGR01612 1062 KeIGKNIELLNKEI---LEEAEINITNFNE--IKEKLKHYNFDDFGKEENIKYADEINKIKDD----IKNLDQKIDHHI- 1131
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1611 srNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNyrntqailkdtqlhlDDALRSQEDLKEQLAMVERRANLLQaEIE 1690
Cdd:TIGR01612 1132 --KALEEIKKKSENYIDEIKAQINDLEDVADKAISN---------------DDPEEIEKKIENIVTKIDKKKNIYD-EIK 1193
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1691 ELRATLEQTERsrkiaEQELLDASERVQLLHTQNTSLI------NTKKKLETDISQIQGEMEDI--IQEARNAEEKAKKA 1762
Cdd:TIGR01612 1194 KLLNEIAEIEK-----DKTSLEEVKGINLSYGKNLGKLflekidEEKKKSEHMIKAMEAYIEDLdeIKEKSPEIENEMGI 1268
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1763 ITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRldeaeQLALKGGKKQIQKLEARVRELEGEVESEQKRNVEavk 1842
Cdd:TIGR01612 1269 EMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREK-----SLKIIEDFSEESDINDIKKELQKNLLDAQKHNSD--- 1340
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1843 gLRKHERKVKELTyqteedrkNILRLQDlVDKLQAKVKSYKRQAEEAEEQSNVNLSK----FRRIQHELEEAEERADIAE 1918
Cdd:TIGR01612 1341 -INLYLNEIANIY--------NILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKseklIKKIKDDINLEECKSKIES 1410
|
810 820
....*....|....*....|....*
gi 115527082 1919 S----QVNKLRVKSREVHTKIISEE 1939
Cdd:TIGR01612 1411 TlddkDIDECIKKIKELKNHILSEE 1435
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
894-1213 |
8.45e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 894 QVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAE--------DEEEINAeltakkRKLEDECSELKKDIDDLELT- 964
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREalqrlaeySWDEIDV------ASAEREIAELEAELERLDASs 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 965 --LAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKikLEQQVDDLEGSl 1042
Cdd:COG4913 685 ddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALGD- 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1043 EQEKKIRMDLERAKRKLEGDLKLAQEstmDIENdkqQLDEKLKKKEFEMSGLQSKIED------------EQALgMQLQK 1110
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEE---ELER---AMRAFNREWPAETADLDADLESlpeylalldrleEDGL-PEYEE 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1111 KIKELqarieeleeeieaerasRAKAEKQ-----RSDLSRELEEISERLEEA---------GGATSAQIEMNKKREAEFQ 1176
Cdd:COG4913 835 RFKEL-----------------LNENSIEfvadlLSKLRRAIREIKERIDPLndslkripfGPGRYLRLEARPRPDPEVR 897
|
330 340 350
....*....|....*....|....*....|....*..
gi 115527082 1177 KMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDN 1213
Cdd:COG4913 898 EFRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
946-1537 |
9.49e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 60.69 E-value: 9.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 946 KLEDECSELKKDIDDLELTLAK---VEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDD---LQAEED 1019
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNidyLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDynnLKSALN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1020 KVNTLTKAKIKLEQQVDDLEGSL----EQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKkefeMSGLQ 1095
Cdd:PRK01156 243 ELSSLEDMKNRYESEIKTAESDLsmelEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQI----LSNID 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1096 SKIEDEQALgmqlQKKIKELQARIEELEeeieaerasraKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEF 1175
Cdd:PRK01156 319 AEINKYHAI----IKKLSVLQKDYNDYI-----------KKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYS 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1176 QKMRR---DLEEATLQHEATAATLRKKHAdsvaELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKakgnlEKM 1252
Cdd:PRK01156 384 KNIERmsaFISEILKIQEIDPDAIKKELN----EINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNG-----QSV 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1253 CRALEDQLSEiktkeEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQqiEELKRQLEEEIKAKSA 1332
Cdd:PRK01156 455 CPVCGTTLGE-----EKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKSINEYNKIESA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1333 lAHALQSSRHDCDLLREQYEEEQEAKAE--------LQRAMSKANSEVAQwRTKYETDAIQ-RTEELEEAKKKLAQRLQD 1403
Cdd:PRK01156 528 -RADLEDIKIKINELKDKHDKYEEIKNRykslkledLDSKRTSWLNALAV-ISLIDIETNRsRSNEIKKQLNDLESRLQE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1404 AEEHVEAVNAkcaSLEKTKQRLQNEVEDL---MIDVERTNAACAALDKKQRNFDKILAEwKQKCEETHAELEASQKESrs 1480
Cdd:PRK01156 606 IEIGFPDDKS---YIDKSIREIENEANNLnnkYNEIQENKILIEKLRGKIDNYKKQIAE-IDSIIPDLKEITSRINDI-- 679
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 115527082 1481 lSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQV 1537
Cdd:PRK01156 680 -EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1462-1682 |
1.05e-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: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1462 QKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEK 1541
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1542 SELQAALEEAEASLeHEEGKILRIQLELNQVKSEvdrKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKK 1621
Cdd:COG4942 100 EAQKEELAELLRAL-YRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115527082 1622 MEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRA 1682
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
871-1550 |
1.08e-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: 60.62 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 871 EAKRKELEEKMVTLMQEKNDLQLQVQAE-ADSLADAEERCDQLIKTKIQLEAKIKEVTERAEdeEEINAELTAKKRKLED 949
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALE--SELREQLEAGKLEFNE 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 950 ECSELKKDIDDLELTLAKVEKEKHATENKvKNLTEEMAGLDETIAKLTKEKKALQE-------AHQQTLDDLQAEEDKVN 1022
Cdd:pfam12128 438 EEYRLKSRLGELKLRLNQATATPELLLQL-ENFDERIERAREEQEAANAEVERLQSelrqarkRRDQASEALRQASRRLE 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1023 TLTKAKIKLEQQVDDLEGSL-EQEKKIRMDLERAKRKLeGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDE 1101
Cdd:pfam12128 517 ERQSALDELELQLFPQAGTLlHFLRKEAPDWEQSIGKV-ISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEW 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1102 QALGMQLQKKIKELQARIEELEEeieaeraSRAKAEKQRSDLSRELEEISERLEEAGGAtsaqiemnkkreaeFQKMRRD 1181
Cdd:pfam12128 596 AASEEELRERLDKAEEALQSARE-------KQAAAEEQLVQANGELEKASREETFARTA--------------LKNARLD 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1182 LEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKgnLEKMCRALEDQLS 1261
Cdd:pfam12128 655 LRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAY--WQVVEGALDAQLA 732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1262 EIKTKEEEQQrlindlTAQRARLQTESGEYSRQLDEKDT---LVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQ 1338
Cdd:pfam12128 733 LLKAAIAARR------SGAKAELKALETWYKRDLASLGVdpdVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWL 806
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1339 SSRhdcDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYET------DAIQRTEELEEAKKKLAQRLQDAEEHVEAVN 1412
Cdd:pfam12128 807 QRR---PRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMerkaseKQQVRLSENLRGLRCEMSKLATLKEDANSEQ 883
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1413 AKCASLEKTKQrlqneVEDLMIDVERtnaACAALDKKQRNFDKILAewKQKCEETHAELEASQKESRSLSTELFKIKNaY 1492
Cdd:pfam12128 884 AQGSIGERLAQ-----LEDLKLKRDY---LSESVKKYVEHFKNVIA--DHSGSGLAETWESLREEDHYQNDKGIRLLD-Y 952
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115527082 1493 EESLDQLETLKreNKNLQQEISDLTEQIAEGGKRIHE----LEKIKKQVEQEKSELQAALEE 1550
Cdd:pfam12128 953 RKLVPYLEQWF--DVRVPQSIMVLREQVSILGVDLTEfydvLADFDRRIASFSRELQREVGE 1012
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1490-1933 |
1.09e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 60.22 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1490 NAYEESLDQL-ETL--KRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALE-EAEASLEHEEGKILRI 1565
Cdd:pfam10174 154 GARDESIKKLlEMLqsKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHrRNQLQPDPAKTKALQT 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1566 QLELNQVK-SEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKME---GDLNEMEIQLnHANRMAA 1641
Cdd:pfam10174 234 VIEMKDTKiSSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDqlkQELSKKESEL-LALQTKL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1642 EALRNYRNtqailkDTQLHLddalrsqEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLH 1721
Cdd:pfam10174 313 ETLTNQNS------DCKQHI-------EVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1722 TQNTSLINTKKKLETDISQIQGEMEDIIQEARNAE-------EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNL-EQT 1793
Cdd:pfam10174 380 GEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDkqlaglkERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQR 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1794 VKDLQHRLDEAEQL--ALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERKVKELTYQTEEDRKNILRLQDL 1871
Cdd:pfam10174 460 EREDRERLEELESLkkENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQ 539
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115527082 1872 VDKLQakvksykrQAEEAEEQSNVNLSKFRRIQHELEEAEERADIAESQVNKLRVKSREVHT 1933
Cdd:pfam10174 540 LKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVEN 593
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
848-1116 |
1.27e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 848 ETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVT 927
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 928 ERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEah 1007
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE-- 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1008 qqtlddlqaeedKVNTLTKAKIKLEQQVDDLEGSLEQEK--KIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLK 1085
Cdd:TIGR04523 525 ------------KIEKLESEKKEKESKISDLEDELNKDDfeLKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
250 260 270
....*....|....*....|....*....|.
gi 115527082 1086 KKEFEMSGLQSKIEDEQALGMQLQKKIKELQ 1116
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
833-1878 |
1.45e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 60.45 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 833 WMKLYFKIKPLL-----KSAETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLmQEKNDLQLQVQAEADSLADAEE 907
Cdd:TIGR01612 556 WKKLIHEIKKELeeeneDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNI-SDKNEYIKKAIDLKKIIENNNA 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 908 RCDQLIKTKIQleakikEVTERAEDEEEINAELTAKKRKLEDEcselkkDIDDLELTLAKVEKekhatENKVKNlTEEMA 987
Cdd:TIGR01612 635 YIDELAKISPY------QVPEHLKNKDKIYSTIKSELSKIYED------DIDALYNELSSIVK-----ENAIDN-TEDKA 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 988 GLDETIAKLTKEKKALQEAHQQTLddlqaeEDKVNTLTKAKIKLEQQVddlegsLEQEKKIRMDLERAKRKLEGDLKLAQ 1067
Cdd:TIGR01612 697 KLDDLKSKIDKEYDKIQNMETATV------ELHLSNIENKKNELLDII------VEIKKHIHGEINKDLNKILEDFKNKE 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1068 ESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQALgmqlqKKIKElqarieeleeeieaerasraKAEKQRSDLSRE- 1146
Cdd:TIGR01612 765 KELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINI-----DNIKD--------------------EDAKQNYDKSKEy 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1147 LEEISERLEEaggaTSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQI--DNLQRVKQKLEKE 1224
Cdd:TIGR01612 820 IKTISIKEDE----IFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEIsdDKLNDYEKKFNDS 895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1225 KS---EMKMEIDDLASNMETVSKAKGNLeKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDekDTL 1301
Cdd:TIGR01612 896 KSlinEINKSIEEEYQNINTLKKVDEYI-KICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFD--NTL 972
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1302 VSQLSRGKQAFTQ-QIEELKRQLEEEIKAKSALAHALQSSRHdcDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYE 1380
Cdd:TIGR01612 973 IDKINELDKAFKDaSLNDYEAKNNELIKYFNDLKANLGKNKE--NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIH 1050
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1381 TDAIQRTEELEEAKKKLAQRLQdaEEHVEAVNAKCASLEKTKQRLQ----------------NEVEDLMIDVErtnaaca 1444
Cdd:TIGR01612 1051 TSIYNIIDEIEKEIGKNIELLN--KEILEEAEINITNFNEIKEKLKhynfddfgkeenikyaDEINKIKDDIK------- 1121
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1445 ALDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKN--AYEESLDQLETLKRENKNLQQEISDLTEQIAE 1522
Cdd:TIGR01612 1122 NLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDpeEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAE 1201
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1523 GGKRIHELEKIK---------------KQVEQEKSELQAALEEAEASLEheegkilriqlELNQVKSEVDRKIAEKDEEI 1587
Cdd:TIGR01612 1202 IEKDKTSLEEVKginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIE-----------DLDEIKEKSPEIENEMGIEM 1270
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1588 DQMKRNHIRIVeSMQSTLDAEIRSRNDairlkKKMEGDLNEMEIQLNHANRMAAealrnyrNTQAILKDTQLHLDDALRS 1667
Cdd:TIGR01612 1271 DIKAEMETFNI-SHDDDKDHHIISKKH-----DENISDIREKSLKIIEDFSEES-------DINDIKKELQKNLLDAQKH 1337
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1668 QEDLKEQLAMVERRANLLQAE-----IEELRATLEQTERSRKIAEQElLDASERVQLLHTQNTSLINTKKKLETDI---- 1738
Cdd:TIGR01612 1338 NSDINLYLNEIANIYNILKLNkikkiIDEVKEYTKEIEENNKNIKDE-LDKSEKLIKKIKDDINLEECKSKIESTLddkd 1416
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1739 ------------SQIQGEMEDIIQEARNAEE-------------------------KAKKAITDAAMMAEELKKEQDTS- 1780
Cdd:TIGR01612 1417 idecikkikelkNHILSEESNIDTYFKNADEnnenvlllfkniemadnksqhilkiKKDNATNDHDFNINELKEHIDKSk 1496
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1781 ----------AHLERMKKNLEQTVKDLQHRLDEAEQLALKGG----KKQIQKLEARVRELEGEVESEQKRNVEAVKGLRK 1846
Cdd:TIGR01612 1497 gckdeadknaKAIEKNKELFEQYKKDVTELLNKYSALAIKNKfaktKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKK 1576
|
1130 1140 1150
....*....|....*....|....*....|..
gi 115527082 1847 HERKVKELTYQTEEDRKNILRLQDLVDKLQAK 1878
Cdd:TIGR01612 1577 EKFRIEDDAAKNDKSNKAAIDIQLSLENFENK 1608
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
918-1246 |
1.77e-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: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 918 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 997
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 998 KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDK 1077
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1078 QQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR------------ 1145
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrtqael 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1146 -----ELEEISERLEEA------GGATSAQ--------IEMNKKR----EAEFQKMRRDLEEATLQHEATAATL------ 1196
Cdd:pfam07888 275 hqarlQAAQLTLQLADAslalreGRARWAQeretlqqsAEADKDRieklSAELQRLEERLQEERMEREKLEVELgrekdc 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 115527082 1197 -RKKHADSVAELGEQIDNL---QRVKQKLEKEKSEMKMEIDDLASNMETVSKAK 1246
Cdd:pfam07888 355 nRVQLSESRRELQELKASLrvaQKEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1668-1904 |
1.87e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.65 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1668 QEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKI--AEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEM 1745
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1746 eDIIQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNLEQTVKDLQHRLDEAEQLALKGGKKQ 1815
Cdd:COG3206 243 -AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1816 IQKLEARVRELEGEVESEQKRnveaVKGLRKHERKvkeltyqteedrknILRLQDLVDKLQAKVKSYKRQAEEAEEQSNV 1895
Cdd:COG3206 322 LEALQAREASLQAQLAQLEAR----LAELPELEAE--------------LRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
....*....
gi 115527082 1896 NLSKFRRIQ 1904
Cdd:COG3206 384 TVGNVRVID 392
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1315-1701 |
1.93e-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: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1315 QIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEqeaKAELQRAMSKANSEVAQWRtkyetdaiQRTEELEEAK 1394
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQ---RRELESRVAELKEELRQSR--------EKHEELEEKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1395 KKLAQRlqdAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKCEE---THAEL 1471
Cdd:pfam07888 104 KELSAS---SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAErkqLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1472 EASQKESRSLSTELFKIKNAYEESLDQLETlkrenknLQQEISDLTEQIAEGGKRIHELEKIKKqveqeksELQAALEEA 1551
Cdd:pfam07888 181 QQTEEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLE-------ELRSLQERL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1552 EASLEHEEGkilrIQLELNQVKSEVDRKIAEKdeeidqmkrnHIRIVESMQSTL---DAEIRSRNDAIRLKKKMEGDLNE 1628
Cdd:pfam07888 247 NASERKVEG----LGEELSSMAAQRDRTQAEL----------HQARLQAAQLTLqlaDASLALREGRARWAQERETLQQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1629 MEIQLNHANRMAAEALRNYRNTQ-------------AILKDTQL-HLDDALRSQEDLKEQLAMVERRANLLQAEIEELRA 1694
Cdd:pfam07888 313 AEADKDRIEKLSAELQRLEERLQeermereklevelGREKDCNRvQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
....*..
gi 115527082 1695 TLEQTER 1701
Cdd:pfam07888 393 YIRQLEQ 399
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
904-1554 |
2.45e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 904 DAEERCDQLIKTKIQLEAkIKEVTERAEDEEEINAELTAKKRKLEdecsELKKDIDDLELTLAKVEKEKHATenKVKNLT 983
Cdd:COG4913 222 DTFEAADALVEHFDDLER-AHEALEDAREQIELLEPIRELAERYA----AARERLAELEYLRAALRLWFAQR--RLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 984 EEMAGLDETIAKLTKEKKALQ---EAHQQTLDDLQAEEDKVNTltKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLE 1060
Cdd:COG4913 295 AELEELRAELARLEAELERLEarlDALREELDELEAQIRGNGG--DRLEQLEREIERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1061 gdlklaqestMDIENDKQQLDEKLKKkefemsgLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQR 1140
Cdd:COG4913 373 ----------LPLPASAEEFAALRAE-------AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1141 SDLSRELEEISERLEEAGGATSAQ-------IEMnKKREAEFqkmrRDLEEATLQHEATAATLRKKHADSVAELGEQIDN 1213
Cdd:COG4913 436 SNIPARLLALRDALAEALGLDEAElpfvgelIEV-RPEEERW----RGAIERVLGGFALTLLVPPEHYAAALRWVNRLHL 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1214 LQRVK-QKLEKEKSEMKMEiddlasnmetvskakgnlekmcRALEDQLSE-IKTKEEEQQRLINDLTAQRARL------- 1284
Cdd:COG4913 511 RGRLVyERVRTGLPDPERP----------------------RLDPDSLAGkLDFKPHPFRAWLEAELGRRFDYvcvdspe 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1285 -------------QTESGEYSRQLDEKDTLVSQLSRGKQAfTQQIEELKRQ---LEEEIKAKSALAHALQSSRHDCDLLR 1348
Cdd:COG4913 569 elrrhpraitragQVKGNGTRHEKDDRRRIRSRYVLGFDN-RAKLAALEAElaeLEEELAEAEERLEALEAELDALQERR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1349 EQYEEEQEAKAELQRAMSkANSEVAQWRTKYE--TDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQ 1426
Cdd:COG4913 648 EALQRLAEYSWDEIDVAS-AEREIAELEAELErlDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1427 NEVEDLMIDVERTNAACAALDkkQRNFDKILAEwkQKCEETHAELEASQKESRSLSTElfKIKNAYEESLDQLETLKREN 1506
Cdd:COG4913 727 EELDELQDRLEAAEDLARLEL--RALLEERFAA--ALGDAVERELRENLEERIDALRA--RLNRAEEELERAMRAFNREW 800
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115527082 1507 KNlqqEISDLTEQIAEGGK-----------RIHELEK-----IKKQVEQEKSELQAALEEAEAS 1554
Cdd:COG4913 801 PA---ETADLDADLESLPEylalldrleedGLPEYEErfkelLNENSIEFVADLLSKLRRAIRE 861
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
902-1330 |
2.98e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.96 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 902 LADAEERCDQLI-KTKIQLEakikEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVK 980
Cdd:pfam05483 263 LEESRDKANQLEeKTKLQDE----NLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQME 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 981 NLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTkakIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLE 1060
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIIT---MELQKKSSELEEMTKFKNNKEVELEELKKILA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1061 GDLKLAQESTM------DIENDKQQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRA 1134
Cdd:pfam05483 416 EDEKLLDEKKQfekiaeELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCD 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1135 KAEKQRSDLSRELEEISERLEEaggaTSAQIEMNKKREAEFQKMRRDLEEATLQheataatLRkkhadsvaelgeqiDNL 1214
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELKK----HQEDIINCKKQEERMLKQIENLEEKEMN-------LR--------------DEL 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1215 QRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQ 1294
Cdd:pfam05483 551 ESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQ 630
|
410 420 430
....*....|....*....|....*....|....*.
gi 115527082 1295 LDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAK 1330
Cdd:pfam05483 631 LNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
867-1717 |
3.30e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 867 LAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKiQLEAKIKEVTERAEDEEEINAELTAKKRK 946
Cdd:PRK04863 302 LAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIE-RYQADLEELEERLEEQNEVVEEADEQQEE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 947 LEDECSELKKDIDDLELTLAKV-----EKEKHATE-NKVKNLTEEMAGLDEtIAKLTKEKkaLQEAHQQtlddLQAEEDk 1020
Cdd:PRK04863 381 NEARAEAAEEEVDELKSQLADYqqaldVQQTRAIQyQQAVQALERAKQLCG-LPDLTADN--AEDWLEE----FQAKEQ- 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1021 vnTLTKAKIKLEQQVDDLEGSLEQEKK----IR-----MDLERAKRKlegdlklAQESTMDIENDKQQlDEKLKKKEFEM 1091
Cdd:PRK04863 453 --EATEELLSLEQKLSVAQAAHSQFEQayqlVRkiageVSRSEAWDV-------ARELLRRLREQRHL-AEQLQQLRMRL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1092 SGLQSKIEDEQalgmQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEaggaTSAQIEMNKKR 1171
Cdd:PRK04863 523 SELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMA----LRQQLEQLQAR 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1172 EAEFQKmrrdLEEATLQHEATAATLRKKHADSVA---ELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGN 1248
Cdd:PRK04863 595 IQRLAA----RAPAWLAAQDALARLREQSGEEFEdsqDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGS 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1249 LEKMCRALEDQ-----LSEIK---TKEE-----------EQQRLINDLTAQRARLQTE------------------SGEY 1291
Cdd:PRK04863 671 EDPRLNALAERfggvlLSEIYddvSLEDapyfsalygpaRHAIVVPDLSDAAEQLAGLedcpedlyliegdpdsfdDSVF 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1292 SRQLDEKDTLV------SQLSR-------GKQAFTQQIEELKRQLEEEIKAKSALA---HALQSSRHDCDLL-------- 1347
Cdd:PRK04863 751 SVEELEKAVVVkiadrqWRYSRfpevplfGRAAREKRIEQLRAEREELAERYATLSfdvQKLQRLHQAFSRFigshlava 830
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1348 -----REQYEEEQEAKAELQRAMSKANSEVAQWRTKYET-----DAIQR-------------TEELEEAKKKLAqRLQDA 1404
Cdd:PRK04863 831 feadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQakeglSALNRllprlnlladetlADRVEEIREQLD-EAEEA 909
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1405 EEHVEAVNAKCASLEKTKQ----------RLQNEVEDLMIDVERTNAACAAL-DKKQR-------NFDKILAEWKQKCEE 1466
Cdd:PRK04863 910 KRFVQQHGNALAQLEPIVSvlqsdpeqfeQLKQDYQQAQQTQRDAKQQAFALtEVVQRrahfsyeDAAEMLAKNSDLNEK 989
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1467 THAELEASQKESRSLSTELFKIKNAYEE------SLDQLETLKREN-KNLQQEISDLTEQIAEGgkrihelekIKKQVEQ 1539
Cdd:PRK04863 990 LRQRLEQAEQERTRAREQLRQAQAQLAQynqvlaSLKSSYDAKRQMlQELKQELQDLGVPADSG---------AEERARA 1060
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1540 EKSELQAALEEAEASLEHEEGKILRIQLELNqvksEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAeIRSRNDAIRLK 1619
Cdd:PRK04863 1061 RRDELHARLSANRSRRNQLEKQLTFCEAEMD----NLTKKLRKLERDYHEMREQVVNAKAGWCAVLRL-VKDNGVERRLH 1135
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1620 KKMEGDLNEMEiqLNHANRMAAEALRnyrntQAILKDTqlHLDDALRSQEDLK--EQL--------AMVERRAN------ 1683
Cdd:PRK04863 1136 RRELAYLSADE--LRSMSDKALGALR-----LAVADNE--HLRDVLRLSEDPKrpERKvqfyiavyQHLRERIRqdiirt 1206
|
970 980 990 1000
....*....|....*....|....*....|....*....|
gi 115527082 1684 ------LLQAEIEELRATLEQTERsrkiaEQELLDASERV 1717
Cdd:PRK04863 1207 ddpveaIEQMEIELSRLTEELTSR-----EQKLAISSESV 1241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1005-1453 |
3.39e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1005 EAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEgdlklaqestmdIENDKQQLDEKL 1084
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP------------LYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1085 KKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAeraSRAKAEKQRSDLSRELEEISERLEEAGGATSAQ 1164
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ---LSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1165 IEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEkseMKMEIDDLASNMETVSK 1244
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV---LFLVLGLLALLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1245 AKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRG-KQAFTQQIEELKRQL 1323
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELeEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1324 EEEIKAKS--ALAHALQssrhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAI-QRTEELEEAKKKLAQR 1400
Cdd:COG4717 376 LAEAGVEDeeELRAALE--------QAEEYQELKEELEELEEQLEELLGELEELLEALDEEELeEELEELEEELEELEEE 447
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115527082 1401 LQDAEEHVEAVNAKCASLEKT---------KQRLQNEVEDLMIDVERTNAACAALDKKQRNF 1453
Cdd:COG4717 448 LEELREELAELEAELEQLEEDgelaellqeLEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1534-1772 |
4.53e-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: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1534 KKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVksevDRKIAEKDEEIDQMkrnhirivESMQSTLDAEIRsrn 1613
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRAL--------EQELAALEAELA--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1614 daiRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELR 1693
Cdd:COG4942 87 ---ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115527082 1694 ATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEE 1772
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
973-1203 |
4.61e-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: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 973 HATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSL----EQEKKI 1048
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1049 RMDLERAKRKLEGDLKLAQEStmdieNDKQQLDEKLKKKEFE-----MSGLQSKIEDEQALGMQLQKKIKELQARIEELE 1123
Cdd:COG4942 96 RAELEAQKEELAELLRALYRL-----GRQPPLALLLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1124 EEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADS 1203
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARL----EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1189-1590 |
4.67e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.43 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1189 HEATAATLRKKHADSVAELGEQIDNLQRVKQKLE---KEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDqLSEIKT 1265
Cdd:PRK04863 284 HLEEALELRRELYTSRRQLAAEQYRLVEMARELAelnEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQAD-LEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1266 KEEEQQRLINDLTAQRARLQTESGEYSrqlDEKDTLVSQLSRGKQAF-TQQIEELKRQleeeiKAKSALahalqssrhdc 1344
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENEARAEAAE---EEVDELKSQLADYQQALdVQQTRAIQYQ-----QAVQAL----------- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1345 dllreqyeeeQEAKAELQrAMSKANSEVAQWRTKYETDAIQRTEELEEakkkLAQRLQDAEEHVEAVnAKCASLektkqr 1424
Cdd:PRK04863 424 ----------ERAKQLCG-LPDLTADNAEDWLEEFQAKEQEATEELLS----LEQKLSVAQAAHSQF-EQAYQL------ 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1425 lqneVEDLMIDVERTNAACAALDK-KQRNFDKILAEWKQKCEETHAELE---ASQKESRSLSTELFKIKNAYEESLDQLE 1500
Cdd:PRK04863 482 ----VRKIAGEVSRSEAWDVARELlRRLREQRHLAEQLQQLRMRLSELEqrlRQQQRAERLLAEFCKRLGKNLDDEDELE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1501 TLKREnknLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSEL----------QAALE-------EAEASLEHEEGKIL 1563
Cdd:PRK04863 558 QLQEE---LEARLESLSESVSEARERRMALRQQLEQLQARIQRLaarapawlaaQDALArlreqsgEEFEDSQDVTEYMQ 634
|
410 420 430
....*....|....*....|....*....|
gi 115527082 1564 RIQL---ELNQVKSEVDRKIAEKDEEIDQM 1590
Cdd:PRK04863 635 QLLErerELTVERDELAARKQALDEEIERL 664
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1249-1522 |
4.94e-08 |
|
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: 57.94 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1249 LEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIK 1328
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1329 AKSALAHALQSSRHdcdllREQYEEEQEAKAELQRAMSKANSevaqwrtkyeTDAI-QRTEELEEAKKKLAQRLQDAEEH 1407
Cdd:pfam09726 480 ARASAEKQLAEEKK-----RKKEEEATAARAVALAAASRGEC----------TESLkQRKRELESEIKKLTHDIKLKEEQ 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1408 VEAVNAKCASLEKTKQRlQNEVEDLMidvertNAACAALDKKQrnfdkilaewkqkceethaELEASQKESRSLSTELFk 1487
Cdd:pfam09726 545 IRELEIKVQELRKYKES-EKDTEVLM------SALSAMQDKNQ-------------------HLENSLSAETRIKLDLF- 597
|
250 260 270
....*....|....*....|....*....|....*
gi 115527082 1488 ikNAYEESLDQLETLKRENKNLQQEISDLTEQIAE 1522
Cdd:pfam09726 598 --SALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAE 630
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
835-1508 |
6.37e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.13 E-value: 6.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 835 KLYFKIKPLLKSAETEKEMANMKEEFEKTKEELAKTE--AKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAE------ 906
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttr 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 907 ERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKV 979
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 980 KNLTEEMAGLDETIAKLTKekkalQEAHQQTLDDLQAEEDKVNT----LTKAKIKLEQQVDDLEGSLEQEKKIRMDLERA 1055
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCG-----SQDEESDLERLKEEIEKSSKqramLAGATAVYSQFITQLTDENQSCCPVCQRVFQT 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1056 KRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAK 1135
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1136 AEKQRSDLSRELEEISERLEEAGGATSAQIEMnKKREAEFQKMRRDLEEATLqhEATAATLRKKHADSVAEL---GEQID 1212
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVCLTDVTIMERFQMEL-KDVERKIAQQAAKLQGSDL--DRTVQQVNQEKQEKQHELdtvVSKIE 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1213 NLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIktkeeeqQRLINDLTAQRARLQTESGEYS 1292
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV-------QSLIREIKDAKEQDSPLETFLE 919
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1293 RQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAK-AELQRAMSKANSE 1371
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQlEECEKHQEKINED 999
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1372 VAQWRTKYETDAIQ------------RTEELEEAKKKLAQRLQDAEEhveavnAKCASLEKTKQRLQNEVEDLMIDVERT 1439
Cdd:TIGR00606 1000 MRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELKQHLKEMGQ------MQVLQMKQEHQKLEENIDLIKRNHVLA 1073
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1440 NAACAALDKKQRNFDKILAEWK-QKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKN 1508
Cdd:TIGR00606 1074 LGRQKGYEKEIKHFKKELREPQfRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEIN 1143
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1274-1720 |
7.95e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1274 INDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFtQQIEELKRQLEEEIKAKSALA--HALQSSRHDCDLLREQY 1351
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL-EELREELEKLEKLLQLLPLYQelEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1352 EEEQEAKAELQRAMSKANSEVAQWRTkyetdaiQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVED 1431
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQE-------ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1432 LMIDVERTNAACAALDKKQRNFDkilAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESL-DQLETLKRENKNLQ 1510
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKE---ARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLaLLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1511 QEISDLteqiaEGGKRIHELEKikKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSevdrkiAEKDEEIDQM 1590
Cdd:COG4717 302 KEAEEL-----QALPALEELEE--EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE------LEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1591 KRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLnhanrmaAEALRNYRNTQAILKDTQLHLDDalrsqED 1670
Cdd:COG4717 369 EQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQL-------EELLGELEELLEALDEEELEEEL-----EE 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 115527082 1671 LKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAE--QELLDASERVQLL 1720
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEEDGELAEllQELEELKAELREL 488
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1392-1592 |
8.30e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1392 EAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAEL 1471
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1472 EASQKESRSLSTELFKIKNA-----------YEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQE 1540
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 115527082 1541 KSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQMKR 1592
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
886-1407 |
1.03e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 886 QEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTER-----AEDEEEINAELTAKKRKLED---ECSELKKD 957
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgngGDRLEQLEREIERLERELEErerRRARLEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 958 IDDLELTLAKVEKE----KHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKakiKLEQ 1033
Cdd:COG4913 368 LAALGLPLPASAEEfaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA---RLLA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1034 QVDDLEGSL-----------------EQEKKIRMDLERA-----------------------KRKLEGDL-----KLAQE 1068
Cdd:COG4913 445 LRDALAEALgldeaelpfvgelievrPEEERWRGAIERVlggfaltllvppehyaaalrwvnRLHLRGRLvyervRTGLP 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1069 STMDIENDKQQLDEKLKKKEFEMSG-LQSKI---------EDEQALGmQLQKKI-KELQARIEELEEEIEAERASRAK-- 1135
Cdd:COG4913 525 DPERPRLDPDSLAGKLDFKPHPFRAwLEAELgrrfdyvcvDSPEELR-RHPRAItRAGQVKGNGTRHEKDDRRRIRSRyv 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1136 ----AEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEAtaatlrkkhADSVAELGEQI 1211
Cdd:COG4913 604 lgfdNRAKLAALEAELAELEEELAEA----EERLEALEAELDALQERREALQRLAEYSWD---------EIDVASAEREI 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1212 DNLQRVKQKLEKEKSEMkmeiddlasnmetvskakgnlekmcRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEY 1291
Cdd:COG4913 671 AELEAELERLDASSDDL-------------------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1292 SRQLDEKDTLVSQLSRGKQAftQQIEELKRQLEEEIKAKSA--LAHALQSSRHDCDLLREQYEEeqeakaELQRAMSKAN 1369
Cdd:COG4913 726 EEELDELQDRLEAAEDLARL--ELRALLEERFAAALGDAVEreLRENLEERIDALRARLNRAEE------ELERAMRAFN 797
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 115527082 1370 SE----VAQWRTKYET----DAI---QRTEELEEAKKKLAQRLQDAEEH 1407
Cdd:COG4913 798 REwpaeTADLDADLESlpeyLALldrLEEDGLPEYEERFKELLNENSIE 846
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1391-1612 |
1.08e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1391 EEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAAcaaLDKKQRNFDKILAEWKQKCEETHAE 1470
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1471 LEASQKESRSLS--TELFKIKNaYEESLDQLETLKRENKNLQQEISDLTEQIAEggkriheLEKIKKQVEQEKSELQAAL 1548
Cdd:COG3883 92 ARALYRSGGSVSylDVLLGSES-FSDFLDRLSALSKIADADADLLEELKADKAE-------LEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115527082 1549 EEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSR 1612
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1436-1884 |
1.11e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1436 VERTNAACAALDKKQRNFDKILAEwKQKCEETHAELEASQKESRSLSTELFKIKNAYEEsLDQLETLKRENKNLQQEISD 1515
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1516 LTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQMKRNHI 1595
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1596 RIVESMQSTLDAEIRSRNDAIRLkkkmegDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQL 1675
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLL------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1676 AMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLEtdISQIQGEMEDIIQEARNA 1755
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1756 EEKakkaitDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALkggKKQIQKLEARVRELEGEVESEQK 1835
Cdd:COG4717 383 DEE------ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL---EEELEELEEELEELEEELEELRE 453
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 115527082 1836 RnveavkgLRKHERKVKELTyQTEEDRKNILRLQDLVDKLQAKVKSYKR 1884
Cdd:COG4717 454 E-------LAELEAELEQLE-EDGELAELLQELEELKAELRELAEEWAA 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1243-1474 |
1.47e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1243 SKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQ 1322
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1323 LEEEIKAKSALAHALQ-SSRHDcdllREQYEEEQEAKAELQRAMsKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRL 1401
Cdd:COG4942 99 LEAQKEELAELLRALYrLGRQP----PLALLLSPEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115527082 1402 QDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEAS 1474
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
655-679 |
1.66e-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: 1.66e-07
10 20
....*....|....*....|....*
gi 115527082 655 FRENLNKLMTNLRSTHPHFVRCIIP 679
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1066-1283 |
1.67e-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: 55.54 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1066 AQESTMDIENDKQQLDE---KLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSD 1142
Cdd:COG4942 15 AAAQADAAAEAEAELEQlqqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1143 LSRELEEISERLEE-------AGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKhadsVAELGEQIDNLQ 1215
Cdd:COG4942 95 LRAELEAQKEELAEllralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115527082 1216 RVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRAR 1283
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
984-1926 |
1.74e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 984 EEMAGLDETIAKLTKEK---KALQEAHQQTLDDLQAEEDkvnTLTKAKIKLEQQVDDLEGSL----------EQEKKIRM 1050
Cdd:PRK04863 279 NERRVHLEEALELRRELytsRRQLAAEQYRLVEMARELA---ELNEAESDLEQDYQAASDHLnlvqtalrqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1051 DLERAKRKLEGDL---KLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQarieeleeeie 1127
Cdd:PRK04863 356 DLEELEERLEEQNevvEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE----------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1128 aerasRAKAEKQRSDLsrELEEISERLEEAggATSAQIEMNKKREAEfQKMRrDLEEATLQHEATAATLRKkhadsvaeL 1207
Cdd:PRK04863 425 -----RAKQLCGLPDL--TADNAEDWLEEF--QAKEQEATEELLSLE-QKLS-VAQAAHSQFEQAYQLVRK--------I 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1208 GEQID--NLQRVKQKLEKEKSEMKMEIDDLA------SNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTA 1279
Cdd:PRK04863 486 AGEVSrsEAWDVARELLRRLREQRHLAEQLQqlrmrlSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1280 QRARLQtesgEYSRQLDEKDTlvsQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHaLQSSRHDCDLLREQYEEEQEAKA 1359
Cdd:PRK04863 566 RLESLS----ESVSEARERRM---ALRQQLEQLQARIQRLAARAPAWLAAQDALAR-LREQSGEEFEDSQDVTEYMQQLL 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1360 ELQRAMSKANSEVAQwrtkyetdaiqRTEELEEAKKKLAQ-------RLQDAEEHVEAV--------------------- 1411
Cdd:PRK04863 638 ERERELTVERDELAA-----------RKQALDEEIERLSQpggsedpRLNALAERFGGVllseiyddvsledapyfsaly 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1412 -NAKCA----SLEKTKQRLQNEvEDLMIDVERTNAACAALDKKQRNFDkilaewkqkcEETHAEL-EASQKE---SRSLS 1482
Cdd:PRK04863 707 gPARHAivvpDLSDAAEQLAGL-EDCPEDLYLIEGDPDSFDDSVFSVE----------ELEKAVVvKIADRQwrySRFPE 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1483 TELFKiKNAYEESLDQLetlkrenknlQQEISDLTEQIAEGGKRIHELEKIKKQV----------------EQEKSELQA 1546
Cdd:PRK04863 776 VPLFG-RAAREKRIEQL----------RAEREELAERYATLSFDVQKLQRLHQAFsrfigshlavafeadpEAELRQLNR 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1547 ALEEAEASLEHEEGKILRIQLELNQVKSEVD--RKIAekdEEIDQMKRNHI--RIVEsmqstLDAEIRSRNDAIRLKKKM 1622
Cdd:PRK04863 845 RRVELERALADHESQEQQQRSQLEQAKEGLSalNRLL---PRLNLLADETLadRVEE-----IREQLDEAEEAKRFVQQH 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1623 EGDLNEMEIQLN--HANRMAAEALR-NYRNTQAILKDTQLHLDdalrsqeDLKEqlaMVERRA--------NLLQAE--- 1688
Cdd:PRK04863 917 GNALAQLEPIVSvlQSDPEQFEQLKqDYQQAQQTQRDAKQQAF-------ALTE---VVQRRAhfsyedaaEMLAKNsdl 986
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1689 IEELRATLEQTERSRKIAEQELLDASERvqllHTQNT-------SLINTKKKLETDISQiqgEMEDI-IQEARNAEEKak 1760
Cdd:PRK04863 987 NEKLRQRLEQAEQERTRAREQLRQAQAQ----LAQYNqvlaslkSSYDAKRQMLQELKQ---ELQDLgVPADSGAEER-- 1057
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1761 kaitdAAMMAEELKKEQDTSahleRMKKN-LEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVRELEGEVESEQKRNVE 1839
Cdd:PRK04863 1058 -----ARARRDELHARLSAN----RSRRNqLEKQLTFCEAEMDNLT--------KKLRKLERDYHEMREQVVNAKAGWCA 1120
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1840 AVKGLRKH--ERKV--KELTYQTEEDRKNI---------------------LRLQDLVDKLQAKVKSY-------KRQAE 1887
Cdd:PRK04863 1121 VLRLVKDNgvERRLhrRELAYLSADELRSMsdkalgalrlavadnehlrdvLRLSEDPKRPERKVQFYiavyqhlRERIR 1200
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|
gi 115527082 1888 ----------EAEEQSNVNLSkfrRIQHELEEAEERADIA-ESQVNKLRV 1926
Cdd:PRK04863 1201 qdiirtddpvEAIEQMEIELS---RLTEELTSREQKLAISsESVANIIRK 1247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1066-1272 |
1.83e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1066 AQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR 1145
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1146 ELEEISERLEE-----------------AGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELG 1208
Cdd:COG4942 98 ELEAQKEELAEllralyrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115527082 1209 EQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQR 1272
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1429-1919 |
2.28e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1429 VEDLMIDVERTNAACAALdkkQRNFDKIlaewkqkcEETHAELEASQKESRSLsTELFKIKNAYEESLDQLETLK----- 1503
Cdd:COG4913 213 VREYMLEEPDTFEAADAL---VEHFDDL--------ERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEylraa 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1504 -------RENKNLQQEISDLTEQIAeggkrihelekikkQVEQEKSELQAALEEAEASLEHEEGKILRIQlelNQVKSEV 1576
Cdd:COG4913 281 lrlwfaqRRLELLEAELEELRAELA--------------RLEAELERLEARLDALREELDELEAQIRGNG---GDRLEQL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1577 DRKIAEKDEEIDQMKRNHiRIVESMQSTLDAEIRSrndairlkkkMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKD 1656
Cdd:COG4913 344 EREIERLERELEERERRR-ARLEALLAALGLPLPA----------SAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1657 TqlhLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLeqtERSRKIAEQ------ELLD----------ASERVqlL 1720
Cdd:COG4913 413 A---LRDLRRELRELEAEIASLERRKSNIPARLLALRDAL---AEALGLDEAelpfvgELIEvrpeeerwrgAIERV--L 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1721 HTQNTSLI--------------NTKK----------------------------KLETDISQIQGEMEDIIQE------A 1752
Cdd:COG4913 485 GGFALTLLvppehyaaalrwvnRLHLrgrlvyervrtglpdperprldpdslagKLDFKPHPFRAWLEAELGRrfdyvcV 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1753 RNAEE--KAKKAITDAAMM-----AEELKKEQDTSAHL------ERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKL 1819
Cdd:COG4913 565 DSPEElrRHPRAITRAGQVkgngtRHEKDDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEE-RLEALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1820 EARVRELEG--EVESEQKRNVEAVKGLRKHERKVKELtyqtEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNVNL 1897
Cdd:COG4913 644 QERREALQRlaEYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLE 719
|
570 580
....*....|....*....|..
gi 115527082 1898 SKFRRIQHELEEAEERADIAES 1919
Cdd:COG4913 720 KELEQAEEELDELQDRLEAAED 741
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
870-1613 |
2.43e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 56.21 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 870 TEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLA----DAEERCDQLIKTKIQ------------LEAKIKEVTERAEDE 933
Cdd:TIGR01612 984 KDASLNDYEAKNNELIKYFNDLKANLGKNKENMLyhqfDEKEKATNDIEQKIEdanknipnieiaIHTSIYNIIDEIEKE 1063
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 934 EEINAELTAKK--RKLEDECSELKKDIDDLEL----TLAKVEKEKHATE-NKVKNlteEMAGLDETIAKLTKEKKALQEA 1006
Cdd:TIGR01612 1064 IGKNIELLNKEilEEAEINITNFNEIKEKLKHynfdDFGKEENIKYADEiNKIKD---DIKNLDQKIDHHIKALEEIKKK 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1007 HQQTLDDLQAEEDKVNTLTKAKIkleqQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTmDIENDK--------- 1077
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDVADKAI----SNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIA-EIEKDKtsleevkgi 1215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1078 -------------QQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELqARIEELEEEIEAERASRAKAEKQRSDLS 1144
Cdd:TIGR01612 1216 nlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEM-GIEMDIKAEMETFNISHDDDKDHHIISK 1294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1145 RELEEISERLEEaggatSAQIEMNKKREAEFQKMRRDLEEATLQHEataatlrkKHADSVAELGEQIDNLQRVKQ--KLE 1222
Cdd:TIGR01612 1295 KHDENISDIREK-----SLKIIEDFSEESDINDIKKELQKNLLDAQ--------KHNSDINLYLNEIANIYNILKlnKIK 1361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1223 KEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALED--QLSEIKTKEEEQ------QRLINDLTAQRARLQTESGE---Y 1291
Cdd:TIGR01612 1362 KIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDdiNLEECKSKIESTlddkdiDECIKKIKELKNHILSEESNidtY 1441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1292 SRQLDEKDTLVSQLSRgkqaftqQIEELKRQLEEEIKAKSALAhalqSSRHDCDLlreqyeeeqeakAELQRAMSKANse 1371
Cdd:TIGR01612 1442 FKNADENNENVLLLFK-------NIEMADNKSQHILKIKKDNA----TNDHDFNI------------NELKEHIDKSK-- 1496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1372 vaqwrtKYETDAIQRTEELEEAKKKLAQRLQDAEEHVE-----AVNAKCASLEKTKQRLQNEVEDLmidverTNAACAAL 1446
Cdd:TIGR01612 1497 ------GCKDEADKNAKAIEKNKELFEQYKKDVTELLNkysalAIKNKFAKTKKDSEIIIKEIKDA------HKKFILEA 1564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1447 DKKQRNFDKILAEwKQKCEETHAELEASQKES-------RSLSTELFKIKNAYEESLDQLetlkRENKNLQQEISDLT-- 1517
Cdd:TIGR01612 1565 EKSEQKIKEIKKE-KFRIEDDAAKNDKSNKAAidiqlslENFENKFLKISDIKKKINDCL----KETESIEKKISSFSid 1639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1518 ---EQIAEGGKRIHELEKIKKQVEQEKSELqaalEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQMKRNH 1594
Cdd:TIGR01612 1640 sqdTELKENGDNLNSLQEFLESLKDQKKNI----EDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEE 1715
|
810 820
....*....|....*....|
gi 115527082 1595 IR-IVESMQSTLDAEIRSRN 1613
Cdd:TIGR01612 1716 IEsIKELIEPTIENLISSFN 1735
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
914-1271 |
2.61e-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: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 914 KTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDD-LELTLAKVEK----EKHATENKVKNLTEEMAG 988
Cdd:pfam09731 86 KKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEvLKEAISKAESatavAKEAKDDAIQAVKAHTDS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 989 LDETIAklTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDL-EGSLEQEKKIRMDLERAKRKLEGDLKLAQ 1067
Cdd:pfam09731 166 LKEASD--TAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLlDAAPETPPKLPEHLDNVEEKVEKAQSLAK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1068 ---ESTMDIENDKQQLDEKLKKKE------------FEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEaeras 1132
Cdd:pfam09731 244 lvdQYKELVASERIVFQQELVSIFpdiipvlkednlLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERAL----- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1133 rakaEKQRSDLSRELEEISERLEEAGGATSAQIEmnKKREAEFQKMRRDLEE---ATLQHEATAATLRKKHADSVAELGE 1209
Cdd:pfam09731 319 ----EKQKEELDKLAEELSARLEEVRAADEAQLR--LEFEREREEIRESYEEklrTELERQAEAHEEHLKDVLVEQEIEL 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115527082 1210 QIDNLQRVKQKLEKEKsemkmeiddlASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQ 1271
Cdd:pfam09731 393 QREFLQDIKEKVEEER----------AGRLLKLNELLANLKGLEKATSSHSEVEDENRKAQQ 444
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
867-1021 |
3.02e-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: 53.39 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 867 LAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTER-AEDEEEINAELTAKKR 945
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARiKKYEEQLGNVRNNKEY 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115527082 946 K-LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKV 1021
Cdd:COG1579 92 EaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
846-1298 |
3.10e-07 |
|
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: 55.50 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 846 SAETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKE 925
Cdd:pfam05483 330 TEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 926 V-TERAEDE---------EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAK 995
Cdd:pfam05483 410 LkKILAEDEklldekkqfEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 996 LT--------KEKKALQEAHQQTLDdLQAEEDKVNTLTKAKIKLEQQVDDLEgslEQEKKIRMDLERAKRKL--EGD--- 1062
Cdd:pfam05483 490 LTahcdklllENKELTQEASDMTLE-LKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFiqKGDevk 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1063 --LKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQalgmqlqKKIKELQARIEELEEEIEAERASRAKAEKQR 1140
Cdd:pfam05483 566 ckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN-------KNIEELHQENKALKKKGSAENKQLNAYEIKV 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1141 SDLSRELEEISERLEEAGGATSAQIEMNKKREaefQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQK 1220
Cdd:pfam05483 639 NKLELELASAKQKFEEIIDNYQKEIEDKKISE---EKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQ 715
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115527082 1221 LEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRlindltaQRARLQTESGEYSRQLDEK 1298
Cdd:pfam05483 716 YDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKE-------EKEKLKMEAKENTAILKDK 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1481-1762 |
3.14e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1481 LSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEheeg 1560
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1561 kilriqlelnqvksEVDRKIAEKDEEIDQMKRNHIRIVESMQstldaeirsrndairlkkkMEGDLNEMEIQLNHANrmA 1640
Cdd:COG4942 87 --------------ELEKEIAELRAELEAQKEELAELLRALY-------------------RLGRQPPLALLLSPED--F 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1641 AEALRNYRNTQAILKDTQLHLddalrsqEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLL 1720
Cdd:COG4942 132 LDAVRRLQYLKYLAPARREQA-------EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL 204
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 115527082 1721 HTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKA 1762
Cdd:COG4942 205 EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
867-1717 |
3.71e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.73 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 867 LAKTEAKRKELEEKMVTLMQEkndLQLQVQAEADSLADAEERCD--QLIKTKIQLEAKIK-------EVTERAEDEEEIN 937
Cdd:COG3096 294 LFGARRQLAEEQYRLVEMARE---LEELSARESDLEQDYQAASDhlNLVQTALRQQEKIEryqedleELTERLEEQEEVV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 938 AELTAKkrkledecselkkdiddleltLAKVEKEKHATENKVKNLTEEMA----GLDE--TIA-KLTKEKKALQEAHQQT 1010
Cdd:COG3096 371 EEAAEQ---------------------LAEAEARLEAAEEEVDSLKSQLAdyqqALDVqqTRAiQYQQAVQALEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1011 -LDDLQAE--EDKVNTLtKAKiklEQQVDDLEGSLEQekkiRMDL-ERAKRKLEGDLKLAQesTMDIENDKQQLDEKLKK 1086
Cdd:COG3096 430 gLPDLTPEnaEDYLAAF-RAK---EQQATEEVLELEQ----KLSVaDAARRQFEKAYELVC--KIAGEVERSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1087 KEFEMSGLQSKIEDEQALGMQLQKKIKELQarieeleeeieaeraSRAKAEKQRSDLSR----------ELEEISERLEe 1156
Cdd:COG3096 500 LLRRYRSQQALAQRLQQLRAQLAELEQRLR---------------QQQNAERLLEEFCQrigqqldaaeELEELLAELE- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1157 aggatsAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKK-----HADSVAE-----LGEQIDNLQRV----KQKLE 1222
Cdd:COG3096 564 ------AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlAAQDALErlreqSGEALADSQEVtaamQQLLE 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1223 KEKsEMKMEIDDLA-------SNMETVSKAKGNLEKMCRALEDQ-----LSEIK---TKEE-----------EQQRLIND 1276
Cdd:COG3096 638 RER-EATVERDELAarkqaleSQIERLSQPGGAEDPRLLALAERlggvlLSEIYddvTLEDapyfsalygpaRHAIVVPD 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1277 LTAQRARLQT-------------------ESGEYSRQLDEKDTLVS---QL--SR-------GKQAFTQQIEELKRQLEE 1325
Cdd:COG3096 717 LSAVKEQLAGledcpedlyliegdpdsfdDSVFDAEELEDAVVVKLsdrQWrySRfpevplfGRAAREKRLEELRAERDE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1326 EIK--AKSA--------LAHALQS--SRHDCDLLREQYEEE----QEAKAELQRAMSKANSEVAQWRTKYEtdaiQRTEE 1389
Cdd:COG3096 797 LAEqyAKASfdvqklqrLHQAFSQfvGGHLAVAFAPDPEAElaalRQRRSELERELAQHRAQEQQLRQQLD----QLKEQ 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1390 LEEAKK-----------KLAQRLQDAEEHVEAVNAKCASLEKTKQRLQnEVEDLMIDVERTNAACAALDKKQRNFDKILA 1458
Cdd:COG3096 873 LQLLNKllpqanlladeTLADRLEELREELDAAQEAQAFIQQHGKALA-QLEPLVAVLQSDPEQFEQLQADYLQAKEQQR 951
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1459 EWKQKC---------------EETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLT------ 1517
Cdd:COG3096 952 RLKQQIfalsevvqrrphfsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKssrdak 1031
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1518 -EQIAEGGKRIHELE-----KIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLE---LNQVKSEVDRKIAEKDEEID 1588
Cdd:COG3096 1032 qQTLQELEQELEELGvqadaEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEmdsLQKRLRKAERDYKQEREQVV 1111
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1589 QMKRNHIRIVEsmqstldaeiRSRNDAirlkkkMEGDLNEMEIQLNHANR---MAAEALRNYRNTQAILKdtqlHLDDAL 1665
Cdd:COG3096 1112 QAKAGWCAVLR----------LARDND------VERRLHRRELAYLSADElrsMSDKALGALRLAVADNE----HLRDAL 1171
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115527082 1666 RSQEDLKEQLAMV-----------ER-----------RANLLQAEIEELRATLEQTERsrkiaEQELLDASERV 1717
Cdd:COG3096 1172 RLSEDPRRPERKVqfyiavyqhlrERirqdiirtddpVEAIEQMEIELARLTEELTSR-----EQKLAISSESV 1240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
891-1364 |
4.26e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 891 LQLQVQAEADSLADAEERCDQLIKTKIQ-LEAKIKEvterAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVE 969
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKeLEEELKE----AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 970 KEK--HATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQtLDDLQAEedkvntLTKAKIKLEQQVDDLEGSLEQEkk 1047
Cdd:COG4717 123 KLLqlLPLYQELEALEAELAELPERLEELEERLEELRELEEE-LEELEAE------LAELQEELEELLEQLSLATEEE-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1048 irmdLERAKRKLEgdlklaqestmDIENDKQQLDEKLKkkefemsglqskiedeqalgmQLQKKIKELQARIEELEEEIE 1127
Cdd:COG4717 194 ----LQDLAEELE-----------ELQQRLAELEEELE---------------------EAQEELEELEEELEQLENELE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1128 AERASRAKAEKQRS--------DLSRELEEISERLEEAGGATSAQIEM-----------NKKREAEFQKMRRDLEEATLQ 1188
Cdd:COG4717 238 AAALEERLKEARLLlliaaallALLGLGGSLLSLILTIAGVLFLVLGLlallflllareKASLGKEAEELQALPALEELE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1189 HEATAATLRKKH------ADSVAELGEQIDNLQRVKQKLEKEKSEmkMEIDDLASNMETVskakgnLEKMCRALEDQLSE 1262
Cdd:COG4717 318 EEELEELLAALGlppdlsPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEIAAL------LAEAGVEDEEELRA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1263 IKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTlvSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRH 1342
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
490 500
....*....|....*....|..
gi 115527082 1343 DcDLLREQYEEEQEAKAELQRA 1364
Cdd:COG4717 468 D-GELAELLQELEELKAELREL 488
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
850-1839 |
4.73e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 55.44 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 850 EKEMANMKEEFEKTKEELAKTEAKRKELeekmvtlmqeKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTER 929
Cdd:TIGR01612 764 EKELSNKINDYAKEKDELNKYKSKISEI----------KNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 930 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVekekhatENKVKNlteEMAglDETIAKLTKEKKALQEAHQQ 1009
Cdd:TIGR01612 834 INEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAEL-------TNKIKA---EIS--DDKLNDYEKKFNDSKSLINE 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1010 TLDDLQAEEDKVNTLTkakiKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKL--KKK 1087
Cdd:TIGR01612 902 INKSIEEEYQNINTLK----KVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLidKIN 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1088 EFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASraKAEKQRSDLSRELEE------------------ 1149
Cdd:TIGR01612 978 ELDKAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFD--EKEKATNDIEQKIEDanknipnieiaihtsiyn 1055
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1150 ISERLEEAGGATSAQIEMNKKREAE-----FQKMRRDLEEATLQHEATAATLR-----KKHADSVAELGEQIDN----LQ 1215
Cdd:TIGR01612 1056 IIDEIEKEIGKNIELLNKEILEEAEinitnFNEIKEKLKHYNFDDFGKEENIKyadeiNKIKDDIKNLDQKIDHhikaLE 1135
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1216 RVKQKLEKEKSEMKMEIDDLASNMETvSKAKGNLEKMCRALEDQLSEIKTKE---EEQQRLINDLTaqrarlQTESGEYS 1292
Cdd:TIGR01612 1136 EIKKKSENYIDEIKAQINDLEDVADK-AISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIA------EIEKDKTS 1208
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1293 rqLDEKDTLvsQLSRGK---QAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQrAMSKAN 1369
Cdd:TIGR01612 1209 --LEEVKGI--NLSYGKnlgKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEME-TFNISH 1283
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1370 SEvaqwRTKYETDAIQRTEELEEAKKKLAQRLQDaeehveavNAKCASLEKTKQRLQNEVEDlmidvertnaacaaldkk 1449
Cdd:TIGR01612 1284 DD----DKDHHIISKKHDENISDIREKSLKIIED--------FSEESDINDIKKELQKNLLD------------------ 1333
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1450 qrnfdkilaewkqkceethaeleaSQKESRSLSTELFKIKNAYeesldqlETLKREN-KNLQQEISDLTEQIAEGGKRIH 1528
Cdd:TIGR01612 1334 ------------------------AQKHNSDINLYLNEIANIY-------NILKLNKiKKIIDEVKEYTKEIEENNKNIK 1382
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1529 -ELEKIKKQVE--QEKSELQAALEEAEASLEHEE--GKILRIQLELNQVKSE---VDRKIAEKDEEIDQMKRNHIRIVES 1600
Cdd:TIGR01612 1383 dELDKSEKLIKkiKDDINLEECKSKIESTLDDKDidECIKKIKELKNHILSEesnIDTYFKNADENNENVLLLFKNIEMA 1462
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1601 MQSTLDAEIRSRNDAirlKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQA---ILKDTQLHLDDALR--SQEDLKEQL 1675
Cdd:TIGR01612 1463 DNKSQHILKIKKDNA---TNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKnkeLFEQYKKDVTELLNkySALAIKNKF 1539
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1676 AMVERRANLLQAEIEELRA--TLEQTERSRKIAE--QELLDASERVQLLHTQNTSLINTKKKLET------DISQIQGEM 1745
Cdd:TIGR01612 1540 AKTKKDSEIIIKEIKDAHKkfILEAEKSEQKIKEikKEKFRIEDDAAKNDKSNKAAIDIQLSLENfenkflKISDIKKKI 1619
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1746 EDIIQEARNAEEKAKKAITDAamMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRldeaeqlalkggKKQIQKLEARVRE 1825
Cdd:TIGR01612 1620 NDCLKETESIEKKISSFSIDS--QDTELKENGDNLNSLQEFLESLKDQKKNIEDK------------KKELDELDSEIEK 1685
|
1050
....*....|....
gi 115527082 1826 LEGEVEsEQKRNVE 1839
Cdd:TIGR01612 1686 IEIDVD-QHKKNYE 1698
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1107-1567 |
5.36e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1107 QLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEAT 1186
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1187 LQHEATAATLRKKH-----ADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVS-KAKGNLEKMCRALEDQL 1260
Cdd:COG4717 126 QLLPLYQELEALEAelaelPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1261 SEIKTKEEEQQRL---INDLTAQRARLQTE--SGEYSRQLDEKDTLVSQLSR--GKQAFTQQIEELKRQLEEEIKAKSAL 1333
Cdd:COG4717 206 QRLAELEEELEEAqeeLEELEEELEQLENEleAAALEERLKEARLLLLIAAAllALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1334 AHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAvnA 1413
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE--L 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1414 KCASLEKTKQRLQNEVedLMIDVERTNAACAALDKKQrnfdkilaEWKQKCEETHAELEASQKESRSLSTELfkiknaye 1493
Cdd:COG4717 364 QLEELEQEIAALLAEA--GVEDEEELRAALEQAEEYQ--------ELKEELEELEEQLEELLGELEELLEAL-------- 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115527082 1494 esldQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEK--SELQAALEEAEASLEHEEGKILRIQL 1567
Cdd:COG4717 426 ----DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKL 497
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1254-1495 |
7.03e-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: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1254 RALEDQLSEIKTKEEEQQRLINDLTAQRARLQtesgeysRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSAl 1333
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALL-------KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1334 ahalqssrhdcdlLREQYEEEQEAKAELQRAMSKaNSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQdaeEHVEAVNA 1413
Cdd:COG4942 95 -------------LRAELEAQKEELAELLRALYR-LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR---EQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1414 KCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYE 1493
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
..
gi 115527082 1494 ES 1495
Cdd:COG4942 238 AA 239
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1053-1866 |
7.73e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.57 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1053 ERAKRKLEGDLKLAQE--STMDIENDKQQLDEKLKKKEFEMSGLQSKIEDE-QAL---------GMQLQKKIKELQARIE 1120
Cdd:COG3096 278 NERRELSERALELRRElfGARRQLAEEQYRLVEMARELEELSARESDLEQDyQAAsdhlnlvqtALRQQEKIERYQEDLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1121 ELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGG--ATSAQ-IEMNKKREAEFQKMRRDLEEATLQHEA---TAA 1194
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSqlADYQQaLDVQQTRAIQYQQAVQALEKARALCGLpdlTPE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1195 TLRKKHADSVAELGEQIDNLQRVKQKLekekSEMKMEIDDLASNMETVSKAKGNLEK----------MCR---------- 1254
Cdd:COG3096 438 NAEDYLAAFRAKEQQATEEVLELEQKL----SVADAARRQFEKAYELVCKIAGEVERsqawqtarelLRRyrsqqalaqr 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1255 --ALEDQLSEIKTKEEEQQRLIN-----------------DLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQ 1315
Cdd:COG3096 514 lqQLRAQLAELEQRLRQQQNAERlleefcqrigqqldaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1316 IEELKRQLEEEIKAKSALAHalqssrhdcdlLREQYEEEQEAKAELQRAMSK-ANSEVAQWRTKYEtdAIQRTEELEEAK 1394
Cdd:COG3096 594 IKELAARAPAWLAAQDALER-----------LREQSGEALADSQEVTAAMQQlLEREREATVERDE--LAARKQALESQI 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1395 KKLAQ-------RLQDAEEHVEAV------------NAKCAS--------------LEKTKQRLQNeVEDLMIDV----- 1436
Cdd:COG3096 661 ERLSQpggaedpRLLALAERLGGVllseiyddvtleDAPYFSalygparhaivvpdLSAVKEQLAG-LEDCPEDLylieg 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1437 -------------ERTNAACAALDKKQRNFDKI-------LAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYeESL 1496
Cdd:COG3096 740 dpdsfddsvfdaeELEDAVVVKLSDRQWRYSRFpevplfgRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLH-QAF 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1497 DQLETLKRE---NKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEE-----AEASLEHEEGKILRIQle 1568
Cdd:COG3096 819 SQFVGGHLAvafAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLlnkllPQANLLADETLADRLE-- 896
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1569 lnQVKSEVDrkIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSrNDAIRLkkkmegDLNEMEIQLNHAnRMAAEALrnyr 1648
Cdd:COG3096 897 --ELREELD--AAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQ-FEQLQA------DYLQAKEQQRRL-KQQIFAL---- 960
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1649 nTQAILKDTQLHLDDAlrsQEDLKEQLAMVERranllqaeieeLRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLI 1728
Cdd:COG3096 961 -SEVVQRRPHFSYEDA---VGLLGENSDLNEK-----------LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLK 1025
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1729 NTKK-KLETdISQIQGEMEDI-IQEARNAEEKAKkaitdaammaeELKKEQDTSAHLERMKKNleQTVKDLQHRLDEAEQ 1806
Cdd:COG3096 1026 SSRDaKQQT-LQELEQELEELgVQADAEAEERAR-----------IRRDELHEELSQNRSRRS--QLEKQLTRCEAEMDS 1091
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115527082 1807 LAlkggkKQIQKLEARVRELEGEVESeQKRNVEAVKGLRKH---ERKV--KELTYQTEEDRKNIL 1866
Cdd:COG3096 1092 LQ-----KRLRKAERDYKQEREQVVQ-AKAGWCAVLRLARDndvERRLhrRELAYLSADELRSMS 1150
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1133-1372 |
1.01e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1133 RAKAEKQRSDLSRELEEISERLEEAGGA------------TSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKH 1200
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAAleefrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1201 ADSVAELGEQIDNlqRVKQKLEKEKSEMKMEIDDLAsnmetvSKAKGNLEKMcRALEDQLSEIKTK-EEEQQRLINDLTA 1279
Cdd:COG3206 250 GSGPDALPELLQS--PVIQQLRAQLAELEAELAELS------ARYTPNHPDV-IALRAQIAALRAQlQQEAQRILASLEA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1280 QRARLQTESGEYSRQLDEKDTLVSQLSRgKQaftQQIEELKRQLEeeikaksalahalqssrhdcdLLREQYEE--EQEA 1357
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPE-LE---AELRRLEREVE---------------------VARELYESllQRLE 375
|
250
....*....|....*
gi 115527082 1358 KAELQRAMSKANSEV 1372
Cdd:COG3206 376 EARLAEALTVGNVRV 390
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1647-1939 |
1.04e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1647 YRNTQAILKDTQL---HLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLD---ASERVQLL 1720
Cdd:PRK03918 164 YKNLGEVIKEIKRrieRLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1721 HTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAK--KAITDAAMMAEELKKE----QDTSAHLERMKKNLEQTV 1794
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelKELKEKAEEYIKLSEFyeeyLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1795 KDLQHRLDEAEQLA--LKGGKKQIQKLEARVRELEGEVE--SEQKRNVEAVKGLRKH---------ERKVKELTYQTEED 1861
Cdd:PRK03918 324 NGIEERIKELEEKEerLEELKKKLKELEKRLEELEERHElyEEAKAKKEELERLKKRltgltpeklEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1862 RKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNV------------NLSKFRRIQHELEEAEERADIAESQVNKLRVKSR 1929
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
330
....*....|
gi 115527082 1930 EVHTKIISEE 1939
Cdd:PRK03918 484 ELEKVLKKES 493
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1457-1938 |
1.38e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1457 LAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQ 1536
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1537 VEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAI 1616
Cdd:pfam05483 181 TRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLT 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1617 RLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATL 1696
Cdd:pfam05483 261 FLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEEL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1697 EQTERSRKIAEQELLDASERVQ-LLHTQNTSLINTKKKLETDISQIQ---GEMEDIIQEARNAE---EKAKKAITDAAMM 1769
Cdd:pfam05483 341 NKAKAAHSFVVTEFEATTCSLEeLLRTEQQRLEKNEDQLKIITMELQkksSELEEMTKFKNNKEvelEELKKILAEDEKL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1770 AEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEqLALKGGKKQIQKLEARVRELEGEVESEQKRNVE---------- 1839
Cdd:pfam05483 421 LDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLE-IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEltahcdklll 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1840 -----------AVKGLRKHERKVKELTYQTEEDRKNILRLQD----LVDKLQAKVKSYKRQAEEAEEQSNVNLSKFRRIQ 1904
Cdd:pfam05483 500 enkeltqeasdMTLELKKHQEDIINCKKQEERMLKQIENLEEkemnLRDELESVREEFIQKGDEVKCKLDKSEENARSIE 579
|
490 500 510
....*....|....*....|....*....|....
gi 115527082 1905 HELEEAEERADIAESQVNKLRvKSREVHTKIISE 1938
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLK-KQIENKNKNIEE 612
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1081-1332 |
1.80e-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: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1081 DEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIeeleeeieaerasrAKAEKQRSDLSRELEEISERLEEAgga 1160
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEY--------------NELQAELEALQAEIDKLQAEIAEA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1161 tSAQIEmnkKREAEFQKMRRDLEEATLQHEATAATLrkkHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNME 1240
Cdd:COG3883 78 -EAEIE---ERREELGERARALYRSGGSVSYLDVLL---GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1241 TVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELK 1320
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|..
gi 115527082 1321 RQLEEEIKAKSA 1332
Cdd:COG3883 231 AAAAAAAAAAAA 242
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
867-1328 |
2.11e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.90 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 867 LAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLiktkiqlEAKIKEVTERAEDEEEINAELTAKKRK 946
Cdd:pfam10174 298 LSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL-------QTEVDALRLRLEEKESFLNKKTKQLQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 947 LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQ------TLDDLQAEEDK 1020
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtaltTLEEALSEKER 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1021 VNTLTKAKIKLEQQVDDLEgsLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGLQSKIED 1100
Cdd:pfam10174 451 IIERLKEQREREDRERLEE--LESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQ 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1101 EQALGMQLQKKIKELQarieeleeeiEAERASRAKAEkqRSDLSRELEEISERLEEAGGATSAQIE--MNKKREAEFQKM 1178
Cdd:pfam10174 529 KKEECSKLENQLKKAH----------NAEEAVRTNPE--INDRIRLLEQEVARYKEESGKAQAEVErlLGILREVENEKN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1179 RRD-----LEEATLQHEATAAT-----------LRKKHADSVAELGEQIDNLQRVKQK---------LEKEKSEMKMEID 1233
Cdd:pfam10174 597 DKDkkiaeLESLTLRQMKEQNKkvanikhgqqeMKKKGAQLLEEARRREDNLADNSQQlqleelmgaLEKTRQELDATKA 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1234 DLASNMETVSKAKGNLEKMCRALEDQLSEI-KTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEkdtlVSQLSRGKQAF 1312
Cdd:pfam10174 677 RLSSTQQSLAEKDGHLTNLRAERRKQLEEIlEMKQEALLAAISEKDANIALLELSSSKKKKTQEE----VMALKREKDRL 752
|
490
....*....|....*.
gi 115527082 1313 TQQieeLKRQLEEEIK 1328
Cdd:pfam10174 753 VHQ---LKQQTQNRMK 765
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1677-1939 |
3.47e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1677 MVERranLLQAEIEELRATLEQ-------TERsRKIAEQELLDASE---RVQLLHTQntslinTKKKLETdiSQIQGEME 1746
Cdd:TIGR02168 145 KISE---IIEAKPEERRAIFEEaagiskyKER-RKETERKLERTREnldRLEDILNE------LERQLKS--LERQAEKA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1747 DIIQEARNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLEARVREL 1826
Cdd:TIGR02168 213 ERYKELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEELRLEVSEL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1827 EGEVESEQKRNVEAVKGLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNVNLSKFRRIQHE 1906
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
250 260 270
....*....|....*....|....*....|...
gi 115527082 1907 LEEAEERADIAESQVNKLRVKSREVHTKIISEE 1939
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1495-1939 |
3.53e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1495 SLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKilriqlelnqvKS 1574
Cdd:PTZ00121 1068 QDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-----------KA 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1575 EVDRKIAEKDEEIDQMKRNHIRIVESMQSTldAEIRSRNDAirlkKKMEGDLNEMEIQLNHANRMAAEAlrnyRNTQAIL 1654
Cdd:PTZ00121 1137 EDARKAEEARKAEDAKRVEIARKAEDARKA--EEARKAEDA----KKAEAARKAEEVRKAEELRKAEDA----RKAEAAR 1206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1655 KDTQLHLDDALRSQEDLKEQLAMveRRANLLQAEIEELRATLEQ--TERSRKIAEQELLDASERVQLLHTQNTSLINTKK 1732
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAV--KKAEEAKKDAEEAKKAEEErnNEEIRKFEEARMAHFARRQAAIKAEEARKADELK 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1733 KLETDISQIQ---GEMEDIIQEARNAEEKAKKAiTDAAMMAEELKKEQDTsahlerMKKNLEQTVKDlqhrlDEAEQLAL 1809
Cdd:PTZ00121 1285 KAEEKKKADEakkAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADA------AKKKAEEAKKA-----AEAAKAEA 1352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1810 KGGKKQIQKLEARvRELEGEVESEQKRNVEAVKGLRKHERKVKELTYQTEEDRKNilrlQDLVDKLQAKVKSYKRQAEEA 1889
Cdd:PTZ00121 1353 EAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK----ADELKKAAAAKKKADEAKKKA 1427
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 115527082 1890 EEQSNVNLSKFR----RIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1939
Cdd:PTZ00121 1428 EEKKKADEAKKKaeeaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1662-1935 |
3.57e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1662 DDALRSQEDLKEQLA-MVERRANL--LQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDI 1738
Cdd:PRK02224 230 EQARETRDEADEVLEeHEERREELetLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1739 SQI---QGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQ 1815
Cdd:PRK02224 310 EAVearREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD---LEERAEELREEAAELESELEEARE-AVEDRREE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1816 IQKLEARVRELEGEVE--SEQKRNVEAVKGLRKHER-----KVKELTYQTEEDRKNILRLQDLVDklQAKVKSYKRQAEE 1888
Cdd:PRK02224 386 IEELEEEIEELRERFGdaPVDLGNAEDFLEELREERdelreREAELEATLRTARERVEEAEALLE--AGKCPECGQPVEG 463
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 115527082 1889 AEeqsnvnlskfrrIQHELEEAEERADIAESQVNKLRVKSREVHTKI 1935
Cdd:PRK02224 464 SP------------HVETIEEDRERVEELEAELEDLEEEVEEVEERL 498
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1005-1189 |
4.04e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1005 EAHQQTLDDLQAEEDKVNTLTKAK-------IKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQEstmDIENDK 1077
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLkelpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1078 QQLDEKLKKKEFEmsGLQSKIEDEQALGMQLQKKIKELQARIEELEEEIeaerasrAKAEKQRSDLSRELEEISERLEEA 1157
Cdd:COG1579 80 EQLGNVRNNKEYE--ALQKEIESLKRRISDLEDEILELMERIEELEEEL-------AELEAELAELEAELEEKKAELDEE 150
|
170 180 190
....*....|....*....|....*....|..
gi 115527082 1158 GGATSAQIEmnkKREAEFQKMRRDLEEATLQH 1189
Cdd:COG1579 151 LAELEAELE---ELEAEREELAAKIPPELLAL 179
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
899-1913 |
5.10e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.98 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 899 ADSLADAEERCDQLIKTKiqleAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDI----DDLELTLAKVEKEKHA 974
Cdd:TIGR01612 768 SNKINDYAKEKDELNKYK----SKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTIsikeDEIFKIINEMKFMKDD 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 975 TENKV-------KNLTEEMAGLDETIAKLTKEKKAlqEAHQQTLDDLQAE----EDKVNTLTKAKIKLEQQVDDL----- 1038
Cdd:TIGR01612 844 FLNKVdkfinfeNNCKEKIDSEHEQFAELTNKIKA--EISDDKLNDYEKKfndsKSLINEINKSIEEEYQNINTLkkvde 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1039 -----EGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKL--KKKEFEMSGLQSKIEDEQALGMQLQKK 1111
Cdd:TIGR01612 922 yikicENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLidKINELDKAFKDASLNDYEAKNNELIKY 1001
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1112 IKELQARIEELEEEIEAERASraKAEKQRSDLSRELEE------------------ISERLEEAGGATSAQIEMNKKREA 1173
Cdd:TIGR01612 1002 FNDLKANLGKNKENMLYHQFD--EKEKATNDIEQKIEDanknipnieiaihtsiynIIDEIEKEIGKNIELLNKEILEEA 1079
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1174 E-----FQKMRRDLEEATLQHEATAATLR-----KKHADSVAELGEQIDN----LQRVKQKLEKEKSEMKMEIDDLASNM 1239
Cdd:TIGR01612 1080 EinitnFNEIKEKLKHYNFDDFGKEENIKyadeiNKIKDDIKNLDQKIDHhikaLEEIKKKSENYIDEIKAQINDLEDVA 1159
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1240 ETvSKAKGNLEKMCRALEDQLSEIKTKE---EEQQRLINDLTaqrarlQTESGEYSrqLDEKDTLvsQLSRGK---QAFT 1313
Cdd:TIGR01612 1160 DK-AISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIA------EIEKDKTS--LEEVKGI--NLSYGKnlgKLFL 1228
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1314 QQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQrAMSKANSEvaqwRTKYETDAIQRTEELEEA 1393
Cdd:TIGR01612 1229 EKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEME-TFNISHDD----DKDHHIISKKHDENISDI 1303
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1394 KKKLAQRLQDaeehveavNAKCASLEKTKQRLQNEVEDlmidvertnaacaaldkkqrnfdkilaewkqkceethaelea 1473
Cdd:TIGR01612 1304 REKSLKIIED--------FSEESDINDIKKELQKNLLD------------------------------------------ 1333
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1474 SQKESRSLSTELFKIKNAYEesldqleTLKREN-KNLQQEISDLTEQIAEGGKRIH-ELEKIKKQVEQEKSELqaALEEA 1551
Cdd:TIGR01612 1334 AQKHNSDINLYLNEIANIYN-------ILKLNKiKKIIDEVKEYTKEIEENNKNIKdELDKSEKLIKKIKDDI--NLEEC 1404
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1552 EASLEheegkilriqlelnqvkSEVDRKiaEKDEEIDQMK--RNHIRIVESMQSTLDAEIRSRNDAIRLkkkmegDLNEM 1629
Cdd:TIGR01612 1405 KSKIE-----------------STLDDK--DIDECIKKIKelKNHILSEESNIDTYFKNADENNENVLL------LFKNI 1459
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1630 EIqlnhANRMAAEALRNYRNTQAILKDTQLHlddalrsqeDLKEQLamveRRANLLQAEIEElraTLEQTERSRKIAEQ- 1708
Cdd:TIGR01612 1460 EM----ADNKSQHILKIKKDNATNDHDFNIN---------ELKEHI----DKSKGCKDEADK---NAKAIEKNKELFEQy 1519
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1709 -----ELLDASERVQLlhtqNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKEQDTSahl 1783
Cdd:TIGR01612 1520 kkdvtELLNKYSALAI----KNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSN--- 1592
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1784 eRMKKNLEQTVKDLQHRLDEAEQLALKGGK--KQIQKLEARVRELE-GEVESEQKRNVEAVKGLRKHERKVKELTYQTEE 1860
Cdd:TIGR01612 1593 -KAAIDIQLSLENFENKFLKISDIKKKINDclKETESIEKKISSFSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIED 1671
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*...
gi 115527082 1861 DRKNILRLQDLVDKLQAKVKSYKRQ-----AEEAEEQSNVNLSKFRRIQHELEEAEER 1913
Cdd:TIGR01612 1672 KKKELDELDSEIEKIEIDVDQHKKNyeigiIEKIKEIAIANKEEIESIKELIEPTIEN 1729
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1236-1557 |
5.10e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1236 ASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLIN------DLTAQRARLQTESGEYSRQLDEKDTLVSQlsRGK 1309
Cdd:COG3096 271 ADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEmareleELSARESDLEQDYQAASDHLNLVQTALRQ--QEK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1310 -QAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMskansEVAQWRTKYETDAIQRTE 1388
Cdd:COG3096 349 iERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQAL-----DVQQTRAIQYQQAVQALE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1389 ELEEAKKKLAQRLQDAEEHVEAVNAKCASLekTKQRLQNE-------------------VEDLMIDVERTNAACAA--LD 1447
Cdd:COG3096 424 KARALCGLPDLTPENAEDYLAAFRAKEQQA--TEEVLELEqklsvadaarrqfekayelVCKIAGEVERSQAWQTAreLL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1448 KKQRNFdKILAEWKQKCEETHAELE---ASQKESRSLSTELFKIKNAYEESLDQLETLKREnknLQQEISDLTEQIAEGG 1524
Cdd:COG3096 502 RRYRSQ-QALAQRLQQLRAQLAELEqrlRQQQNAERLLEEFCQRIGQQLDAAEELEELLAE---LEAQLEELEEQAAEAV 577
|
330 340 350
....*....|....*....|....*....|....*.
gi 115527082 1525 KRIHELEKIKKQVEQEKSELQA---ALEEAEASLEH 1557
Cdd:COG3096 578 EQRSELRQQLEQLRARIKELAArapAWLAAQDALER 613
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1255-1413 |
5.41e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1255 ALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAK--SA 1332
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1333 LAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVN 1412
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
.
gi 115527082 1413 A 1413
Cdd:COG1579 174 P 174
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1307-1902 |
5.46e-06 |
|
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: 51.68 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1307 RGKQAFTQQIEELKRQ------LEEEI----------------------------KAKSALAHALQSSRHDCDLLREQYE 1352
Cdd:pfam07111 56 EGSQALSQQAELISRQlqelrrLEEEVrllretslqqkmrleaqameldalavaeKAGQAEAEGLRAALAGAEMVRKNLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1353 E------------EQEAKAELQRAMSKANSEVA-------QWRTKYETDAIQRTEELEEAKKK---LAQRLQDAEEHVEA 1410
Cdd:pfam07111 136 EgsqreleeiqrlHQEQLSSLTQAHEEALSSLTskaegleKSLNSLETKRAGEAKQLAEAQKEaelLRKQLSKTQEELEA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1411 VNAKCASLEK-----------------TKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILA----EWKQKCEETHA 1469
Cdd:pfam07111 216 QVTLVESLRKyvgeqvppevhsqtwelERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLAlqeeELTRKIQPSDS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1470 ELEASQKESRSLstelfkIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEggkrihELEKIKKQvEQEKSELQAALE 1549
Cdd:pfam07111 296 LEPEFPKKCRSL------LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAE------LQEQVTSQ-SQEQAILQRALQ 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1550 EAEASLEHEEGKILRIQLELNQVKsEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEM 1629
Cdd:pfam07111 363 DKAAEVEVERMSAKGLQMELSRAQ-EARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYA 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1630 EIQLNHANRMAAE--ALRNYRNTQAILKDTQLHLDdalrsqEDLKEQLAMVERRANLLQAEIeELRATLEQTERSRKIAE 1707
Cdd:pfam07111 442 VRKVHTIKGLMARkvALAQLRQESCPPPPPAPPVD------ADLSLELEQLREERNRLDAEL-QLSAHLIQQEVGRAREQ 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1708 QElldaSERVQllhtqntsLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKEQdtsahlERMK 1787
Cdd:pfam07111 515 GE----AERQQ--------LSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQ------EIYG 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1788 KNLEQTVKDLQHRLDEaeqlalkggkkQIQKLEARVRElegevesEQKRNVEAVKGLRKHERKVKeltyQTEEDRKNILR 1867
Cdd:pfam07111 577 QALQEKVAEVETRLRE-----------QLSDTKRRLNE-------ARREQAKAVVSLRQIQHRAT----QEKERNQELRR 634
|
650 660 670
....*....|....*....|....*....|....*
gi 115527082 1868 LQDLVDKLQAkvKSYKRQAEEAEEQSNVNLSKFRR 1902
Cdd:pfam07111 635 LQDEARKEEG--QRLARRVQELERDKNLMLATLQQ 667
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1579-1930 |
5.75e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.44 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1579 KIAEKDEEIDQMKRNHIRIVESM--QSTLDAEIRSRNDAIRLKK----------KMEGDLNEMEIQLNHANRMAAEALRN 1646
Cdd:PLN02939 64 KLQSNTDENGQLENTSLRTVMELpqKSTSSDDDHNRASMQRDEAiaaidneqqtNSKDGEQLSDFQLEDLVGMIQNAEKN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1647 YrntqailkdtqLHLDDA-LRSQEDLKEQLAmvERRAnlLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNT 1725
Cdd:PLN02939 144 I-----------LLLNQArLQALEDLEKILT--EKEA--LQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1726 SLINTKKKLETDISQIQGEMEDIIQEarNAEEKAkkaitDAAMMAEELKKEQDTS---AHLERMKKNLEQTVKDLQHRLD 1802
Cdd:PLN02939 209 ELLIRGATEGLCVHSLSKELDVLKEE--NMLLKD-----DIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1803 EAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKH---ERKVKELTYQTEEdrKNILRLQ-DLVDKLQAK 1878
Cdd:PLN02939 282 VAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNqdlRDKVDKLEASLKE--ANVSKFSsYKVELLQQK 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 115527082 1879 VKSYKRQAEEAEEQSNvnlSKFRRIQHELEEAEeraDIAESQVNKLRVKSRE 1930
Cdd:PLN02939 360 LKLLEERLQASDHEIH---SYIQLYQESIKEFQ---DTLSKLKEESKKRSLE 405
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1457-1589 |
6.44e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1457 LAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLK--RENKNLQQEISDLTEQIAEGGKRIHELEKIK 1534
Cdd:COG1579 40 LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQKEIESLKRRISDLEDEILELMERI 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 115527082 1535 KQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQ 1589
Cdd:COG1579 120 EELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1137-1428 |
7.13e-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: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1137 EKQRSDLSRELEEISERLEEAggatsaQIEMNKKREAEFQKMRRDLEEATLQHEAT---AATLRKKHADSVAELGEQIDN 1213
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQE------RLRQEKEEKAREVERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1214 LQRVKQKLEKEK---SEMKMEIDDLaSNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESgE 1290
Cdd:pfam17380 353 IRQEERKRELERirqEEIAMEISRM-RELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ-E 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1291 YSRQL------DEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAE---- 1360
Cdd:pfam17380 431 EARQRevrrleEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQamie 510
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115527082 1361 -------LQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNE 1428
Cdd:pfam17380 511 eerkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESE 585
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1138-1733 |
9.40e-06 |
|
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: 50.91 E-value: 9.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1138 KQRSDLSRELEEIsERLEEaggatsaqiEMNKKREAEFQKMRRdLEEATLQHEATAATLRKKHADSVAeLGEQIDNLQRV 1217
Cdd:pfam07111 63 QQAELISRQLQEL-RRLEE---------EVRLLRETSLQQKMR-LEAQAMELDALAVAEKAGQAEAEG-LRAALAGAEMV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1218 KQKLEKEKSEMKMEIDDLASNmetvskakgNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRArlqTESGEYSRQLDE 1297
Cdd:pfam07111 131 RKNLEEGSQRELEEIQRLHQE---------QLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRA---GEAKQLAEAQKE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1298 KDTLVSQLSRGKQAFTQQI---EELKRQLEEEIKA----------KSALAHALQSSRHDCDLLREQYE------------ 1352
Cdd:pfam07111 199 AELLRKQLSKTQEELEAQVtlvESLRKYVGEQVPPevhsqtweleRQELLDTMQHLQEDRADLQATVEllqvrvqslthm 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1353 ---EEQEAKAELQRAMS-------KANSEVAQWRTKYETDAIQ-RTEELE--EAKKKLAQRLQDAEEHVEAVNAKCASLE 1419
Cdd:pfam07111 279 lalQEEELTRKIQPSDSlepefpkKCRSLLNRWREKVFALMVQlKAQDLEhrDSVKQLRGQVAELQEQVTSQSQEQAILQ 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1420 KTKQRLQNEVE-------DLMIDVERTNAA-------CAALDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTEL 1485
Cdd:pfam07111 359 RALQDKAAEVEvermsakGLQMELSRAQEArrrqqqqTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRL 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1486 -FKIKNAYeeSLDQLETLKRENKNLQQEISDLTEQIAEGGKRIH-ELEKIKKQVEQEKSELQ--AALEEAEASLEHEEGK 1561
Cdd:pfam07111 439 sYAVRKVH--TIKGLMARKVALAQLRQESCPPPPPAPPVDADLSlELEQLREERNRLDAELQlsAHLIQQEVGRAREQGE 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1562 ILRIQLelnqvkSEVDRKIaekDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEgdlNEMEIQLNHANRMAA 1641
Cdd:pfam07111 517 AERQQL------SEVAQQL---EQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELT---QQQEIYGQALQEKVA 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1642 EALRNYRNTqaiLKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQterSRKIAEQELldaSERVQLLH 1721
Cdd:pfam07111 585 EVETRLREQ---LSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDE---ARKEEGQRL---ARRVQELE 655
|
650
....*....|..
gi 115527082 1722 TQNTSLINTKKK 1733
Cdd:pfam07111 656 RDKNLMLATLQQ 667
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1472-1700 |
9.80e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1472 EASQKESRSLSTELFKIKNAYEESLDQLETLKRENK--NLQQEISDLTEQIAEggkrihelekikkqVEQEKSELQAALE 1549
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE--------------LESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1550 EAEASLEHEEGKILRIQLEL-----NQVKSEVDRKIAEKDEEIDQMKR----NHIRIVEsmqstLDAEIRSrndairLKK 1620
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALpellqSPVIQQLRAQLAELEAELAELSArytpNHPDVIA-----LRAQIAA------LRA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1621 KMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRsqedlkeQLAMVERRANLLQAEIEELRATLEQTE 1700
Cdd:COG3206 306 QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEA-------ELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1485-1887 |
1.19e-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: 50.24 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1485 LFKIKNAYEEsLDQLETLKRE--NKNLQQEISDLtEQIAEGGKRIHELEKIKKQ----VEQEKSELQAALEEAEASLEhe 1558
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1559 EGKILRIQLELNQVKS---EVDRKIAEKDEEIDQMK------RNHIRIVESMQSTLDAEIRSRNDAI-RLKKKMEGDLNE 1628
Cdd:pfam06160 78 KYRFKKAKKALDEIEElldDIEEDIKQILEELDELLeseeknREEVEELKDKYRELRKTLLANRFSYgPAIDELEKQLAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1629 MEIQLNHANRMAAEAlrNYRNTQAILKDTQLHLDDAlrsQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQ 1708
Cdd:pfam06160 158 IEEEFSQFEELTESG--DYLEAREVLEKLEEETDAL---EELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALEH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1709 elLDASERVQLLHTQNTSLINTKKKLETD-----ISQIQGEMEDIiQEARNAEEKAKKaitdaammaeELKKEQDT-SAH 1782
Cdd:pfam06160 233 --LNVDKEIQQLEEQLEENLALLENLELDeaeeaLEEIEERIDQL-YDLLEKEVDAKK----------YVEKNLPEiEDY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1783 LERMKKNLEQTVKDLQH-----RLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNV-------EAVKGLRKHERK 1850
Cdd:pfam06160 300 LEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSelqeeleEILEQLEEIEEE 379
|
410 420 430
....*....|....*....|....*....|....*..
gi 115527082 1851 VKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAE 1887
Cdd:pfam06160 380 QEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
863-1233 |
1.24e-05 |
|
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: 50.40 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 863 TKEELAKTEAKRKELEEKMVTLMQEKNDLQLQVQaeaDSLADAEERCDQLIKTKIQLEaKIKEvtERAEDEEEINaELTA 942
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELT---NSESENSEKQRELEEKQNEIE-KLKK--ENQSYKQEIK-NLES 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 943 KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALqeahqqtlddlqaeEDKVN 1022
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK--------------ELIIK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1023 TLTKAKIKLEQQVDDLEGSLeqeKKIRMDLERAKRKLEGDLKLAQEstmdIENDKQQLDEKLKKKEFEMSGLQSKIEDEQ 1102
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSI---NKIKQNLEQKQKELKSKEKELKK----LNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1103 ALGMQLQKKIKELQARIEELEEEIEaerasRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDL 1182
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 115527082 1183 EEatlqHEATAATLRKKHADSVAE---LGEQIDNLQRVKQKLEKEKSEMKMEID 1233
Cdd:TIGR04523 606 EE----KEKKISSLEKELEKAKKEnekLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1348-1709 |
1.56e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 49.76 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1348 REQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQD-AEEHVEAVNAKCASLEKTKQRLQ 1426
Cdd:pfam09731 77 GESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEvLKEAISKAESATAVAKEAKDDAI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1427 NEVEDLMIDVERTNAACAALDKKQRNFDKILAE-WKQKCEETHAELEASQKES-RSLSTELFKIKNAYEESLDQLETLKR 1504
Cdd:pfam09731 157 QAVKAHTDSLKEASDTAEISREKATDSALQKAEaLAEKLKEVINLAKQSEEEAaPPLLDAAPETPPKLPEHLDNVEEKVE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1505 ENKNLQQEISDLTEQIAEG-GKRIHELEKIKKQVEQEKSELQAAL-EEAEASLEHEEGKILRIQLELNQVKSEVDRK--- 1579
Cdd:pfam09731 237 KAQSLAKLVDQYKELVASErIVFQQELVSIFPDIIPVLKEDNLLSnDDLNSLIAHAHREIDQLSKKLAELKKREEKHier 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1580 -IAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIR--LKKKMEgdlNEMEIQLNHANRMAAEALRNYRNTQAILKD 1656
Cdd:pfam09731 317 aLEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREReeIRESYE---EKLRTELERQAEAHEEHLKDVLVEQEIELQ 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 115527082 1657 tqlhlddaLRSQEDLKEQlamVERRANLLQAEIEELRATLEQTER---SRKIAEQE 1709
Cdd:pfam09731 394 --------REFLQDIKEK---VEEERAGRLLKLNELLANLKGLEKatsSHSEVEDE 438
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
882-1434 |
1.61e-05 |
|
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: 50.12 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 882 VTLMQEKNDLQLQ----VQAEADSLADAEERCDQLiktKIQLEAK---IKEVTERAEDEEEINAELTAKKRKLEDECSEL 954
Cdd:pfam15921 519 ITKLRSRVDLKLQelqhLKNEGDHLRNVQTECEAL---KLQMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQL 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 955 KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT-------KEKKALQEAHQQTLDDLQAEEDKVNTLTKA 1027
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSED 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1028 KIKLEQQVDDLEGSLEQE-KKIRMDLERAKRKLEgdlklaqestmdiendkqQLDEKLKKKEfEMSGLQSKIedeqALGM 1106
Cdd:pfam15921 676 YEVLKRNFRNKSEEMETTtNKLKMQLKSAQSELE------------------QTRNTLKSME-GSDGHAMKV----AMGM 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1107 QLQ-----KKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRD 1181
Cdd:pfam15921 733 QKQitakrGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVA 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1182 LEEATLQ----------HEATAATLRKKHADSVAEL-GEQIDNLQRVKQKLEKEKSEMKMEiDDLASNMETVS------- 1243
Cdd:pfam15921 813 LDKASLQfaecqdiiqrQEQESVRLKLQHTLDVKELqGPGYTSNSSMKPRLLQPASFTRTH-SNVPSSQSTASflshhsr 891
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1244 KAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARlQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQL 1323
Cdd:pfam15921 892 KTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGR-APSLGALDDRVRDCIIESSLRSDICHSSSNSLQTEGSKS 970
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1324 EEEIKAKSALAHALQ-SSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKK-KLAQRL 1401
Cdd:pfam15921 971 SETCSREPVLLHAGElEDPSSCFTFPSTASPSVKNSASRSFHSSPKKSPVHSLLTSSAEGSIGSSSQYRSAKTiHSPDSV 1050
|
570 580 590
....*....|....*....|....*....|....
gi 115527082 1402 QDAEEH-VEAVNAKCASLEKTKQRLQNEVEDLMI 1434
Cdd:pfam15921 1051 KDSQSLpIETTGKTCRKLQNRLESLQTLVEDLQL 1084
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
839-1086 |
2.01e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 839 KIKPLLKSAETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLMQEK-----------NDLQLQVQAEADSLADAEE 907
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEElekkaeeyeklKEKLIKLKGEIKSLKKELE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 908 RCDQLIKTKIQLEAKIKEV-TERAEDEEEINAELTAKKRKLEDECSELKKdIDDLELTLAKVEKEKHATENKVKNLTEEm 986
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELeEELAELLKELEELGFESVEELEERLKELEP-FYNEYLELKDAEKELEREEKELKKLEEE- 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 987 agLDETIAKLTKEKKALQEAHQQtLDDLQAE--EDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLK 1064
Cdd:PRK03918 628 --LDKAFEELAETEKRLEELRKE-LEELEKKysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
250 260
....*....|....*....|....*...
gi 115527082 1065 LAQESTMDIEN------DKQQLDEKLKK 1086
Cdd:PRK03918 705 EREKAKKELEKlekaleRVEELREKVKK 732
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
848-1334 |
2.16e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.51 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 848 ETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLMQEKNDLQlqvQAEADSLADAEERCDQLIKTKIQLEAKIK--- 924
Cdd:PRK01156 239 SALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHM---KIINDPVYKNRNYINDYFKYKNDIENKKQils 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 925 ----------EVTERAEDEEEINAELTAKKRKLED---ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDE 991
Cdd:PRK01156 316 nidaeinkyhAIIKKLSVLQKDYNDYIKKKSRYDDlnnQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 992 TIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEqekkirMDLERAKRKLEGDlKLAQESTM 1071
Cdd:PRK01156 396 ILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNME------MLNGQSVCPVCGT-TLGEEKSN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1072 DI----ENDKQQLDEKLKKKEFEMSGLQSKIEDEQALGMQLQK-----------KIKELQARIEELEEEIEAERASRAKA 1136
Cdd:PRK01156 469 HIinhyNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeeinksineynKIESARADLEDIKIKINELKDKHDKY 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1137 EKQRSDL-SRELEEISERLEEAGGATSA----QIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQI 1211
Cdd:PRK01156 549 EEIKNRYkSLKLEDLDSKRTSWLNALAVisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEA 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1212 DNLQRVKQKLEKEKSEMKmEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQtesgey 1291
Cdd:PRK01156 629 NNLNNKYNEIQENKILIE-KLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLE------ 701
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 115527082 1292 srqldekdTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALA 1334
Cdd:PRK01156 702 --------STIEILRTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1496-1751 |
2.43e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 48.38 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1496 LDQLETLKRENKNLQQEISDLTEQ---------------IAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEG 1560
Cdd:pfam00038 17 IDKVRFLEQQNKLLETKISELRQKkgaepsrlyslyekeIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1561 K---------ILRIQL-ELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRN-DAIRlKKKMEGDLNEM 1629
Cdd:pfam00038 97 LrtsaendlvGLRKDLdEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEmDAAR-KLDLTSALAEI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1630 EIQL-NHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQedlKEQLAMVERRANLLQAEIEELRATLEQTERSrkIAEQ 1708
Cdd:pfam00038 176 RAQYeEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSA---KEEITELRRTIQSLEIELQSLKKQKASLERQ--LAET 250
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 115527082 1709 ElldasERVQLLHTQNTSLINtkkKLETDISQIQGEMEDIIQE 1751
Cdd:pfam00038 251 E-----ERYELQLADYQELIS---ELEAELQETRQEMARQLRE 285
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1306-1861 |
2.54e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.69 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1306 SRGKQAFTQQIEELKRQLEEEIKAKSalahalqssrhdcdLLREQYEEEQEAKAE--LQRAMSKANSEVAQWRTKYETDA 1383
Cdd:COG5022 805 LLGSRKEYRSYLACIIKLQKTIKREK--------------KLRETEEVEFSLKAEvlIQKFGRSLKAKKRFSLLKKETIY 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1384 IQRTEELEEAKKKLaQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVE-DLMIDVERTNAACAALDKKQRNFDKILAEWKQ 1462
Cdd:COG5022 871 LQSAQRVELAERQL-QELKIDVKSISSLKLVNLELESEIIELKKSLSsDLIENLEFKTELIARLKKLLNNIDLEEGPSIE 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1463 KCEEThaELEASQKESRSLSTELFKIKNAYEesldQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKS 1542
Cdd:COG5022 950 YVKLP--ELNKLHEVESKLKETSEEYEDLLK----KSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPV 1023
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1543 ELqAALEEAEASLEHeEGKILRIQLELNQVKSEVDRKIAE---KDEEIDQMKRNHIRI---VESMQSTldaeirsRNDAI 1616
Cdd:COG5022 1024 EV-AELQSASKIISS-ESTELSILKPLQKLKGLLLLENNQlqaRYKALKLRRENSLLDdkqLYQLEST-------ENLLK 1094
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1617 RLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAE----IEEL 1692
Cdd:COG5022 1095 TINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEalpsPPPF 1174
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1693 RATLEQTERSRKIAEQELLDASERVQLLhtqnTSLINTKKKLETDISQIQGEMEDIIQEARNAEEkAKKAITDAAMMAEE 1772
Cdd:COG5022 1175 AALSEKRLYQSALYDEKSKLSSSEVNDL----KNELIALFSKIFSGWPRGDKLKKLISEGWVPTE-YSTSLKGFNNLNKK 1249
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1773 LKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQI-----QKLEARVRELEGEVESEQKRNVEaVKGLRKH 1847
Cdd:COG5022 1250 FDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYInvglfNALRTKASSLRWKSATEVNYNSE-ELDDWCR 1328
|
570
....*....|....
gi 115527082 1848 ERKVKELTYQTEED 1861
Cdd:COG5022 1329 EFEISDVDEELEEL 1342
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
941-1235 |
2.65e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 941 TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATE------NKVKNLTEE---MAGLDETIAKLTKEKKALQEAHqqtl 1011
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQerrealQRLAEYSWDeidVASAEREIAELEAELERLDASS---- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1012 DDLQAEEDKVNTLTKAKIKLEQQVDDL---EGSLEQEKK-IRMDLERAKRKLEGDLKLAQestmdiENDKQQLDEKLKKK 1087
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELkgeIGRLEKELEqAEEELDELQDRLEAAEDLAR------LELRALLEERFAAA 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1088 EFEmsglqskiEDEQALGMQLQKKIKELqarieeleeeieaerasRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEm 1167
Cdd:COG4913 759 LGD--------AVERELRENLEERIDAL-----------------RARLNRAEEELERAMRAFNREWPAETADLDADLE- 812
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115527082 1168 nkkREAEFQKMRRDLEEATL-QHEATAATLRKKHAdsvaelGEQIDNLQrvkQKLEKEKSEMKMEIDDL 1235
Cdd:COG4913 813 ---SLPEYLALLDRLEEDGLpEYEERFKELLNENS------IEFVADLL---SKLRRAIREIKERIDPL 869
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1493-1691 |
3.12e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.09 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1493 EESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKikkqveqEKSELQAALEEAEASLEHEEGKILRIQLELNQv 1572
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-------EVEELEAELEEKDERIERLERELSEARSEERR- 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1573 KSEVDRKIAEKDEEIDQMKrnhiRIVESMQSTLDaEIRSRNDaiRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQA 1652
Cdd:COG2433 460 EIRKDREISRLDREIERLE----RELEEERERIE-ELKRKLE--RLKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYG 532
|
170 180 190
....*....|....*....|....*....|....*....
gi 115527082 1653 ILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEE 1691
Cdd:COG2433 533 LKEGDVVYLRDASGAGRSTAELLAEAGPRAVIVPGELSE 571
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
848-1340 |
3.17e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 848 ETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKI---------- 917
Cdd:pfam05483 276 KTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAahsfvvtefe 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 918 ----QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKV-----EKEKHATENK-VKNLTEEMA 987
Cdd:pfam05483 356 attcSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELkkilaEDEKLLDEKKqFEKIAEELK 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 988 GLDEtiakltkEKKALQEAHQQTLDDLqaeEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLE-GDLKLA 1066
Cdd:pfam05483 436 GKEQ-------ELIFLLQAREKEIHDL---EIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLlENKELT 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1067 QE-STMDIENDKQQLDEKLKKKEFEMsgLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR 1145
Cdd:pfam05483 506 QEaSDMTLELKKHQEDIINCKKQEER--MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVL 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1146 ELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQ-------HEATAATLRKKHADSVAELGEQIDNLQRVK 1218
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAenkqlnaYEIKVNKLELELASAKQKFEEIIDNYQKEI 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1219 QKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCralEDQLSEIKTKEEEQQRLINDLTAQRarlQTESGEYSRQLDEK 1298
Cdd:pfam05483 664 EDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRC---QHKIAEMVALMEKHKHQYDKIIEER---DSELGLYKNKEQEQ 737
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 115527082 1299 DTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSS 1340
Cdd:pfam05483 738 SSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKEN 779
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
872-1094 |
3.33e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 872 AKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKiqlEAKIKEVTERAEDEEEINAELTakkrkleDEC 951
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARK---QNKYDELVEEAKTIKAEIEELT-------DEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 952 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEE-------------MAGLDET---IAKLTKEKKALQEAHQQTLDDLQ 1015
Cdd:PHA02562 244 LNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcptcTQQISEGpdrITKIKDKLKELQHSLEKLDTAID 323
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115527082 1016 AEEDKVNTLTKAKIKLEqqvdDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSGL 1094
Cdd:PHA02562 324 ELEEIMDEFNEQSKKLL----ELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
867-1070 |
3.90e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 867 LAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRK 946
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 947 LEDEcSELK-----KDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKV 1021
Cdd:COG4942 116 LGRQ-PPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 115527082 1022 NTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQEST 1070
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1746-1939 |
3.95e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1746 EDIIQE-----------ARNAEE----KAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAE----- 1805
Cdd:COG1196 192 EDILGElerqleplerqAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEaelee 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1806 -QLALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKR 1884
Cdd:COG1196 272 lRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 115527082 1885 QAEEAEEQSNVNLSKFRRIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1939
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1626-1925 |
4.01e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1626 LNEMEIQLnHANRMAAEALRNYRNTQAILK-------------------DTQLHLDDALRSQEDL---KEQLAMVERRAN 1683
Cdd:PRK04863 232 FQDMEAAL-RENRMTLEAIRVTQSDRDLFKhlitestnyvaadymrhanERRVHLEEALELRRELytsRRQLAAEQYRLV 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1684 LLQAEIEELratleqtERSRKIAEQELLDASERVQLLhtqNTSLINTKKkletdISQIQGEMEDIiqEARNAEekAKKAI 1763
Cdd:PRK04863 311 EMARELAEL-------NEAESDLEQDYQAASDHLNLV---QTALRQQEK-----IERYQADLEEL--EERLEE--QNEVV 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1764 TDAAMMAEELkKEQDTSAHLE--RMKKNLE--QTVKDLQHR-----------LDEAEQ------LALKGGKKQIQKLEAR 1822
Cdd:PRK04863 372 EEADEQQEEN-EARAEAAEEEvdELKSQLAdyQQALDVQQTraiqyqqavqaLERAKQlcglpdLTADNAEDWLEEFQAK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1823 VRELEGEV-ESEQKRNV---------EAVKGLRK---------HERKVKELTYQTEEDRKNILRLQDLVDKLQA------ 1877
Cdd:PRK04863 451 EQEATEELlSLEQKLSVaqaahsqfeQAYQLVRKiagevsrseAWDVARELLRRLREQRHLAEQLQQLRMRLSEleqrlr 530
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 115527082 1878 KVKSYKRQAEEAEEQSNVNLSKFRRIQHELEEAEERADIAESQVNKLR 1925
Cdd:PRK04863 531 QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1352-1522 |
4.13e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1352 EEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVED 1431
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1432 lmidvertnaacaaLDKKQRNFDKILAEWKQKCEE----THAE-----LEASQKESRSLSTELfkIKNAYEESldQLETL 1502
Cdd:PRK12704 126 --------------LEKKEEELEELIEEQLQELERisglTAEEakeilLEKVEEEARHEAAVL--IKEIEEEA--KEEAD 187
|
170 180
....*....|....*....|.
gi 115527082 1503 KRENKNLQQEISDL-TEQIAE 1522
Cdd:PRK12704 188 KKAKEILAQAIQRCaADHVAE 208
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1267-1582 |
4.46e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.61 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1267 EEEQQRLIND-----------LTAQRARLQTESgeysRQLDEKDTlvSQLSRGKQAFTQQIEELKRQLEEEIKAKsalah 1335
Cdd:pfam00038 2 EKEQLQELNDrlasyidkvrfLEQQNKLLETKI----SELRQKKG--AEPSRLYSLYEKEIEDLRRQLDTLTVER----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1336 alqssrhdcdllreqyeeeqeAKAELQRamSKANSEVAQWRTKYETDAIQRTeELEEAKKKLAQRLQDA-------EEHV 1408
Cdd:pfam00038 71 ---------------------ARLQLEL--DNLRLAAEDFRQKYEDELNLRT-SAENDLVGLRKDLDEAtlarvdlEAKI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1409 EAVNAKCASLEKTKQ----RLQNEVEDLMIDVERTNAACAALdkkqrnfDKILAEWKqkceethAELEASQKESRSLSTE 1484
Cdd:pfam00038 127 ESLKEELAFLKKNHEeevrELQAQVSDTQVNVEMDAARKLDL-------TSALAEIR-------AQYEEIAAKNREEAEE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1485 LFKIKnaYEESLDQLETLKRENKNLQQEISDLTEQIAEggkRIHELEKIKKQveqeKSELQAALEEAEASLEHE----EG 1560
Cdd:pfam00038 193 WYQSK--LEELQQAAARNGDALRSAKEEITELRRTIQS---LEIELQSLKKQ----KASLERQLAETEERYELQladyQE 263
|
330 340
....*....|....*....|..
gi 115527082 1561 KILRIQLELNQVKSEVDRKIAE 1582
Cdd:pfam00038 264 LISELEAELQETRQEMARQLRE 285
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1132-1334 |
4.50e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1132 SRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAEFQKMRRDLEEATLQHEATAATLRKKHADsVAELGEQI 1211
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAA--------------QAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1212 DNLQrvkQKLEKEKSEMKM----------------------EIDDLASNMETVSKAKGN-------LEKMCRALEDQLSE 1262
Cdd:COG3883 75 AEAE---AEIEERREELGEraralyrsggsvsyldvllgseSFSDFLDRLSALSKIADAdadlleeLKADKAELEAKKAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115527082 1263 IKTKEEEQQRLINDLTAQRARLQTesgeysrQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALA 1334
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEA-------QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1640-1840 |
4.54e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1640 AAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERV-- 1717
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELge 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1718 QLLHTQNTSLINTK-------KKLETDISQIQGeMEDIIQEARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNL 1790
Cdd:COG3883 91 RARALYRSGGSVSYldvllgsESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 115527082 1791 EQTVKDLQHRLDEAEQLaLKGGKKQIQKLEARVRELEGEVESEQKRNVEA 1840
Cdd:COG3883 167 EAAKAELEAQQAEQEAL-LAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
938-1164 |
4.54e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 938 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAE 1017
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1018 EDKVNTLTkakIKLE--------QQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKkef 1089
Cdd:COG3883 99 GGSVSYLD---VLLGsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE--- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115527082 1090 emsgLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQ 1164
Cdd:COG3883 173 ----LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
892-1103 |
4.95e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 48.31 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 892 QLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAeltakkRKLEDECSELKKDIDDLELTLAKVEKE 971
Cdd:PLN03229 536 KLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKEKMEA------LKAEVASSGASSGDELDDDLKEKVEKM 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 972 KHATENKVKNLTEEMaGLDETIAKltkeKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKkirmd 1051
Cdd:PLN03229 610 KKEIELELAGVLKSM-GLEVIGVT----KKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSKIELLK----- 679
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 115527082 1052 LERAKRKLEGDLKLAQEstmdIENDKQQLDEKLKKKeFEMSGLQSKIEDEQA 1103
Cdd:PLN03229 680 LEVAKASKTPDVTEKEK----IEALEQQIKQKIAEA-LNSSELKEKFEELEA 726
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
839-1259 |
5.05e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 839 KIKPLLKSAETEKEMANMKEEFEKTKEELAKTEAKRKELEEKmvtlMQEKNDLQLQVQAEADSLADAEERCDQLIK-TKI 917
Cdd:COG4717 113 ELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEqLSL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 918 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTE----EMAGLDETI 993
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaallALLGLGGSL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 994 AKLTKEKKALQEAHQQTLDDLqaeedkVNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDI 1073
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALL------FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1074 ENDKQQLDEKLKKKEfemsglqskIEDEQALGMQLQKKIKELqarIEELEEEIEAERASRAKAEKQRSDLSRELEEISER 1153
Cdd:COG4717 343 LDRIEELQELLREAE---------ELEEELQLEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1154 LEEAGGATSAQIEMNKKR--EAEFQKMRRDLEEATLQHEAtaatLRKKHADSVAELG--EQIDNLQRVKQKLEKEKSEMK 1229
Cdd:COG4717 411 LEELLGELEELLEALDEEelEEELEELEEELEELEEELEE----LREELAELEAELEqlEEDGELAELLQELEELKAELR 486
|
410 420 430
....*....|....*....|....*....|
gi 115527082 1230 MEIDDLASNMetvsKAKGNLEKMCRALEDQ 1259
Cdd:COG4717 487 ELAEEWAALK----LALELLEEAREEYREE 512
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1389-1935 |
5.16e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1389 ELEEAKKKLAQ---RLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQ--K 1463
Cdd:PRK01156 198 ELENIKKQIADdekSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYykE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1464 CEETHAELEASQK-ESRSLSTELFKIKNayeesldQLETLKRENKNLQQEISDLTEQIaeggKRIHELEKIKKQVEQEKS 1542
Cdd:PRK01156 278 LEERHMKIINDPVyKNRNYINDYFKYKN-------DIENKKQILSNIDAEINKYHAII----KKLSVLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1543 ELQAaLEEAEASLEHEEGKILRIQLELNQVKsevdRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKM 1622
Cdd:PRK01156 347 RYDD-LNNQILELEGYEMDYNSYLKSIESLK----KKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1623 EGDLNemeiQLNHANRMAAEALRNYRNTQAILKD--------TQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELra 1694
Cdd:PRK01156 422 SSKVS----SLNQRIRALRENLDELSRNMEMLNGqsvcpvcgTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDI-- 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1695 tleqTERSRKIAEQELLDASERVQllhtqntSLINTKKKLETDISQIQGEMEDIiQEARNAEEKAKKAITDAAMMAEELK 1774
Cdd:PRK01156 496 ----DEKIVDLKKRKEYLESEEIN-------KSINEYNKIESARADLEDIKIKI-NELKDKHDKYEEIKNRYKSLKLEDL 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1775 KEQDTSaHLERMKKNLEQTVKDLQHRLDEAeqlalkggKKQIQKLEARVRELEGEVESEQKRNveaVKGLRKHERKVKEL 1854
Cdd:PRK01156 564 DSKRTS-WLNALAVISLIDIETNRSRSNEI--------KKQLNDLESRLQEIEIGFPDDKSYI---DKSIREIENEANNL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1855 TYQTEEdrknILRLQDLVDKLQAKVKSYKRQAEEAEE----QSNVNlSKFRRIQHELEEAEERADIAESQVNKLRVKSRE 1930
Cdd:PRK01156 632 NNKYNE----IQENKILIEKLRGKIDNYKKQIAEIDSiipdLKEIT-SRINDIEDNLKKSRKALDDAKANRARLESTIEI 706
|
....*
gi 115527082 1931 VHTKI 1935
Cdd:PRK01156 707 LRTRI 711
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1462-1914 |
5.85e-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: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1462 QKCEETHAELEASQKESRSLSTELFKIKNAyEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEK 1541
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLREALQQTQQS-HAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1542 SELQAALEEAeaSLEHEEGKILRIQLELnQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDA-----I 1616
Cdd:TIGR00618 291 KAAPLAAHIK--AVTQIEQQAQRIHTEL-QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHevatsI 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1617 RLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATL 1696
Cdd:TIGR00618 368 REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1697 EQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKlETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKE 1776
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ-ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPL 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1777 QDTSAHLERMKKNLEQTVKDLQHRLDEAeqlalkggKKQIQKLEARVRELEGEveseqkrnveavkgLRKHERKVKELTY 1856
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTSE--------RKQRASLKEQMQEIQQS--------------FSILTQCDNRSKE 584
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 115527082 1857 QTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNVNLSKFRRIQHELEEAEERA 1914
Cdd:TIGR00618 585 DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA 642
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1494-1743 |
8.77e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1494 ESLDQLETLKRENKNLQQEISDLTEQIAEGGKrihELEKIKKQVEQEKSE---------LQAALEEAEASLEheegkilR 1564
Cdd:PRK11281 70 ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQA---ELEALKDDNDEETREtlstlslrqLESRLAQTLDQLQ-------N 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1565 IQLELNQVKSEVdrkiaekdeeIDQMKRNhirivESMQSTLDAEIrSRNDAIRLKKKmEGDLNEMEIQLNHANRMAAE-- 1642
Cdd:PRK11281 140 AQNDLAEYNSQL----------VSLQTQP-----ERAQAALYANS-QRLQQIRNLLK-GGKVGGKALRPSQRVLLQAEqa 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1643 --ALRNYRNTQAILKDTQLHldDALRSQEDLK-EQLAMVERRANLLQAEIEELR-----ATLEQTERSRKIAE------- 1707
Cdd:PRK11281 203 llNAQNDLQRKSLEGNTQLQ--DLLQKQRDYLtARIQRLEHQLQLLQEAINSKRltlseKTVQEAQSQDEAARiqanplv 280
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 115527082 1708 -----------QELLDASERVQLLHTQN-------TSLINTKKKLETDISQIQG 1743
Cdd:PRK11281 281 aqeleinlqlsQRLLKATEKLNTLTQQNlrvknwlDRLTQSERNIKEQISVLKG 334
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1193-1554 |
8.99e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1193 AATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQR 1272
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1273 LINDLTAQRARLQTESGEYS---RQLDEKDTLVSQLSRGKQA----FTQQIEELKRQLEEEIKAKSALAHALQSSRHDCD 1345
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEariRELEEDIKTLTQRVLERETelerMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1346 LLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETdAIQRTEELEEAKKKLA---QRLQDAEEHVEAVNAKCASLEKTK 1422
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT-AHRKEAENEALLEELRslqERLNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1423 QRLQNEVEDLMIDVERTNAACAALDKKQRNFDkilAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEE-------- 1494
Cdd:pfam07888 268 DRTQAELHQARLQAAQLTLQLADASLALREGR---ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEermerekl 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115527082 1495 ----------SLDQLETLKRENKNL-------QQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEAS 1554
Cdd:pfam07888 345 evelgrekdcNRVQLSESRRELQELkaslrvaQKEKEQLQAEKQELLEYIRQLEQRLETVADAKWSEAALTSTERPD 421
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1669-1925 |
9.54e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1669 EDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQllhTQNTSLINTKKKLETDISQIQGEMEDI 1748
Cdd:pfam07888 16 EEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYK---RDREQWERQRRELESRVAELKEELRQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1749 IQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEqLALKGGKKQIQKLEARVRELEG 1828
Cdd:pfam07888 93 REKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE-TELERMKERAKKAGAQRKEEEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1829 EVESEQKRNVEAVKGLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNvnlskfrriqhELE 1908
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE-----------ELR 240
|
250
....*....|....*..
gi 115527082 1909 EAEERADIAESQVNKLR 1925
Cdd:pfam07888 241 SLQERLNASERKVEGLG 257
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
879-1092 |
9.85e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.59 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 879 EKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKI-------QLEAKIKEVTERAEDEEEINAELTAKKRKLEDEC 951
Cdd:PLN02939 156 EDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIhveileeQLEKLRNELLIRGATEGLCVHSLSKELDVLKEEN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 952 SELKKDIDDLELTLAKVEKekhaTENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQtLDDLQAEE--DKVNTLT---- 1025
Cdd:PLN02939 236 MLLKDDIQFLKAELIEVAE----TEERVFKLEKERSLLDASLRELESKFIVAQEDVSK-LSPLQYDCwwEKVENLQdlld 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1026 -------KAKIKLEQ------QVDDLEGSLEQ--------------EKKIRM---DLERAKRKLEGDLKLAQESTMDIEN 1075
Cdd:PLN02939 311 ratnqveKAALVLDQnqdlrdKVDKLEASLKEanvskfssykvellQQKLKLleeRLQASDHEIHSYIQLYQESIKEFQD 390
|
250
....*....|....*..
gi 115527082 1076 DKQQLDEKLKKKEFEMS 1092
Cdd:PLN02939 391 TLSKLKEESKKRSLEHP 407
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1489-1939 |
9.88e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1489 KNAYEESLDQLETLKRENKNLQQEISDLTEQIAEggkRIHELEKIKKQVEQEKselqaaLEEAEASLEHEEGKILRIQLE 1568
Cdd:COG5278 85 RAEIDELLAELRSLTADNPEQQARLDELEALIDQ---WLAELEQVIALRRAGG------LEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1569 LNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYR 1648
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1649 NTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLI 1728
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1729 NTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLA 1808
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1809 LKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEE 1888
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 115527082 1889 AEEQSNVNLSKFRRIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1939
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1303-1542 |
1.02e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1303 SQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRtkyetd 1382
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1383 aiqrtEELEEAKKKLAQRLQDAEEHVEAVNAKCAslekTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQ 1462
Cdd:COG4942 97 -----AELEAQKEELAELLRALYRLGRQPPLALL----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1463 KCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLEtlkRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKS 1542
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
929-1061 |
1.10e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 46.59 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 929 RAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETI-AKLTKEKKALQEAH 1007
Cdd:cd22656 101 DDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALkDLLTDEGGAIARKE 180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 115527082 1008 qqtLDDLQAEEDKVNT----LTKAKI-KLEQQVDDLEGSLEQEKKIRMDLERAKRKLEG 1061
Cdd:cd22656 181 ---IKDLQKELEKLNEeyaaKLKAKIdELKALIADDEAKLAAALRLIADLTAADTDLDN 236
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1262-1587 |
1.10e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 47.26 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1262 EIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIkakSALAHALQSSR 1341
Cdd:COG5185 226 KEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQF---ENTKEKIAEYT 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1342 HDCDLLREQYEEEQEAKAelqramSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCAsLEKT 1421
Cdd:COG5185 303 KSIDIKKATESLEEQLAA------AEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE-LSKS 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1422 KQRLQNEVEDLMIDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLET 1501
Cdd:COG5185 376 SEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1502 LKRENKNLQQEiSDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKIlrIQLELNQVKSEVDRKIA 1581
Cdd:COG5185 456 EADEESQSRLE-EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGV--RSKLDQVAESLKDFMRA 532
|
....*.
gi 115527082 1582 EKDEEI 1587
Cdd:COG5185 533 RGYAHI 538
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1526-1760 |
1.11e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1526 RIHELEKIKKQVEQEKSELQAALEEAEASLEH--EEGKILRIQLELNQV---KSEVDRKIAEKDEEIDQMKRNHIRIVES 1600
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLlqqLSELESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1601 MQSTLDAEIRSRNDAIRlkKKMEGDLNEMEIQLnhanrmaAEALRNYRNTQAILKDTQLHLDDALRS-QEDLKEQLAMVE 1679
Cdd:COG3206 249 LGSGPDALPELLQSPVI--QQLRAQLAELEAEL-------AELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1680 RRANLLQAEIEELRATLEQTERSRKI---AEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEdIIQEARNAE 1756
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR-VIDPAVVPL 398
|
....
gi 115527082 1757 EKAK 1760
Cdd:COG3206 399 KPVS 402
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1757-1929 |
1.20e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1757 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLalkggkKQIQKLEARVRELEGEVESEQKR 1836
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1837 nveaVKGLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQA-EEAEEQSNVNLSKFRRIQHELEEAEERAD 1915
Cdd:COG4717 148 ----LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....
gi 115527082 1916 IAESQVNKLRVKSR 1929
Cdd:COG4717 224 ELEEELEQLENELE 237
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1455-1939 |
1.27e-04 |
|
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: 47.35 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1455 KILAEWKQKCEETHAELEASQKESRSLStelfKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIK 1534
Cdd:TIGR00606 210 KYLKQYKEKACEIRDQITSKEAQLESSR----EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1535 KQVEQEKSELQAALEEAEASLEHEEG--------KILRIQLE----------LNQVKSEVDRKIAEKDEEIDQ-----MK 1591
Cdd:TIGR00606 286 SELELKMEKVFQGTDEQLNDLYHNHQrtvrekerELVDCQREleklnkerrlLNQEKTELLVEQGRLQLQADRhqehiRA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1592 RNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDL 1671
Cdd:TIGR00606 366 RDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELK 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1672 KEQLAMVERRANLLQAEIEELRAT----LEQTERSRKiAEQELLDASE---------RVQLLHTQNTSLINTKKKLETDI 1738
Cdd:TIGR00606 446 KEILEKKQEELKFVIKELQQLEGSsdriLELDQELRK-AERELSKAEKnsltetlkkEVKSLQNEKADLDRKLRKLDQEM 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1739 SQIQGEMEDIIQEARNAEEKAKK-------------AITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAE 1805
Cdd:TIGR00606 525 EQLNHHTTTRTQMEMLTKDKMDKdeqirkiksrhsdELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1806 QLA------LKGGKKQIQKLEARVRELEG--EVESEQKRNVEAVKGLRK-----------HERKVKELTYQT-------E 1859
Cdd:TIGR00606 605 QNKnhinneLESKEEQLSSYEDKLFDVCGsqDEESDLERLKEEIEKSSKqramlagatavYSQFITQLTDENqsccpvcQ 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1860 EDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNVNLSKFRRIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1939
Cdd:TIGR00606 685 RVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1296-1559 |
1.33e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1296 DEKDTLVSQLsRGKQAFtqQIEELKRQLEEEiKAKSALAHALQSSRHdCDLLREQYEEEQEAKAELQRamskansevaqw 1375
Cdd:PRK05771 16 SYKDEVLEAL-HELGVV--HIEDLKEELSNE-RLRKLRSLLTKLSEA-LDKLRSYLPKLNPLREEKKK------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1376 rtkyetdaiQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLM------IDV------ERTNAAC 1443
Cdd:PRK05771 79 ---------VSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdLDLslllgfKYVSVFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1444 AALDKKQrnfdkiLAEWKQKCEETHAELEASQKESRSLSteLFKIKNAYEESLDQLETLKRENKNL------QQEISDLT 1517
Cdd:PRK05771 150 GTVPEDK------LEELKLESDVENVEYISTDKGYVYVV--VVVLKELSDEVEEELKKLGFERLELeeegtpSELIREIK 221
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 115527082 1518 EQIAEGGKRIHEL-EKIKKQVEQEKSELQAALEEAEASLEHEE 1559
Cdd:PRK05771 222 EELEEIEKERESLlEELKELAKKYLEELLALYEYLEIELERAE 264
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1300-1582 |
1.40e-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: 46.93 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1300 TLVSQLSRGKQAFTQQIEELKRQLEEEI--KAKSALAHALQSSRHDCDLLREQYEE------EQEAKAELQRAMSKANSE 1371
Cdd:NF033838 88 ALNKKLSDIKTEYLYELNVLKEKSEAELtsKTKKELDAAFEQFKKDTLEPGKKVAEatkkveEAEKKAKDQKEEDRRNYP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1372 VAQWRT----KYETDAIQRTEELEEAKKKlAQRLQDaEEHVEAVNAKCASLEKTKQRLQNevedlmIDVERTNAAcaalD 1447
Cdd:NF033838 168 TNTYKTleleIAESDVEVKKAELELVKEE-AKEPRD-EEKIKQAKAKVESKKAEATRLEK------IKTDREKAE----E 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1448 KKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELF---KIKNAYEESLDQL--ETLKRENKNLQQEISDLTEQIAE 1522
Cdd:NF033838 236 EAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPAtpdKKENDAKSSDSSVgeETLPSPSLKPEKKVAEAEKKVEE 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115527082 1523 GGKRIHELEK---------IKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAE 1582
Cdd:NF033838 316 AKKKAKDQKEedrrnyptnTYKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAE 384
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
893-1017 |
1.46e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 893 LQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEI---NAELTAKKRKLEDECSELKKDIDDLELTLAKVE 969
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELrerRNELQKLEKRLLQKEENLDRKLELLEKREEELE 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 115527082 970 KEKHATENKVKNLTEEMAGLD----------ETIAKLTKEkkalqEAHQQTLDDLQAE 1017
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEelieeqlqelERISGLTAE-----EAKEILLEKVEEE 166
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1453-1625 |
1.48e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1453 FDKILAEWKQKCEETHAE--LEASQKESRSLSTElfKIKNAYEESLDQLETLKRENKnlqqeisdlteqiaeggKRIHEL 1530
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKriLEEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELR-----------------ERRNEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1531 EKIKKQVEQEKSEL---QAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKD---EEIDQMKRNHIR--IVESMQ 1602
Cdd:PRK12704 85 QKLEKRLLQKEENLdrkLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLqelERISGLTAEEAKeiLLEKVE 164
|
170 180
....*....|....*....|...
gi 115527082 1603 STLDAEIRSRNDAIRLKKKMEGD 1625
Cdd:PRK12704 165 EEARHEAAVLIKEIEEEAKEEAD 187
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1737-1935 |
1.62e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1737 DISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEqlalkggkKQI 1816
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE--------KEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1817 QKLEARVRELEGEVES------------------EQKRNVEAVKGLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAK 1878
Cdd:COG4942 93 AELRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 115527082 1879 VKSYKRQAEEAEEQSNVNLSKFRRIQHELEEAEERADIAESQVNKLRVKSREVHTKI 1935
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1406-1712 |
1.75e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1406 EHVEAVNAKCAS--LEKTKQ-RLQNEVEDLMIDVERTNAACAALDKKQRNFDK---ILAEWKQKCEETHAELEASQKESR 1479
Cdd:pfam17380 279 QHQKAVSERQQQekFEKMEQeRLRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1480 slstelfkiknayeesldqletlKRENKNLQQEisdlteQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEE 1559
Cdd:pfam17380 359 -----------------------KRELERIRQE------EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1560 gkilriqlelnqvksEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAIRLKkkmegdlnEMEIQlnhanrm 1639
Cdd:pfam17380 410 ---------------ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE--------EQERQ------- 459
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115527082 1640 aaEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQlamverRANLLQAEIEELRATLEQTERSRKIAEQELLD 1712
Cdd:pfam17380 460 --QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ------RRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1355-1554 |
1.76e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1355 QEAKAELQRAMSKANSEVAQWRTKYE-TDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLM 1433
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGlVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1434 idverTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLD-QLETLKRENKNLQQE 1512
Cdd:COG3206 261 -----QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEaELEALQAREASLQAQ 335
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 115527082 1513 ISDLTEQIAEGGKRIHELEKIKKQVEQEKS---ELQAALEEAEAS 1554
Cdd:COG3206 336 LAQLEARLAELPELEAELRRLEREVEVARElyeSLLQRLEEARLA 380
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1661-1939 |
1.86e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1661 LDDALRSQEDLKEQLAMVER-----RANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLlHTQNTSLINTkkkLE 1735
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEADEVLEE-HEERREELET---LE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1736 TDISqiqgEMEDIIQEARNAEEKAKKAITDAAMMAEELKKEqdtsahlermkknLEQTVKDLQhrLDEAEQLALKGGKKQ 1815
Cdd:PRK02224 258 AEIE----DLRETIAETEREREELAEEVRDLRERLEELEEE-------------RDDLLAEAG--LDDADAEAVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1816 IQKLEARVRELEGEVESEQKRNVEAVKGLRKherKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNV 1895
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLRE---DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 115527082 1896 NLSKFRRIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE 1939
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1035-1452 |
1.87e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1035 VDDLEGSLeqeKKIRMDLE--RAKRKLEGDLK-LAQEST-------MDIENDKQQLDEKLKKKEFEMSGLQSKIEDEQAL 1104
Cdd:PRK04863 232 FQDMEAAL---RENRMTLEaiRVTQSDRDLFKhLITESTnyvaadyMRHANERRVHLEEALELRRELYTSRRQLAAEQYR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1105 GMQLQKKIKELQARIEELEEEIEAERASRAK---AEKQRSDLSR---ELEEISERLEEAGGATSAQIEMNKKREAEFqkm 1178
Cdd:PRK04863 309 LVEMARELAELNEAESDLEQDYQAASDHLNLvqtALRQQEKIERyqaDLEELEERLEEQNEVVEEADEQQEENEARA--- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1179 rrdlEEATLQHEATAATLrkkhADSVAELGEQ---IDNLQRVKQKLEKEKS---EMKMEIDDLASNMET-VSKAKGNLEK 1251
Cdd:PRK04863 386 ----EAAEEEVDELKSQL----ADYQQALDVQqtrAIQYQQAVQALERAKQlcgLPDLTADNAEDWLEEfQAKEQEATEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1252 McRALEDQLS---EIKTKEEEQQRLINDLTAQ--RARLQTESGEYSRQLDEKDTLVSQLsrgkQAFTQQIEELKRQLEEE 1326
Cdd:PRK04863 458 L-LSLEQKLSvaqAAHSQFEQAYQLVRKIAGEvsRSEAWDVARELLRRLREQRHLAEQL----QQLRMRLSELEQRLRQQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1327 IKAKSALAHALQSSRHDCDlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYEtdaiQRTEELEEAKKKLAQR------ 1400
Cdd:PRK04863 533 QRAERLLAEFCKRLGKNLD-DEDELEQLQEELEARLESLSESVSEARERRMALR----QQLEQLQARIQRLAARapawla 607
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 115527082 1401 LQDA----EEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRN 1452
Cdd:PRK04863 608 AQDAlarlREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1222-1374 |
1.87e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1222 EKEKSEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSeikTKEEEQQRL---INDLTAQRARLQTESGEYSRQLDEK 1298
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLS---AAEAERSRLqalLAELAGAGAAAEGRAGELAQELDSE 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115527082 1299 DTLVSQLSRGKQAFTQQIEELKRQLeeeikakSALAHALQSSRhdcdllreqyEEEQEAKAELQRAMSKANSEVAQ 1374
Cdd:PRK09039 129 KQVSARALAQVELLNQQIAALRRQL-------AALEAALDASE----------KRDRESQAKIADLGRRLNVALAQ 187
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1454-1619 |
1.92e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1454 DKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEIS-------DLTEQIAE---- 1522
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAeaeaeieERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1523 ----GG------------------KRIHELEKI----KKQVEQEKsELQAALEEAEASLEHEEGKILRIQLELNQVKSEV 1576
Cdd:COG3883 95 lyrsGGsvsyldvllgsesfsdflDRLSALSKIadadADLLEELK-ADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 115527082 1577 DRKIAEKDEEIDQMKRNhIRIVESMQSTLDAEIRSRNDAIRLK 1619
Cdd:COG3883 174 EAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1388-1775 |
2.03e-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: 46.17 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1388 EELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKqrlqNEVEDLMIDVERtnaacAALDKKQRNFDKILAewKQKCEET 1467
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTK----RLIEELKLNLER-----AQTEEAQAKQDSELA--KLRVEEM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1468 haELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKR----IHELEKIKKQVEQEKSE 1543
Cdd:pfam05701 111 --EQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRaeeaVSASKEIEKTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1544 LQAALEEAE----ASLEHEEGKIlRIQLELNQVKSEVDRKIAEKDEEIDQMkRNHIRIVESMQSTLDAeirsrndAIRLK 1619
Cdd:pfam05701 189 LIATKESLEsahaAHLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-------ASALL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1620 KKMEGDLNE-MEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELR---AT 1695
Cdd:pfam05701 260 LDLKAELAAyMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAASLRSELEKEKaelAS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1696 LEQTERSRKIAEQELLDASERVQllhtqntSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKaitdAAMMA-EELK 1774
Cdd:pfam05701 340 LRQREGMASIAVSSLEAELNRTK-------SEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKS----LAQAArEELR 408
|
.
gi 115527082 1775 K 1775
Cdd:pfam05701 409 K 409
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
867-1088 |
2.17e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 867 LAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTER----AEDEEEINAELTA 942
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaelEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 943 KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTlddlqaeEDKVN 1022
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL-------EAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115527082 1023 TLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKE 1088
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1173-1330 |
2.41e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1173 AEFQKMRRDLEEATLQHEATAATLRKKhadsVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAK------ 1246
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEAR----LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1247 ---GNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKdtlVSQLSRGKQAFTQQIEELKRQL 1323
Cdd:COG1579 96 keiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEAEREELAAKI 172
|
....*..
gi 115527082 1324 EEEIKAK 1330
Cdd:COG1579 173 PPELLAL 179
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
885-1063 |
2.48e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 885 MQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELT 964
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 965 LAKVEKEKHatenkVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQ 1044
Cdd:COG1579 82 LGNVRNNKE-----YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170 180
....*....|....*....|
gi 115527082 1045 E-KKIRMDLERAKRKLEGDL 1063
Cdd:COG1579 157 ElEELEAEREELAAKIPPEL 176
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1311-1723 |
2.56e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1311 AFTQQIEELKRQLEEEIKAKSALAHAlqssrhdcdllREQYEEEQEAKAELQRAMskansevaqwrtkyetdaiqrtEEL 1390
Cdd:PRK04863 273 DYMRHANERRVHLEEALELRRELYTS-----------RRQLAAEQYRLVEMAREL----------------------AEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1391 EEAKKKLAQRLQDAEEHVEAVNAKCASLEKTkQRLQNEVEDLMIDVERTNAACAALDKKQrnfdkilaewkqkcEETHAE 1470
Cdd:PRK04863 320 NEAESDLEQDYQAASDHLNLVQTALRQQEKI-ERYQADLEELEERLEEQNEVVEEADEQQ--------------EENEAR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1471 LEASQKESRSLSTELFKiknaYEESLDQLETLKRENKNLQQ---------EISDLTEQIAEGgkRIHELEKIKKQVEQEK 1541
Cdd:PRK04863 385 AEAAEEEVDELKSQLAD----YQQALDVQQTRAIQYQQAVQalerakqlcGLPDLTADNAED--WLEEFQAKEQEATEEL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1542 SELQAALEEAEASLE-HEEGKILriqleLNQVKSEVDRKIAEkdeeidqmkrnhirivESMQSTLDAEIRSRNDAIRLKK 1620
Cdd:PRK04863 459 LSLEQKLSVAQAAHSqFEQAYQL-----VRKIAGEVSRSEAW----------------DVARELLRRLREQRHLAEQLQQ 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1621 kMEGDLNEMEIQLNH---ANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRAtle 1697
Cdd:PRK04863 518 -LRMRLSELEQRLRQqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA--- 593
|
410 420
....*....|....*....|....*.
gi 115527082 1698 QTERSRKIAeQELLDASERVQLLHTQ 1723
Cdd:PRK04863 594 RIQRLAARA-PAWLAAQDALARLREQ 618
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
806-1912 |
2.92e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 46.36 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 806 QKMVERRESIFCIQYNVRAfMNVKHWPWMKLYFKIKPLLKSAETEKEMANMKeefektKEELAKTEAKRKELEEKMVTLM 885
Cdd:PTZ00440 316 KKIEKGKEYIKRIQNNNIP-PQVKKDELKKKYFESAKHYASFKFSLEMLSML------DSLLIKKEKILNNLFNKLFGDL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 886 QEKndlqlqvqaeADSLADAEercdQLIKTKIQLEAKIKEVTERAEDEEEINAELTAK-KRKLEDECSELKKDIDDLELT 964
Cdd:PTZ00440 389 KEK----------IETLLDSE----YFISKYTNIISLSEHTLKAAEDVLKENSQKIADyALYSNLEIIEIKKKYDEKINE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 965 LAKvekekhaTENKVKNLTEEMAGLDETIaklTKEKKALQEAHQQTLDDLQAEEdKVNTLTKAKIKLEQQVDDLEGSLEQ 1044
Cdd:PTZ00440 455 LKK-------SINQLKTLISIMKSFYDLI---ISEKDSMDSKEKKESSDSNYQE-KVDELLQIINSIKEKNNIVNNNFKN 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1045 EKKIRMDLERAKRKLEGDLKLaqestmdIENDKQQLdEKLKKKEFEMSGLQSKIEDEQALGMQLQKKIKELQARIEELEE 1124
Cdd:PTZ00440 524 IEDYYITIEGLKNEIEGLIEL-------IKYYLQSI-ETLIKDEKLKRSMKNDIKNKIKYIEENVDHIKDIISLNDEIDN 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1125 EIEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqieMNKKREAEFQKMRRDLEEATLQHEATAatlrkKHADSV 1204
Cdd:PTZ00440 596 IIQQIEELINEALFNKEKFINEKNDLQEKVKYI---------LNKFYKGDLQELLDELSHFLDDHKYLY-----HEAKSK 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1205 AELGEQIDNLQRVKQKLEKEKSEmkmEIDDLASNMETVSKAKGNLEKmcRALEDQLSEIKTkeeEQQRLINDLTAQRARL 1284
Cdd:PTZ00440 662 EDLQTLLNTSKNEYEKLEFMKSD---NIDNIIKNLKKELQNLLSLKE--NIIKKQLNNIEQ---DISNSLNQYTIKYNDL 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1285 QTESGEYSRQLDEKDTLVSQLSRGKQAFtqqIEELKRQLEEEIKAKSalahalqssrhdcdlLREQYEEEQEAKAELQRA 1364
Cdd:PTZ00440 734 KSSIEEYKEEEEKLEVYKHQIINRKNEF---ILHLYENDKDLPDGKN---------------TYEEFLQYKDTILNKENK 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1365 MS------KANSEVAQWRTKYETDAIQRTE-ELEEAKKKLAQRLQDAEEHVEavNAKCASLEKTKQRLQNEVEDLMIDVE 1437
Cdd:PTZ00440 796 ISndinilKENKKNNQDLLNSYNILIQKLEaHTEKNDEELKQLLQKFPTEDE--NLNLKELEKEFNENNQIVDNIIKDIE 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1438 RTNAACAALdkKQRNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKN--AYEESLDQLETLKRENKNLQQEISD 1515
Cdd:PTZ00440 874 NMNKNINII--KTLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINTDNiiQKNEKLNLLNNLNKEKEKIEKQLSD 951
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1516 ltEQIAEGGKRIHE-LEKIKKQVEQEKSELQAALEEAEA---SLEHEEGKILRIQLE-----------LNQVKSEV---- 1576
Cdd:PTZ00440 952 --TKINNLKMQIEKtLEYYDKSKENINGNDGTHLEKLDKekdEWEHFKSEIDKLNVNynilnkkiddlIKKQHDDIieli 1029
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1577 DRKIAEKDEEIDQMKRNHIRIVESMQSTL-----------DAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALR 1645
Cdd:PTZ00440 1030 DKLIKEKGKEIEEKVDQYISLLEKMKTKLssfhfnidikkYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHE 1109
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1646 NYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANllqaEIEELRATLEQTERSRKIAEQELLDasERVQLLHTQNT 1725
Cdd:PTZ00440 1110 HVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELE----NMNLEDITLNEVNEIEIEYERILID--HIVEQINNEAK 1183
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1726 SLINTKKKLETDISQIQGEMEDIIQEARN-AEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQhRLDEA 1804
Cdd:PTZ00440 1184 KSKTIMEEIESYKKDIDQVKKNMSKERNDhLTTFEYNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELK-EIKLQ 1262
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1805 EQLALKGGKKQIQKLEARVRELEGEVESEQKRNVEAV-KGLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYK 1883
Cdd:PTZ00440 1263 VFSYLQQVIKENNKMENALHEIKNMYEFLISIDSEKIlKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAKEHK 1342
|
1130 1140 1150
....*....|....*....|....*....|.
gi 115527082 1884 RQAEEAEE--QSNVNLSKFRRIQHELEEAEE 1912
Cdd:PTZ00440 1343 NKIYGSLEdkQIDDEIKKIEQIKEEISNKRK 1373
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1257-1451 |
2.98e-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: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1257 EDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSALAHA 1336
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1337 LQSSRHDCDLLR--------EQYEEEQEAKAELQRAMSKANSEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQDAEEHV 1408
Cdd:COG3883 95 LYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELE----AKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 115527082 1409 EAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQR 1451
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1686-1913 |
3.03e-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: 45.89 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1686 QAEIEELRATLEQTERSRKiaEQELLDASERVQLLHTQNTSlintKKKLETDISQIQgEMEDIIQEARNAEEKAKKAITD 1765
Cdd:pfam05557 1 RAELIESKARLSQLQNEKK--QMELEHKRARIELEKKASAL----KRQLDRESDRNQ-ELQKRIRLLEKREAEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1766 AAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRL-DEAEQLalkggKKQIQKLEARVRELEGEVESEQKRNVEAVKGL 1844
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSEL-----RRQIQRAELELQSTNSELEELQERLDLLKAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115527082 1845 RKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVksykrQAEEAEEQSNVNLSKFRRIQHELEEAEER 1913
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQE-----QDSEIVKNSKSELARIPELEKELERLREH 212
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
1147-1365 |
3.81e-04 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 45.34 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1147 LEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLrkKHADSVAE-LGEQIDNLQRVKQKLEKEK 1225
Cdd:PRK15374 101 LSQLESRLAVWQAMIESQKEMGIQVSKEFQTALGEAQEATDLYEASIKKT--DTAKSVYDaAEKKLTQAQNKLQSLDPAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1226 SEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQqrlINDLTAQRARLQTESGEYSRQLDEKDtlVSQL 1305
Cdd:PRK15374 179 PGYAQAEAAVEQAGKEATEAKEALDKATDATVKAGTDAKAKAEKA---DNILTKFQGTANAASQNQVSQGEQDN--LSNV 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115527082 1306 SRGKQAFTQQIEELKRQLEEEIKAKSALAHALQSSRH-DCDLLREQYEEEQEAKAELQRAM 1365
Cdd:PRK15374 254 ARLTMLMAMFIEIVGKNTEESLQNDLALFNALQEGRQaEMEKKSAEFQEETRKAEETNRIM 314
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1454-1753 |
3.91e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.66 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1454 DKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKI 1533
Cdd:PLN02939 113 NEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1534 KKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEvdrKIAEKDEeidqmkrnhiriVESMQSTLDAEIRSRN 1613
Cdd:PLN02939 193 KIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEE---NMLLKDD------------IQFLKAELIEVAETEE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1614 DAIRLKKK---MEGDLNEMEIQLNHANrmaAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIE 1690
Cdd:PLN02939 258 RVFKLEKErslLDASLRELESKFIVAQ---EDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVD 334
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115527082 1691 ELRATLEQTERSR------KIAEQELLDASERVQLLHTQNTSLIntkKKLETDISQIQGEMEDIIQEAR 1753
Cdd:PLN02939 335 KLEASLKEANVSKfssykvELLQQKLKLLEERLQASDHEIHSYI---QLYQESIKEFQDTLSKLKEESK 400
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1313-1587 |
4.47e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 45.02 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1313 TQQIEELKRQLEEEIKAksalahalqssrhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQwrTKYETDAIQRT-EELE 1391
Cdd:pfam05667 323 VETEEELQQQREEELEE-----------------LQEQLEDLESSIQELEKEIKKLESSIKQ--VEEELEELKEQnEELE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1392 EA---KKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVED----LMIDVERTNAACAA-LDKKQRNFDKIlAEWKQK 1463
Cdd:pfam05667 384 KQykvKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKhrvpLIEEYRALKEAKSNkEDESQRKLEEI-KELREK 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1464 CEETHAelEASQKEsrslstELFKiknayeESLDQLETLKREnKNLQQEIsdlteqiaeggKRIHElekIKKQVEQEKSE 1543
Cdd:pfam05667 463 IKEVAE--EAKQKE------ELYK------QLVAEYERLPKD-VSRSAYT-----------RRILE---IVKNIKKQKEE 513
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 115527082 1544 LQAALEEAEAsleheegkilrIQLELNQVKSEVDRKIAEKDEEI 1587
Cdd:pfam05667 514 ITKILSDTKS-----------LQKEINSLTGKLDRTFTVTDELV 546
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1654-1889 |
4.68e-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: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1654 LKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKK 1733
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1734 LETDISQIqgemeDIIQEARNAEEkakkAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLAlkggk 1813
Cdd:COG3883 98 SGGSVSYL-----DVLLGSESFSD----FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK----- 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115527082 1814 kqiQKLEARVRELEGEVESEQKRNVEAVKGLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEA 1889
Cdd:COG3883 164 ---AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
906-1048 |
5.20e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 44.24 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 906 EERCDQLIKTKIQLEAKIKEVTEraeDEEEINAELTakkrkledECSELKKDIDDLELTL-AKVEKEKHATENKVKNLTE 984
Cdd:smart00787 136 EWRMKLLEGLKEGLDENLEGLKE---DYKLLMKELE--------LLNSIKPKLRDRKDALeEELRQLKQLEDELEDCDPT 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115527082 985 EMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKI 1048
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGF 268
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1382-1676 |
5.91e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1382 DAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNevedlmidvertnaACAALDKKQRNFDKILAEWK 1461
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQ--------------APAKLRQAQAELEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1462 QKCEETHAELEASQKESR--SLSTELFKIKNAYEESLDQLETLKRENKNLQQEISdlteqiaEGGKRIHELEKIKKQVEQ 1539
Cdd:PRK11281 112 EETRETLSTLSLRQLESRlaQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALY-------ANSQRLQQIRNLLKGGKV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1540 EKSEL---QAALEEAEASLeheegkiLRIQLELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNdAI 1616
Cdd:PRK11281 185 GGKALrpsQRVLLQAEQAL-------LNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKR-LT 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115527082 1617 RLKKKMEGDLNEMEIQLNHANRM-AAEALRNYRNTQAILKDTQL-------------HLDDALRSQEDLKEQLA 1676
Cdd:PRK11281 257 LSEKTVQEAQSQDEAARIQANPLvAQELEINLQLSQRLLKATEKlntltqqnlrvknWLDRLTQSERNIKEQIS 330
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1674-1853 |
6.03e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1674 QLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQntslintKKKLETDISQIQGEMEDI---IQ 1750
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE-------IKRLELEIEEVEARIKKYeeqLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1751 EARNAEEkakkaitdaammAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVRELEGEV 1830
Cdd:COG1579 84 NVRNNKE------------YEALQKEIES---LKRRISDLEDEILELMERIEELE--------EELAELEAELAELEAEL 140
|
170 180
....*....|....*....|...
gi 115527082 1831 ESEQKRNVEAVKGLRKHERKVKE 1853
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEA 163
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1438-1582 |
6.21e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1438 RTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEsrslstELFKIKNAYE-ESLDQLETLKRENKNLQQEISDL 1516
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKE------EIHKLRNEFEkELRERRNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115527082 1517 TEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEASLEHEEGKILRI---------QLELNQVKSEVDRKIAE 1582
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaeeakEILLEKVEEEARHEAAV 173
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
933-1333 |
6.21e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 933 EEEINAEL-TAKKRKL-EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQT 1010
Cdd:PRK11281 38 EADVQAQLdALNKQKLlEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1011 LDDLQAEEdkvntltkakikLEQQVDDLEGSLEQEKK-----------IRMDLERAKRKLEGDLKLAQEstmdIENdkqQ 1079
Cdd:PRK11281 118 LSTLSLRQ------------LESRLAQTLDQLQNAQNdlaeynsqlvsLQTQPERAQAALYANSQRLQQ----IRN---L 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1080 LDEKLKKKEFEMSGLQSKIEDEQA-LGMQLQKKIKELQARIEELEEeieaerasrakAEKQRSdlsrELEEISERLEEAg 1158
Cdd:PRK11281 179 LKGGKVGGKALRPSQRVLLQAEQAlLNAQNDLQRKSLEGNTQLQDL-----------LQKQRD----YLTARIQRLEHQ- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1159 gATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQI------------DNLqRVKQKLEkeks 1226
Cdd:PRK11281 243 -LQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLlkateklntltqQNL-RVKNWLD---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1227 emkmeiddlasnmetvskakgNLEKMCRALEDQ---------LSEIKTKEEE---QQRLINDLTAQRARLQTESGEYSRQ 1294
Cdd:PRK11281 317 ---------------------RLTQSERNIKEQisvlkgsllLSRILYQQQQalpSADLIEGLADRIADLRLEQFEINQQ 375
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 115527082 1295 LDE---KDTLVSQLSRG-KQAFTqqiEELKRQLEEEIKAKSAL 1333
Cdd:PRK11281 376 RDAlfqPDAYIDKLEAGhKSEVT---DEVRDALLQLLDERREL 415
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1666-1939 |
6.30e-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: 44.73 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1666 RSQEDLKEQLAMVERRANL------LQAEIEELRATLEQTERSRKIAEQELldasERVQLLHTQNTSLINTKKKLETDIS 1739
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLeeaekaRQAEMDRQAAIYAEQERMAMEREREL----ERIRQEERKRELERIRQEEIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1740 QIQgEMEDIIQEARNAEEKAKKAITDA----AMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQ 1815
Cdd:pfam17380 376 RMR-ELERLQMERQQKNERVRQELEAArkvkILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1816 IQKLEARVRELEGEVESEQKRNVEAVKGLRKH----ERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKsyKRQAEEAEE 1891
Cdd:pfam17380 455 EQERQQQVERLRQQEEERKRKKLELEKEKRDRkraeEQRRKILEKELEERKQAMIEEERKRKLLEKEME--ERQKAIYEE 532
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 115527082 1892 QSNVNLSKFRRIQHELEE---AEERADIAESQVNKLRV--KSREVHTKIISEE 1939
Cdd:pfam17380 533 ERRREAEEERRKQQEMEErrrIQEQMRKATEERSRLEAmeREREMMRQIVESE 585
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1463-1855 |
6.34e-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: 44.50 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1463 KCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLET----LKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVE 1538
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRdreqWERQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1539 QEKSELQaalEEAEASLEHEEGKILRIqLELNQVKSEVDRKIAEKDEEIDQMKRNhiriVESMQSTLDAEIRSRNDAIRL 1618
Cdd:pfam07888 108 ASSEELS---EEKDALLAQRAAHEARI-RELEEDIKTLTQRVLERETELERMKER----AKKAGAQRKEEEAERKQLQAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1619 KKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQ---EDLKEQLAMVERRANLLQAEIEELRAT 1695
Cdd:pfam07888 180 LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEaenEALLEELRSLQERLNASERKVEGLGEE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1696 LEQTERSRKIAEQELLDAseRVQLLHTqNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKK 1775
Cdd:pfam07888 260 LSSMAAQRDRTQAELHQA--RLQAAQL-TLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1776 EQdtsahLERMKKNLEQTvkdlqhRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERKVKELT 1855
Cdd:pfam07888 337 ER-----MEREKLEVELG------REKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1135-1405 |
6.36e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1135 KAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKmrrDLEEATLQHEataatlrkkhaDSVAELGEQIDNL 1214
Cdd:PRK05771 47 KLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIK---DVEEELEKIE-----------KEIKELEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1215 QRVKQKLEKEKSEMK------MEIDDLASNmETVSKAKGNLEKmcrALEDQLSEIKTKEEEqqrlindltaqrarlqtes 1288
Cdd:PRK05771 113 ENEIKELEQEIERLEpwgnfdLDLSLLLGF-KYVSVFVGTVPE---DKLEELKLESDVENV------------------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1289 gEYSRQLDEKDTLVSQLSrgKQAFTQQIEELKRQLEEEIKAKsalahalqssrhDCDLLREQYEEEQEAKAELQRAMSKA 1368
Cdd:PRK05771 170 -EYISTDKGYVYVVVVVL--KELSDEVEEELKKLGFERLELE------------EEGTPSELIREIKEELEEIEKERESL 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 115527082 1369 NSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAE 1405
Cdd:PRK05771 235 LEELKELAKKYLEELLALYEYLEIELERAEALSKFLK 271
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1731-1918 |
6.42e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1731 KKKLETDISQIQGEMEDIIQEARN-AEEKAKKAITDAAMMAEELKKEQDtsahlermkknleqtvKDLQHRldeaeqlal 1809
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKeAEAIKKEALLEAKEEIHKLRNEFE----------------KELRER--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1810 kggKKQIQKLEARVRELEGEVESEQKRnveavkgLRKHERKVkeltyqtEEDRKNILRLQDLVDKLQAKVKS-YKRQAEE 1888
Cdd:PRK12704 81 ---RNELQKLEKRLLQKEENLDRKLEL-------LEKREEEL-------EKKEKELEQKQQELEKKEEELEElIEEQLQE 143
|
170 180 190
....*....|....*....|....*....|
gi 115527082 1889 AEEQSNVNLSKFRRIQHELEEAEERADIAE 1918
Cdd:PRK12704 144 LERISGLTAEEAKEILLEKVEEEARHEAAV 173
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
867-1060 |
6.68e-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: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 867 LAKTEAKRKELEEKMVTLmqeknDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAkkrk 946
Cdd:COG3206 191 LEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ---- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 947 lEDECSELKKDIDDLELTLAkvEKEKHATEN--KVKNLTEEMAGLdetiakltkeKKALQEAHQQTLDDLQAEedkVNTL 1024
Cdd:COG3206 262 -SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL----------RAQLQQEAQRILASLEAE---LEAL 325
|
170 180 190
....*....|....*....|....*....|....*.
gi 115527082 1025 TKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLE 1060
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1642-1933 |
7.74e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.36 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1642 EALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRAnllQAEIEELRATLEQTERSRKIAEQELLDASERVQLLH 1721
Cdd:pfam07111 73 QELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAG---QAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRLH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1722 TQN------------TSLINTKKKLETDISQIQ----GEMEDIIQEARNAE------EKAKKAITDAAMMAEELKK---E 1776
Cdd:pfam07111 150 QEQlssltqaheealSSLTSKAEGLEKSLNSLEtkraGEAKQLAEAQKEAEllrkqlSKTQEELEAQVTLVESLRKyvgE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1777 Q------------------DTSAHLERMKKNLEQTVKDLQHRLDE-AEQLALKGGK----------------KQIQKLEA 1821
Cdd:pfam07111 230 QvppevhsqtwelerqellDTMQHLQEDRADLQATVELLQVRVQSlTHMLALQEEEltrkiqpsdslepefpKKCRSLLN 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1822 RVRE----LEGEVESEQKRNVEAVKGLRKH------------------ERKVKELTYQTEEDRKNILRLQDLVDKLQAKV 1879
Cdd:pfam07111 310 RWREkvfaLMVQLKAQDLEHRDSVKQLRGQvaelqeqvtsqsqeqailQRALQDKAAEVEVERMSAKGLQMELSRAQEAR 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 115527082 1880 KSYKRQAEEAEEQSNVNLSKFRRIQHELEEAEERADIAESQV----NKLRVKSREVHT 1933
Cdd:pfam07111 390 RRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIpslsNRLSYAVRKVHT 447
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1015-1286 |
8.47e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1015 QAEEDKVNTLTKAKIKLEQQVDDLEGSLEQekkirmdlerAKRKLEgDLKlAQESTMDIENDKQQLDEKLKkkefemsgl 1094
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEE----------AEAALE-EFR-QKNGLVDLSEEAKLLLQQLS--------- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1095 qskiedeqalgmQLQKKIKELQArieeleeeieaerasrakaekQRSDLSRELEEISERLEEAGGATSAQIEmnkkrEAE 1174
Cdd:COG3206 223 ------------ELESQLAEARA---------------------ELAEAEARLAALRAQLGSGPDALPELLQ-----SPV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1175 FQKMRRDLEEATLQHEATAATLRKKHADsVAELGEQIDNLQRVKQKlekeksEMKMEIDDLASNMETVSKAKGNLEKMCR 1254
Cdd:COG3206 265 IQQLRAQLAELEAELAELSARYTPNHPD-VIALRAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLA 337
|
250 260 270
....*....|....*....|....*....|..
gi 115527082 1255 ALEDQLSEIKTKEEEQQRLINDLTAQRARLQT 1286
Cdd:COG3206 338 QLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1671-1939 |
8.62e-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: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1671 LKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKklETDISQIQGEMEDIIQ 1750
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQ--ERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1751 EARNAEEKAkkaitdaaMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEV 1830
Cdd:pfam17380 356 EERKRELER--------IRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1831 ESEQKRNVEAVKGLRKHERKVKELTYQTEEDRKNILRL-QDLVDKLQAKVKSYKRQAE--EAEEQSnvnlskfRRIQHEL 1907
Cdd:pfam17380 428 EQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLrQQEEERKRKKLELEKEKRDrkRAEEQR-------RKILEKE 500
|
250 260 270
....*....|....*....|....*....|..
gi 115527082 1908 EEAEERADIAESQVNKLRVKSREVHTKIISEE 1939
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEE 532
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1191-1450 |
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 115527082 1191 ATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNMETVSKAKGNLEKmcraledqlsEIKTKEEEQ 1270
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----------EIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1271 QRLINDLtAQRARLQTESGeysRQLDEKDTLVSqlSRGKQAFTQQIEELKRQleeeikaksalahalqsSRHDCDLLREQ 1350
Cdd:COG3883 82 EERREEL-GERARALYRSG---GSVSYLDVLLG--SESFSDFLDRLSALSKI-----------------ADADADLLEEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1351 yeeeQEAKAELQRAMSKANSEVAqwrtkyetdaiqrteELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVE 1430
Cdd:COG3883 139 ----KADKAELEAKKAELEAKLA---------------ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
250 260
....*....|....*....|
gi 115527082 1431 DLMIDVERTNAACAALDKKQ 1450
Cdd:COG3883 200 ELEAELAAAEAAAAAAAAAA 219
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1350-1554 |
1.11e-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: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1350 QYEEEQEAKAELQRAMSKANSEVAQWRTKYEtdaiqrteELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEV 1429
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE--------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1430 EDLMIDVERTNAA-------------------CAALDKKQRNFDKILAEWKQkceeTHAELEASQKESRSLSTELFKIKN 1490
Cdd:COG3883 89 GERARALYRSGGSvsyldvllgsesfsdfldrLSALSKIADADADLLEELKA----DKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115527082 1491 AYEESLDQLETLKRENknlQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEEAEAS 1554
Cdd:COG3883 165 ELEAAKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1239-1326 |
1.24e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 41.84 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1239 METVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSRGKQAFTQQ--- 1315
Cdd:pfam08614 66 LAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQlnm 145
|
90
....*....|.
gi 115527082 1316 IEELKRQLEEE 1326
Cdd:pfam08614 146 AEEKLRKLEKE 156
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1783-1908 |
1.29e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1783 LERMKK-NLEQTVKDLQHRLDEAEQL------ALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVkglrkheRKVKELT 1855
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEAErsrlqaLLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 115527082 1856 YQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNVNLSkfRRIQhELE 1908
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALA--QRVQ-ELN 193
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1347-1556 |
1.35e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1347 LREQYEEEQEAKAELQRAmsKANSEVAQWRTKYETDAIqrtEELEEAKkklaqrLQDAEEhveavnakcASLEKTKQRLQ 1426
Cdd:COG0497 160 YREAYRAWRALKKELEEL--RADEAERARELDLLRFQL---EELEAAA------LQPGEE---------EELEEERRRLS 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1427 NeVEDLMIDV--------ERTNAACAALDKKQRNFDKI------LAEWKQKCEETHAELEASQKESRSLST-------EL 1485
Cdd:COG0497 220 N-AEKLREALqealealsGGEGGALDLLGQALRALERLaeydpsLAELAERLESALIELEEAASELRRYLDslefdpeRL 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115527082 1486 FKIknayEESLDQLETLKRENKNLQQEISDLTEQIAEggkRIHELEkikkQVEQEKSELQAALEEAEASLE 1556
Cdd:COG0497 299 EEV----EERLALLRRLARKYGVTVEELLAYAEELRA---ELAELE----NSDERLEELEAELAEAEAELL 358
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1463-1798 |
1.44e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 43.74 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1463 KCEETHAELE----------ASQKESRSLSTELFKiknayeesldqlETLKRENKNLQQEISDLTEQIAEggkriheLEK 1532
Cdd:pfam15964 357 QCEQLKSELErqkerlekelASQQEKRAQEKEALR------------KEMKKEREELGATMLALSQNVAQ-------LEA 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1533 IKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQMKRNHIRIVEsmqsTLDAEIrsr 1612
Cdd:pfam15964 418 QVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLE----IKDQEI--- 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1613 ndairlkKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDT--QLHLDdalRSQEDLKEQLAMVERRANLLQAEIE 1690
Cdd:pfam15964 491 -------EKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESehQLHLT---RLEKESIQQSFSNEAKAQALQAQQR 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1691 ElratLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTK-------KKLETDISQIQGEMEDIIQEARNAEEKAKKAI 1763
Cdd:pfam15964 561 E----QELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKeecctlaKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQ 636
|
330 340 350
....*....|....*....|....*....|....*
gi 115527082 1764 TDAAMMAEELKkeQDTSAHlERMKKNLEQTVKDLQ 1798
Cdd:pfam15964 637 KRNEELEEQCV--QHGRMH-ERMKQRLRQLDKHCQ 668
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1134-1284 |
1.72e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1134 AKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKH-----ADSVAELG 1208
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAAL----EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115527082 1209 EQIDNLQRVKQKLEKEKSEMKMEIDDLAsnmETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARL 1284
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELE---EELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1078-1240 |
1.90e-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: 41.83 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1078 QQLDEKLKKKEFEMSGLQSKIEDeqalgmqLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEA 1157
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1158 GG-----ATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEI 1232
Cdd:COG1579 86 RNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*...
gi 115527082 1233 DDLASNME 1240
Cdd:COG1579 166 EELAAKIP 173
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
918-1735 |
2.19e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.12 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 918 QLEAKIKEVTERAEDEEEINAELtakkRKLEDECSELKKDIDDLE---------------LTLAKVEKEKHATENKVKNL 982
Cdd:TIGR01612 1170 EIEKKIENIVTKIDKKKNIYDEI----KKLLNEIAEIEKDKTSLEevkginlsygknlgkLFLEKIDEEKKKSEHMIKAM 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 983 TEEMAGLDEtiaklTKEKKALQEAHQQTLDDLQAEEDKVNT--------LTKAKIKLEQQVDDLEGSLE--QEKKIRMDL 1052
Cdd:TIGR01612 1246 EAYIEDLDE-----IKEKSPEIENEMGIEMDIKAEMETFNIshdddkdhHIISKKHDENISDIREKSLKiiEDFSEESDI 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1053 ERAKRKLEGDLKLAQESTMDI-------------------------------------ENDKQQLD--EKLKKKEFEMSG 1093
Cdd:TIGR01612 1321 NDIKKELQKNLLDAQKHNSDInlylneianiynilklnkikkiidevkeytkeieennKNIKDELDksEKLIKKIKDDIN 1400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1094 LQ---SKIE---DEQALGMQLQkKIKELQARIEELEEEIEAERAS--------------------------RAKAEKQRS 1141
Cdd:TIGR01612 1401 LEeckSKIEstlDDKDIDECIK-KIKELKNHILSEESNIDTYFKNadennenvlllfkniemadnksqhilKIKKDNATN 1479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1142 DLSRELEEISERLEEAGG------ATSAQIEMNKKReaeFQKMRRDLEEatLQHEATAATLRKKHADSVAELGEQIDNLQ 1215
Cdd:TIGR01612 1480 DHDFNINELKEHIDKSKGckdeadKNAKAIEKNKEL---FEQYKKDVTE--LLNKYSALAIKNKFAKTKKDSEIIIKEIK 1554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1216 RVKQK--LEKEKSEMKME--------IDDLASNMETVSKAKGNLEKMCRALEDQL---SEIKTKeeeqqrlINDLTAQRA 1282
Cdd:TIGR01612 1555 DAHKKfiLEAEKSEQKIKeikkekfrIEDDAAKNDKSNKAAIDIQLSLENFENKFlkiSDIKKK-------INDCLKETE 1627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1283 RLQTESGEYSrqLDEKDTLVSQLSRGK---QAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLREQY-------- 1351
Cdd:TIGR01612 1628 SIEKKISSFS--IDSQDTELKENGDNLnslQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYeigiieki 1705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1352 -EEEQEAKAELQRAMSKANSEVAQWRTKYET---DAIQRTEELEEAKKKLAQRLQDAEE-------HVEAVNAKCASLEK 1420
Cdd:TIGR01612 1706 kEIAIANKEEIESIKELIEPTIENLISSFNTndlEGIDPNEKLEEYNTEIGDIYEEFIElyniiagCLETVSKEPITYDE 1785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1421 TKQRLQNEVEDLMIDVERTNAACAALDK-KQRNFDKILAEWKQKCEETHAeleasqkesrSLSTELFKIKNAYEESLDQL 1499
Cdd:TIGR01612 1786 IKNTRINAQNEFLKIIEIEKKSKSYLDDiEAKEFDRIINHFKKKLDHVND----------KFTKEYSKINEGFDDISKSI 1855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1500 ETLKRE-NKNLQQEISDLTEQIAEG--GKRIH----ELEKIKKQVEQEKSELQAALEEAE-------------ASLEHEE 1559
Cdd:TIGR01612 1856 ENVKNStDENLLFDILNKTKDAYAGiiGKKYYsykdEAEKIFINISKLANSINIQIQNNSgidlfdniniailSSLDSEK 1935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1560 GKILRIqLELNQVKSEVDRKIA----------EKDEEIDQMKRNHIRIVESMQStLDAEIRSRND----AIRLKKKMEGD 1625
Cdd:TIGR01612 1936 EDTLKF-IPSPEKEPEIYTKIRdsydtlldifKKSQDLHKKEQDTLNIIFENQQ-LYEKIQASNElkdtLSDLKYKKEKI 2013
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1626 LNEMEIQLNHANRMAAEALrNYRNTQAILKDT-QLHLDDALRSQEDLKEQLAMvERRANLLQAEIEELRATLEQTERSRK 1704
Cdd:TIGR01612 2014 LNDVKLLLHKFDELNKLSC-DSQNYDTILELSkQDKIKEKIDNYEKEKEKFGI-DFDVKAMEEKFDNDIKDIEKFENNYK 2091
|
970 980 990
....*....|....*....|....*....|.
gi 115527082 1705 IAEQELLDASErvqllhtQNTSLINTKKKLE 1735
Cdd:TIGR01612 2092 HSEKDNHDFSE-------EKDNIIQSKKKLK 2115
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1664-1859 |
2.28e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1664 ALRSQEDLKEQLAMVERRAN------LLQAEIEELRATLEQTERSRKI----------AEQELLDASERVQLLHTQNTSL 1727
Cdd:PRK11281 34 DLPTEADVQAQLDALNKQKLleaedkLVQQDLEQTLALLDKIDRQKEEteqlkqqlaqAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1728 INTK------KKLETDISQIQGEMEDiIQEA-----------RNAEEKAKKAITDAAMMAEE----LKKEQDTSAHL--- 1783
Cdd:PRK11281 114 TRETlstlslRQLESRLAQTLDQLQN-AQNDlaeynsqlvslQTQPERAQAALYANSQRLQQirnlLKGGKVGGKALrps 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1784 ERMKKNLEQTVKDLQHRLdeaEQLALKG-------GKKQIQKLEARVRELEGEVESEQkrnvEAV--KGLRKHERKVKEL 1854
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDL---QRKSLEGntqlqdlLQKQRDYLTARIQRLEHQLQLLQ----EAInsKRLTLSEKTVQEA 265
|
....*
gi 115527082 1855 TYQTE 1859
Cdd:PRK11281 266 QSQDE 270
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1610-1927 |
2.39e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.00 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1610 RSRNDAI-RLKKKMEGDL------NEMEIQLNHANRMAAEAlrnYRNTQAILKdTQLHLDDALRSQEDLKEQLAMVERra 1682
Cdd:PLN03188 915 QTREDKIiRLESLMDGVLskedflEEELASLMHEHKLLKEK---YENHPEVLR-TKIELKRVQDELEHYRNFYDMGER-- 988
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1683 NLLQAEIEELRATLEQTERSrkiaeqELLDASERVQLLHTQNTSLINTKKKLETdISQIQGEM--EDIIQEARNAEEKAK 1760
Cdd:PLN03188 989 EVLLEEIQDLRSQLQYYIDS------SLPSARKRNSLLKLTYSCEPSQAPPLNT-IPESTDESpeKKLEQERLRWTEAES 1061
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1761 KAITdaamMAEELKKEQDTSAHL-ERMKKNLEqTVKDLQHRLDEAEQLALKGGKKQIQK----------LEARVRELEGE 1829
Cdd:PLN03188 1062 KWIS----LAEELRTELDASRALaEKQKHELD-TEKRCAEELKEAMQMAMEGHARMLEQyadleekhiqLLARHRRIQEG 1136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1830 VESEQKRNVEA-VKGLR--------------KHERKvKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRqAEEAEEQSN 1894
Cdd:PLN03188 1137 IDDVKKAAARAgVRGAEskfinalaaeisalKVERE-KERRYLRDENKSLQAQLRDTAEAVQAAGELLVR-LKEAEEALT 1214
|
330 340 350
....*....|....*....|....*....|...
gi 115527082 1895 VnlskfrrIQHELEEAEERADIAESQVNKLRVK 1927
Cdd:PLN03188 1215 V-------AQKRAMDAEQEAAEAYKQIDKLKRK 1240
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
846-1034 |
2.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 846 SAETEKEMANMKEEFEKTKEELAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEErcdQLIKTKIQLEAKIKE 925
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA---EIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 926 VTERA------------------------------------EDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVE 969
Cdd:COG3883 88 LGERAralyrsggsvsyldvllgsesfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115527082 970 KEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQ 1034
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
867-1002 |
2.72e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 42.05 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 867 LAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAeercdQLIKTKI-QLEAKIKEVTERAEdeeEINAELTAKKR 945
Cdd:pfam10186 28 LARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKL-----RLLKSEVaISNERLNEIKDKLD---QLRREIAEKKK 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 115527082 946 KLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKA 1002
Cdd:pfam10186 100 KIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRS 156
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1742-1931 |
2.77e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1742 QGEMEDIIqEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVK---DLQHRLDEAEQlALKGGKKQIQK 1818
Cdd:PRK03918 134 QGEIDAIL-ESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKrteNIEELIKEKEK-ELEEVLREINE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1819 LEARVRELEGEVEseqkrnveavkGLRKHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNVNLS 1898
Cdd:PRK03918 212 ISSELPELREELE-----------KLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE 280
|
170 180 190
....*....|....*....|....*....|...
gi 115527082 1899 KFRRIQhELEEAEERADIAESQVNKLRVKSREV 1931
Cdd:PRK03918 281 KVKELK-ELKEKAEEYIKLSEFYEEYLDELREI 312
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1678-1917 |
3.09e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1678 VERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLhtqntslintKKKLETDISQIQgEMEDIIQEARNAEE 1757
Cdd:pfam00038 45 PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDF----------RQKYEDELNLRT-SAENDLVGLRKDLD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1758 KAKKAITDAAMMAEELKKEqdtsahLERMKKNLEQTVKDLQHRL-DEAEQLALKGGKKQiqKLEARVRELEGEVESEQKR 1836
Cdd:pfam00038 114 EATLARVDLEAKIESLKEE------LAFLKKNHEEEVRELQAQVsDTQVNVEMDAARKL--DLTSALAEIRAQYEEIAAK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1837 NVEAVKglRKHERKVKELTYQTE--------------EDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNVNLSKFRR 1902
Cdd:pfam00038 186 NREEAE--EWYQSKLEELQQAAArngdalrsakeeitELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQE 263
|
250
....*....|....*..
gi 115527082 1903 IQHELEEA--EERADIA 1917
Cdd:pfam00038 264 LISELEAElqETRQEMA 280
|
|
| EcCorA_ZntB-like |
cd12821 |
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily ... |
1299-1411 |
3.17e-03 |
|
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. Members of this family are found in all three kingdoms of life. It is a functionally diverse family, including the Mg2+ transporters Escherichia coli and Salmonella typhimurium CorAs (which can also transport Co2+, and Ni2+ ), and the Zn2+ transporter Salmonella typhimurium ZntB which mediates the efflux of Zn2+ (and Cd2+). It also includes two Saccharomyces cerevisiae members: the inner membrane Mg2+ transporters Mfm1p/Lpe10p, and Mrs2p, and a family of Arabidopsis thaliana members (AtMGTs) some of which are localized to distinct tissues, and not all of which can transport Mg2+. Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport.
Pssm-ID: 213355 [Multi-domain] Cd Length: 285 Bit Score: 41.53 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1299 DTLVSQLSRGKQAFTQQIEELKRQLEEEIKAKSaLAHALqSSRHDCDLLREQYEEEQEAKAELQRAMSKANSEvaQWRTK 1378
Cdd:cd12821 110 GAIIKALLTGIDQFEEKLEELEWDLLEGNNAIK-LDRIL-ELRRELLRLTNLIEPQQEVLMALQEAFAELLFS--EDEEE 185
|
90 100 110
....*....|....*....|....*....|...
gi 115527082 1379 YEtDAIQRTEELEEAKKKLAQRLQDAEEHVEAV 1411
Cdd:cd12821 186 LR-RTLDRIERLLQLIEEYEQELDTLQDIEEVV 217
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1686-1892 |
3.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1686 QAEIEELRATLEQTERSRKIAEQELLDASERVQllhtqntSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITD 1765
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELE-------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1766 AAMMAEELKKEQDTSAHLERMKKNleQTVKDLQHRLDEAEQLAlKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLR 1845
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLGS--ESFSDFLDRLSALSKIA-DADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 115527082 1846 KHERKVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQ 1892
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
867-1098 |
3.44e-03 |
|
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: 42.45 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 867 LAKTEAKRKELEEKMVTLMQEK--NDLQLQVQAEADSLADaeercdqliktkiQLEAKIKEVTERAEDEEEINAELTAKK 944
Cdd:pfam18971 619 LEKSLRKREHLEKEVEKKLESKsgNKNKMEAKAQANSQKD-------------EIFALINKEANRDARAIAYTQNLKGIK 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 945 RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL-------DETIAKLTKEKKALQEAHQQTLDDLqae 1017
Cdd:pfam18971 686 RELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSvkdlginPEWISKVENLNAALNEFKNGKNKDF--- 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1018 edkvNTLTKAKIKLEQQVDDLEGSLEQEKKI-RMDLERAKRKLEGDLKLAQESTMDIEN-DKQQLDEKLKKKEFEMSGLQ 1095
Cdd:pfam18971 763 ----SKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfSKEQLAQQAQKNEDFNTGKN 838
|
...
gi 115527082 1096 SKI 1098
Cdd:pfam18971 839 SEL 841
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1538-1781 |
3.54e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1538 EQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR---KIAEKDEEIDQMKRNhirivesmQSTLDAEIRSRND 1614
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNElqaELEALQAEIDKLQAE--------IAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1615 AIrlkkkmegdlnemeiqlnhaNRMAAEALRNYRNTQAIlkdtqlhldDALRSQEDLKEQLamveRRANLLQAEIEELRA 1694
Cdd:COG3883 87 EL--------------------GERARALYRSGGSVSYL---------DVLLGSESFSDFL----DRLSALSKIADADAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1695 TLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELK 1774
Cdd:COG3883 134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
....*..
gi 115527082 1775 KEQDTSA 1781
Cdd:COG3883 214 AAAAAAA 220
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
868-1070 |
3.57e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.16 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 868 AKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINA---ELTAKK 944
Cdd:PRK00106 24 IKMKSAKEAAELTLLNAEQEAVNLRGKAERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSerqELKQIE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 945 RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEmaglDETIAKLTKEKkalqEAHQQTLDDLQAEEDKVNTL 1024
Cdd:PRK00106 104 SRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDER----EEQVEKLEEQK----KAELERVAALSQAEAREIIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 115527082 1025 TKAKIKLEQQVDDLEGSLEQEKKIRMD------LERAKRKLEGDLKLAQEST 1070
Cdd:PRK00106 176 AETENKLTHEIATRIREAEREVKDRSDkmakdlLAQAMQRLAGEYVTEQTIT 227
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
913-1115 |
3.72e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 913 IKTKIQLEaKIKEVTERAED--------EEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEkhatenkVKNLTE 984
Cdd:PRK05771 36 LKEELSNE-RLRKLRSLLTKlsealdklRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKE-------IKELEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 985 EMAGLDETIAKLTKEKKALQ--EAHQQTLDDLQAEED---KVNTLTKAKIKLEQQVDDLEGSLEQEKK------IRMDLE 1053
Cdd:PRK05771 108 EISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvFVGTVPEDKLEELKLESDVENVEYISTDkgyvyvVVVVLK 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115527082 1054 RAKRKLEGDLKLAQESTMDIENDKqQLDEKLKKKEFEMSGLQSKIEDeqalgmqLQKKIKEL 1115
Cdd:PRK05771 188 ELSDEVEEELKKLGFERLELEEEG-TPSELIREIKEELEEIEKERES-------LLEELKEL 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1607-1767 |
3.81e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1607 AEIRSRNDAIR-LKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMV--ERRAN 1683
Cdd:COG1579 13 QELDSELDRLEhRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1684 LLQAEIEELratleqtERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAI 1763
Cdd:COG1579 93 ALQKEIESL-------KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....
gi 115527082 1764 TDAA 1767
Cdd:COG1579 166 EELA 169
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1647-1798 |
4.17e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1647 YRNTQAILKDTQLHLDDALRSQ--EDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTqN 1724
Cdd:cd22656 93 YAEILELIDDLADATDDEELEEakKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLT-D 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115527082 1725 TSLINTKKKLETDISQIQGEMEDIIQEARNAEEKAKKAITDAammAEELKKEQDTSAHLERMKKNLEQTVKDLQ 1798
Cdd:cd22656 172 EGGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADD---EAKLAAALRLIADLTAADTDLDNLLALIG 242
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1487-1708 |
4.84e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.60 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1487 KIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIK------KQVEQEKS------ELQAALEEAEAS 1554
Cdd:COG0497 155 ELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAAlqpgeeEELEEERRrlsnaeKLREALQEALEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1555 LEHEEGKILRIqleLNQVKSEVDRkIAEKDEEIDQMkrnhIRIVESMQSTLD---AEIRSRNDAIrlkkkmEGD---LNE 1628
Cdd:COG0497 235 LSGGEGGALDL---LGQALRALER-LAEYDPSLAEL----AERLESALIELEeaaSELRRYLDSL------EFDperLEE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1629 MEIQLNHANRMAaealRNYRNTqailkdtqlhLDDALRSQEDLKEQLAMVERRANL---LQAEIEELRATLEQ-----TE 1700
Cdd:COG0497 301 VEERLALLRRLA----RKYGVT----------VEELLAYAEELRAELAELENSDERleeLEAELAEAEAELLEaaeklSA 366
|
....*...
gi 115527082 1701 RSRKIAEQ 1708
Cdd:COG0497 367 ARKKAAKK 374
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1680-1831 |
5.06e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.43 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1680 RRANLLQAEIEELratLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETdisqiqgEMEDIIQEARNAEEKA 1759
Cdd:pfam04012 4 RLGRLVRANIHEG---LDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLER-------RLEQQTEQAKKLEEKA 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115527082 1760 KKAITDAAmmaEELKKEqdtsahLERMKKNLEQTVKDLQHRLDEAEQLALKGgKKQIQKLEARVRELEGEVE 1831
Cdd:pfam04012 74 QAALTKGN---EELARE------ALAEKKSLEKQAEALETQLAQQRSAVEQL-RKQLAALETKIQQLKAKKN 135
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
867-1070 |
5.09e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 867 LAKTEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRK 946
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 947 LEDECSELK-----KDIDDLeltLAKVEKEKHATENKvknlTEEMAGLDETIAKLTKEKKALQEAhQQTLDDLQAE-EDK 1020
Cdd:COG3883 98 SGGSVSYLDvllgsESFSDF---LDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAK-LAELEALKAElEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 115527082 1021 VNTLTKAKIKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQEST 1070
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
898-1298 |
5.88e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 898 EADSLADAEERCDQLIKTKIQLEAKIKE-VTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEK----EK 972
Cdd:COG5185 118 ILISLLYLYKSEIVALKDELIKVEKLDEiADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGiselKK 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 973 HATE---NKVKNLTEEMAGLDETIaKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLE-----GSLEQ 1044
Cdd:COG5185 198 AEPSgtvNSIKESETGNLGSESTL-LEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRleklgENAES 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1045 EKKIRMDLERAKRKLEGDLKLAQEST--MDIENDKQQLDEKLKKKEFE------MSGLQSKIEDEQALGMQLQKKIKELQ 1116
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAEYTksIDIKKATESLEEQLAAAEAEqeleesKRETETGIQNLTAEIEQGQESLTENL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1117 ARIEELEEEIEAERASRAKAEKQRSdLSRELEEISERLEEAGGATSAQIEMNKKREA--------EFQKMRRDLEEATLQ 1188
Cdd:COG5185 357 EAIKEEIENIVGEVELSKSSEELDS-FKDTIESTKESLDEIPQNQRGYAQEILATLEdtlkaadrQIEELQRQIEQATSS 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1189 HEATAATLRKKHADSVAELGEQIDNLQ-RVKQKLEKEKSEMKMEIDDLASNME----TVSKAKGNLEKMCRALEDQLSEI 1263
Cdd:COG5185 436 NEEVSKLLNELISELNKVMREADEESQsRLEEAYDEINRSVRSKKEDLNEELTqiesRVSTLKATLEKLRAKLERQLEGV 515
|
410 420 430
....*....|....*....|....*....|....*
gi 115527082 1264 KTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEK 1298
Cdd:COG5185 516 RSKLDQVAESLKDFMRARGYAHILALENLIPASEL 550
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
871-1338 |
5.92e-03 |
|
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: 41.66 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 871 EAKRKELEEKMVTLMQEKNDLQLQVqaeadsladaeercdQLIKTKIQ-----LEAKIKEVTERAEDEEEINAELTAKKR 945
Cdd:pfam07111 241 ELERQELLDTMQHLQEDRADLQATV---------------ELLQVRVQslthmLALQEEELTRKIQPSDSLEPEFPKKCR 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 946 KLedecseLKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTL- 1024
Cdd:pfam07111 306 SL------LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLq 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1025 ------TKAKIKLEQQVDDLEgslEQEKKIRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEfemsglqski 1098
Cdd:pfam07111 380 melsraQEARRRQQQQTASAE---EQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVH---------- 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1099 edeqalgmqlqkKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISE---RL--EEAGGATSAQIEMNKKREa 1173
Cdd:pfam07111 447 ------------TIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREernRLdaELQLSAHLIQQEVGRARE- 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1174 EFQKMRRDLEEATLQHEATAatlrKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDlasnmetvskakgNLEKMC 1253
Cdd:pfam07111 514 QGEAERQQLSEVAQQLEQEL----QRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQ-------------QQEIYG 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1254 RALEDQLSEIKTKEEEQ----QRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQLSR-GKQAFTQQIEELKRQLEEEIK 1328
Cdd:pfam07111 577 QALQEKVAEVETRLREQlsdtKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRlQDEARKEEGQRLARRVQELER 656
|
490
....*....|
gi 115527082 1329 AKSALAHALQ 1338
Cdd:pfam07111 657 DKNLMLATLQ 666
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1385-1552 |
6.36e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1385 QRTEELEEAKKKLAQRLQDA--EEHVEAVNAKCASLEKTKQR---LQNEVEDLMIDVERTNAACAALDKKQ--------- 1450
Cdd:pfam09787 14 QKAARILQSKEKLIASLKEGsgVEGLDSSTALTLELEELRQErdlLREEIQKLRGQIQQLRTELQELEAQQqeeaessre 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1451 --RNFDKILAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIH 1528
Cdd:pfam09787 94 qlQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLH 173
|
170 180 190
....*....|....*....|....*....|.
gi 115527082 1529 ELEK--IKKQ-----VEQEKSELQAALEEAE 1552
Cdd:pfam09787 174 QLTEtlIQKQtmleaLSTEKNSLVLQLERME 204
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1457-1738 |
6.38e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1457 LAEWKQKCEETHAELEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQ 1536
Cdd:COG4372 61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1537 VEQEKSELQAALEEAEASLEHEEGKILRIQLELNQvksevdRKIAEKDEEIDQMKRNHIRIVESMQSTLDAEIRSRNDAI 1616
Cdd:COG4372 141 LQSEIAEREEELKELEEQLESLQEELAALEQELQA------LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1617 RLKKKMEGDLNEMEIQLNhanrmAAEALRNYRNTQAILKDTQLHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATL 1696
Cdd:COG4372 215 ELAEELLEAKDSLEAKLG-----LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 115527082 1697 EQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDI 1738
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1447-1592 |
6.98e-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: 41.17 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1447 DKKQRNFDKILAEWKQKCEETHAELEASQKESRS-LSTEL--FKIKNAYEESLDQLETLKRENK-NLQQEISDLTEQIAE 1522
Cdd:pfam05667 242 KRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQdLAELLssFSGSSTTDTGLTKGSRFTHTEKlQFTNEAPAATSSPPT 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115527082 1523 GGKrihELEKIKKQVEQEKSELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRK---IAEKDEEIDQMKR 1592
Cdd:pfam05667 322 KVE---TEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELkeqNEELEKQYKVKKK 391
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1310-1485 |
7.28e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1310 QAFTQQIEELKRQLEEEIKAKSALAHALQSsrhdcdlLREQYEEEQEAKAELQRAMSKANSEVAQWRTKyetdaiqrtee 1389
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEAR----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1390 LEEAKKKLAQrLQDAEEhVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNAACAA----LDKKQRNFDKILAEWKQKCE 1465
Cdd:COG1579 75 IKKYEEQLGN-VRNNKE-YEALQKEIESLKRRISDLEDEILELMERIEELEEELAEleaeLAELEAELEEKKAELDEELA 152
|
170 180
....*....|....*....|
gi 115527082 1466 ETHAELEASQKESRSLSTEL 1485
Cdd:COG1579 153 ELEAELEELEAEREELAAKI 172
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
870-1559 |
7.57e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.32 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 870 TEAKRKELEEKMVTLMQEKNDLQLQVQAEADSLaDAEERCDQLiktkiQLEAKIKEVTERAEDEEEINAELTAKKRKLED 949
Cdd:PRK10246 214 TPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSL-NWLTRLDEL-----QQEASRRQQALQQALAAEEKAQPQLAALSLAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 950 ECSELKKDIDDLELTLAKVEKEKHATEnKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKV----NTLT 1025
Cdd:PRK10246 288 PARQLRPHWERIQEQSAALAHTRQQIE-EVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFrqwnNELA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1026 KAKIKLEQQVDDLEgsleQEKKIRMDLERAKRKLEG----DLKLAQEST---MDIENDKQQLDEKLkkkefemSGLQSKI 1098
Cdd:PRK10246 367 GWRAQFSQQTSDRE----QLRQWQQQLTHAEQKLNAlpaiTLTLTADEVaaaLAQHAEQRPLRQRL-------VALHGQI 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1099 EDEQALGMQLQKKIKELQARIEELEEEIEAERAS---------RAKAEKQRSDLSRELEEISERLEEA------GGATSA 1163
Cdd:PRK10246 436 VPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRykektqqlaDVKTICEQEARIKDLEAQRAQLQAGqpcplcGSTSHP 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1164 QIEMNKKREAEFQKMRRDL---EEATLQHEatAATLRKkhadsvaelgeQIDNLQRVKQKLEKEKSEMKMEIDDLASNME 1240
Cdd:PRK10246 516 AVEAYQALEPGVNQSRLDAlekEVKKLGEE--GAALRG-----------QLDALTKQLQRDESEAQSLRQEEQALTQQWQ 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1241 TVSKAKGnlekMCRALEDQLSEIKTKEEEQQRLInDLTAQRARLQTesgeysrQLDEKDTLVSQlsrgkqaFTQQIEELK 1320
Cdd:PRK10246 583 AVCASLN----ITLQPQDDIQPWLDAQEEHERQL-RLLSQRHELQG-------QIAAHNQQIIQ-------YQQQIEQRQ 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1321 RQLEEEIkakSALAHALQSSRHDCDLLREQYEEE---QEAKAELQRAMSKANSEVAQWRTKYETDaiqrtEELEEAKKKL 1397
Cdd:PRK10246 644 QQLLTAL---AGYALTLPQEDEEASWLATRQQEAqswQQRQNELTALQNRIQQLTPLLETLPQSD-----DLPHSEETVA 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1398 AQRLQDAEEhveavnaKCASLEKTKQRLQNEVEDLMIDVERTNAACAALDKKQRNFDK--ILA-----EWKQKCEETHAE 1470
Cdd:PRK10246 716 LDNWRQVHE-------QCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQqaFLAalldeETLTQLEQLKQN 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1471 LEASQKESRSLSTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKSELQAALEE 1550
Cdd:PRK10246 789 LENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQQ 868
|
730
....*....|
gi 115527082 1551 -AEASLEHEE 1559
Cdd:PRK10246 869 iAQATQQVED 878
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
928-1184 |
8.23e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 928 ERAEDEEEINAELTAKKRKLEDECSELKKDID--------------DLELTLAKVEKEKHATENKvKNLTEEMAGLDETI 993
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRKLEEAEKARQAEMDrqaaiyaeqermamERERELERIRQEERKRELE-RIRQEEIAMEISRM 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 994 AKLTKEKKALQEAHQQTLDDLQA-------EEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKiRMDLERAkRKLEGDLKLA 1066
Cdd:pfam17380 378 RELERLQMERQQKNERVRQELEAarkvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVR-RLEEERA-REMERVRLEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1067 QESTMDIENDKQQLDEKlKKKEFEMsglqSKIEDEQALGMQLQKKIkeLQARIEELEEEIEAERASRAKAEKQRSDLSRE 1146
Cdd:pfam17380 456 QERQQQVERLRQQEEER-KRKKLEL----EKEKRDRKRAEEQRRKI--LEKELEERKQAMIEEERKRKLLEKEMEERQKA 528
|
250 260 270
....*....|....*....|....*....|....*...
gi 115527082 1147 LEEiSERLEEAGGATSAQIEMNKKREAEfQKMRRDLEE 1184
Cdd:pfam17380 529 IYE-EERRREAEEERRKQQEMEERRRIQ-EQMRKATEE 564
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1190-1433 |
8.44e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1190 EATAATLRKKHADSVAELGEQidNLQRVKQKLEkeksEMKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEE 1269
Cdd:PRK04778 255 EKEIQDLKEQIDENLALLEEL--DLDEAEEKNE----EIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1270 QQRLInDLTAQRARLQTESGEYSRQLDEkdtlvsQLsrgkQAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDCDLLRE 1349
Cdd:PRK04778 329 LKEEI-DRVKQSYTLNESELESVRQLEK------QL----ESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEK 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1350 QYEEEQEAKAELQRAMSKANSEVAQWRTKYET---------------DAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAK 1414
Cdd:PRK04778 398 EQEKLSEMLQGLRKDELEAREKLERYRNKLHEikryleksnlpglpeDYLEMFFEVSDEIEALAEELEEKPINMEAVNRL 477
|
250
....*....|....*....
gi 115527082 1415 CASLEKTKQRLQNEVEDLM 1433
Cdd:PRK04778 478 LEEATEDVETLEEETEELV 496
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1149-1398 |
8.71e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.09 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1149 EISERLEEAggatsAQIEMNKKR-EAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIdnlqRVKQKLEKEKSE 1227
Cdd:PRK05035 437 EIRAIEQEK-----KKAEEAKARfEARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARV----KAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1228 MKMEIDDLASNMETVSKAKGNLEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEYSRQLDEKDTLVSQ-LS 1306
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAaIA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1307 RGK-----QAFTQQIEELKRQLEEEIKAKSALAHALQSSRHDC-DLLREQYEEEQEAKAELQRAMSKAnsevaqwRTKYE 1380
Cdd:PRK05035 588 RAKakkaaQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEqQANAEPEEPVDPRKAAVAAAIARA-------KARKA 660
|
250
....*....|....*...
gi 115527082 1381 TDAIQRTEELEEAKKKLA 1398
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKA 678
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1132-1447 |
8.87e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1132 SRAKAEKQRSDLSRELEEIseRLEEAGGATSAQiemnkkREAEfqKMRRDLEEATLQHEATAATLRkkhADSVAELGEQI 1211
Cdd:NF041483 955 AAAQAEQLIAEATGEAERL--RAEAAETVGSAQ------QHAE--RIRTEAERVKAEAAAEAERLR---TEAREEADRTL 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1212 DNlqrVKQKLEKEKSEMKMEIDDLASnmETVSKAKgnlEKMCRALEDQLSEIKTKEEEQQRLINDLTAQRARLQTESGEY 1291
Cdd:NF041483 1022 DE---ARKDANKRRSEAAEQADTLIT--EAAAEAD---QLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVE 1093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1292 SRQLDEK-----DTLVSQLSRGKQAFTQQIEELKRQLEEEI-----KAKSALAHALQSSRHDCDLLREQYEEEQ-EAKAE 1360
Cdd:NF041483 1094 GNSLVEKartdaDELLVGARRDATAIRERAEELRDRITGEIeelheRARRESAEQMKSAGERCDALVKAAEEQLaEAEAK 1173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115527082 1361 LQRAMSKANSEVAQWRtkyeTDAIQRTEEL-EEAKKKLAQRLQDAEE-HVEAVNAKCASLEKTKQRLQNEV---EDLMID 1435
Cdd:NF041483 1174 AKELVSDANSEASKVR----IAAVKKAEGLlKEAEQKKAELVREAEKiKAEAEAEAKRTVEEGKRELDVLVrrrEDINAE 1249
|
330
....*....|..
gi 115527082 1436 VERTNAACAALD 1447
Cdd:NF041483 1250 ISRVQDVLEALE 1261
|
|
| |
